MBP antibody | 12
Rat anti MBP antibody, clone 12 (MCA409S) used to identify rat oligodendrocyte progenitors in vitro by immunofluorescence.
Image caption:
Protandim promotes differentiation of primary rat OPCs under oxidative stress. After 2 day de-differentiation of OLs with growth factors bFGF-2 and PDGF-AA, primary rat OPCs were incubated with 30 μg/mL Protandim or vehicle control (EtOH) for 24 h. After removal of medium, cells were subsequently exposed to either control medium or medium with 10 μM tert-butyl hydrogen peroxide (tbH2O2) for 5 days. MBP and Olig2 expression were assayed by immunocytochemistry. Data are presented as percentage of control and expressed as the mean ± SEM of 3 independent experiments. Statistics reflect student's t-test, one-tailed; * p<0.05.
From: Lim JL, van der Pol SM, Baron W, McCord JM, de Vries HE, van Horssen J.
Protandim Protects Oligodendrocytes against an Oxidative Insult.
Antioxidants (Basel). 2016 Sep 7;5(3). pii: E30.
This is an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used to identify rat oligodendrocyte progenitors in vitro by immunofluorescence.
Image caption:
Protandim marginally promotes differentiation of primary rat OPCs in the presence of TNF. After 2 days of de-differentiation, primary rat OPCs were incubated with 30 μg/mL Protandim or vehicle control (EtOH) for 24 h. After removal of medium, cells were subsequently exposed to either control medium or medium with 10 ng/mL TNF for 5 days. MBP and Olig2 expression were assayed by immunocytochemistry. Data are presented as percentage of control and expressed as the mean ± SEM of 3 independent experiments. Statistics reflect student's t-test, one-tailed;*p<0.05.
From: Lim JL, van der Pol SM, Baron W, McCord JM, de Vries HE, van Horssen J.
Protandim Protects Oligodendrocytes against an Oxidative Insult.
Antioxidants (Basel). 2016 Sep 7;5(3). pii: E30.
This is an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of Myelin basic protein in murine myelinating cell cultures using immunofluorescence.
Image caption:
In vitro time-lapse imaging of cyto-GFP labelled OPC-like cells in shiverer myelinating cultures reveal dynamic cellular interactions. Neurospheres expressing cyto-GFP under the β-actin promoter were added to myelinating cultures prepared from shiverer embryos on DIV 13 and visualised on DIV 17 over 24 hours in 4 min intervals, using a Nikon TE2000 time-lapse microscope (40×, 0.75NA short distance working lens) with perfect focus. A–I) Images captured from a time-lapse sequence illustrate cells with morphology typical of oligodendrocyte progenitor cells (OPCs). Spirals of processes appear over the neurites. Both the cell soma and processes are highly motile, continually moving along the neurites. Processes appear to move over the nerve bundles (arrows and asterisk). J) Manual tracking of the cell bodies of the entire video illustrates the pathway of the putative OPC-like cells (asterisks green and blue) over time, demonstrating their highly motile behaviour. K) A sister culture was immunostained for myelin (PLP/DM20; green) and neurites/axons (SMI-31; red) on DIV 27, demonstrating that the added cyto-GFP neurospheres myelinated the axons.
From: Ioannidou K, Anderson KI, Strachan D, Edgar JM, Barnett SC (2012) Time-Lapse Imaging of the Dynamics of CNS Glial-Axonal Interactions In Vitro and Ex Vivo.
PLoS ONE 7(1): e30775.
This is an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of Myelin basic protein in murine myelinating cell cultures using immunofluorescence.
Image caption:
Time-lapse imaging of fluorescently labelled cells in association with neurites in vitro. A–E) Myelinating cultures generated from a mix of wild type/beta-actin mice were visualised using time-lapse microscopy (Nikon TE2000 (60×, 0.75NA) over 16 hr in 5 min intervals on DIV 27 after the addition of wild type neurospheres previously infected with lentivirus carrying dsRed/GFP gene and addition of cyto-GFP cells. Two cell types were followed over time, one that expressed DS red/cyto-GFP and the other cyto-GFP. A–E) Strongly positive green cells typical of cyto-GFP morphologically resembled oligodendrocytes in contact with neurite bundles. The membrane appears to ruffle and form flaps/bubbles (arrow). In addition, the soma changes its location with respect to the neurite processes, over time, by moving closer to the neurite bundle. C–E) Dynamic imaging over 7.5 hours of a dsred/GFP labelled cell (asterisk) which was engulfed by a cell resembling a microglial cell (yellow arrow). This fluorescence was very much weaker than the cells generated from the beta-actin cyto-GFP mouse. Time frames obtained with 40× magnification (long distance working lens) and without perfect focus.
From: Ioannidou K, Anderson KI, Strachan D, Edgar JM, Barnett SC (2012) Time-Lapse Imaging of the Dynamics of CNS Glial-Axonal Interactions In Vitro and Ex Vivo.
PLoS ONE 7(1): e30775.
This is an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of Myelin basic protein in murine myelinating cell cultures using immunofluorescence.
Image caption:
Time-lapse imaging of the putative assembly of myelin membrane. A) Neurospheres expressing farns-GFP were added to shiverer myelinating cultures on DIV 19 and time-lapse imaging (Nikon TE2000) was performed on 29 DIV, over 24 hr with 4 min time intervals. Ai–iv) Magnified view of the inset in A illustrates a farns-GFP process looping around a presumptive neurite and forming a membranous protrusions or ‘bubble’ (yellow arrow head). This membrane bubble appears to moves along the neurite over time. See Video S3. B) The cells from the Petri dish imaged with confocal microscopy were immunostained with anti-GFP and anti-MBP to confirm differentiation of cyto-GFP labelled oligodendrocytes.C–F) Time-lapse sequence of the same culture for a period of 30 hours, with 3 min time interval, on 24 DIV revealed membrane cuffs (arrowheads) extending and joining up over a neurite. After about 13 hours, the farns-GFP-positive cuffs were observed to form a single, united thick membrane sheath over a neurite. G) Manual tracking of the pathway of a weakly GFP-positive cell which was possibly associated with the membranous fragments.
From: Ioannidou K, Anderson KI, Strachan D, Edgar JM, Barnett SC (2012) Time-Lapse Imaging of the Dynamics of CNS Glial-Axonal Interactions In Vitro and Ex Vivo.
PLoS ONE 7(1): e30775.
This is an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of Myelin basic protein in murine myelinating cell cultures using immunofluorescence.
Image caption:
Time-lapse imaging of the elongation of a putative farns-GFP labelled myelin-like sheath. Neurospheres expressing farns-GFP were added to shiverer myelinating cultures on 19 DIV and time-lapse imaging (Nikon TE2000) performed on 26 DIV, for a period of 14 hr with 4 min time interval. Ai–iii) A farns-GFP process increases in length by 10 μm, over the time course. Membranous protrusions were seen (yellow arrowhead) in addition to the cell body of the farns-GFP labelled oligodendrocyte-like cell (yellow arrow). B) MBP staining of cells in the Petri dish using a Zeiss 710 (×63, 1.4NA) after imaging confirms that farns-GFP expressing cells belong to the oligodendroglial lineage.
From: Ioannidou K, Anderson KI, Strachan D, Edgar JM, Barnett SC (2012) Time-Lapse Imaging of the Dynamics of CNS Glial-Axonal Interactions In Vitro and Ex Vivo.
PLoS ONE 7(1): e30775.
This is an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of Myelin basic protein in murine myelinating cell cultures using immunofluorescence.
Image caption:
Immunohistochemistry of transplanted neurospheres demonstrate that cyto-GFP labelled cells form early and mature myelinating oligodendrocytes. Cyto-GFP-expressing neurospheres were transplanted into a shiverer mouse 3, 7 or 15 days post-transplantation, and 10 µm thick frozen sections were cut and immunolabelled with antibodies to GFP and MBP. Low magnification image of a dorso-vental section of spinal cord, 15 days post-transplantation showing GFP (A) and MBP (B) immunostaining. Transplanted cells were located in both grey and white matter (dorsal columns are delineated by the dotted lines) and expressed MBP-positive myelin sheaths. C) A pre-myelinating cell in which multiple fine GFP positive processes emanate from a central cell body. The soma is also lightly stained with MBP, confirming the identity of the cell as that of the oligodendroglial lineage. MBP-positive myelin sheaths, belonging to a second cell are seen in the bottom left hand corner of the images. D) An early myelinating cell in which short MBP-positive profiles are present at the periphery of the GFP-positive soma. All images were obtained using epifluorescence Olympus microscope (FV10 ASW). Representative images from at least 30 separate experiments.
From: Ioannidou K, Anderson KI, Strachan D, Edgar JM, Barnett SC (2012) Time-Lapse Imaging of the Dynamics of CNS Glial-Axonal Interactions In Vitro and Ex Vivo.
PLoS ONE 7(1): e30775<
This is an open access article distributed under the terms of the Creative Commons Attribution License./a>.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of Myelin basic protein in murine spinal cord using immunofluorescence.
Image caption:
Confocal images of transplanted cyto-GFP expressing cells in the shiverer spinal cord. Four weeks after transplantation of cyto-GFP expressing neurospheres, fixed sections of the shiverer spinal cord were immunolabelled for MBP (red) and GFP (green). A) A cyto-GFP labelled cell appears to extend spirals of cytoplasm around an MBP-positive myelin-like sheath (yellow arrows). Below the cell body, cyto-GFP is seen at the lateral edges (in relation to the long axis of the sheaths, white arrow) of adjacent sheaths and probably represents the cytoplasm filled paranodal loops on either side of the node of Ranvier (asterisks). B) Schematic of visualisation of the sections in C and D. Ci–ii and Di–ii) Spiral of GFP cytoplasm was followed by focussing up and down through the plane of view where they crossed up, traversed the axonal surface, then crossed down again representing the looping as shown in the schematic in B. E–G) 3D reconstruction of cyto-GFP structures (E), illustrates cyto-GFP either side of a space typical of a node of Ranvier (white arrows). F) is a tilted perspective of E) and shows the cyto-GFP form complete rings (white arrows representing the same position in E), consistent with the morphology of paranodal loops. I) Asymmetric caspr positive structures in association with cyto-GFP, at either side of a heminode. On the left, caspr forms a single vertical line and co-localises with cyto-GFP from the myelinating cell. On the right, caspr appears like a loose coil, consistent with its pattern of expression in non-myelinated axons. All images were acquired using an Olympus FV1000 confocal microscope (×60, 1.35NA). Representative images from at least 10 separate experiments.
From: Ioannidou K, Anderson KI, Strachan D, Edgar JM, Barnett SC (2012) Time-Lapse Imaging of the Dynamics of CNS Glial-Axonal Interactions In Vitro and Ex Vivo.
PLoS ONE 7(1): e30775.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the evaluation of myelin basic protein expression in mouse brain lysates by western blotting
Image caption:
MBP and sncRNA715 Expression in Schwann cells. A, Reverse transcription PCR (RT-PCR) on RNA extracted from Oli-neu or IMS32 cells using Mbp-specific primers. The 88nt long amplicon for Mbp was visualized in an ethidium bromide-stained 4% agarose gel. B, Western Blots of lysates from P18 mouse brain (brain lysate), primary oligodendrocytes (pOL, 7DIV), IMS32 and Oli-neu cells using MBP and GAPDH (loading control) specific antibodies. C, Reverse transcription PCR (RT-PCR) on RNA extracted from Oli-neu or IMS32 cells using a sncRNA715-specific primer assays. PCR products (~60-nt long due to the use of hairpin primers in the RT reaction) were visualized in an ethidium bromide stained 4% agarose gel. D, Northern Blots with RNA from IMS32 and undifferentiated primary Schwann cells (pSC) shows expression of sncRNA715 in IMS32 and a lower expression in pSC. Synthetic sncRNA715 (715-mimic) and U6 snRNA were used as positive control and loading control, respectively. E, RT-PCR on RNA from IMS32 and undifferentiated pSC confirms lower expression of sncRNA715 in pSC compared to IMS32 cells shown in D. 715-mimic was used as positive control and snoRNA135 as loading control.
From: Müller C, Hochhaus NM, Fontana X, Luhmann HJ, White R (2015) SncRNA715 Inhibits Schwann Cell Myelin Basic Protein Synthesis.
PLoS ONE 10(8): e0136900.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the evaluation of myelin basic protein expression in mouse Schwann cells using immunofluorescence and western blotting
Image caption:
Inverse correlation of MBP and sncRNA715 in primary Schwann cells. A, Primary Schwann cells derived from sciatic nerves of P3 Wistar rats were cultured in non-differentiating (untreated) or differentiating (+NRG1 +dbcAMP) conditions. MBP protein can only be detected by immunocytochemistry in differentiated Schwann cells. Scale bar represents 50μm. B, Western Blots of undifferentiated and differentiated primary Schwann cells show MBP protein only present in differentiated Schwann cells. CNP is expressed in both maturation stages of primary Schwann cells. GAPDH serves as loading control. C, MBP and sncRNA715-specific RT-PCR on RNA extracted from undifferentiated or differentiated primary Schwann cells. Mbp mRNA is present at both differentiation states while sncRNA715 is detectable in undifferentiated and hardly in differentiated Schwann cells. SnoRNA135 and G6pdh mRNA were used as loading controls.
From: Müller C, Hochhaus NM, Fontana X, Luhmann HJ, White R (2015) SncRNA715 Inhibits Schwann Cell Myelin Basic Protein Synthesis.
PLoS ONE 10(8): e0136900.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the evaluation of myelin basic protein expression in mouse sciatic nerve lysates by western blotting
Image caption:
Inverse correlation of MBP and sncRNA715 in the sciatic nerve. A&B, The sciatic nerve was lysed from mice at postnatal day 1, 4 and 9 and myelin proteins as well as sncRNA715 expression was analyzed by Western blotting (A) and qPCR (B), respectively. MBP and CNP Western blots show increasing levels in differentiating sciatic nerves (A) while sncRNA715 levels decrease during differentiation, P-values P4: 0,0313, P9: 0,0313 (B, log2 values are plotted, sncRNA715 levels at P4 and P9 were quantified relative to P1 using snoRNA135 as a reference gene). Number of experiments (n) are indicated and bar graphs represent mean values ± s.e.m. (Wilcoxon signed-rank test, *P< 0.05, GraphPad Prism5 was used for statistical analysis).
From: Müller C, Hochhaus NM, Fontana X, Luhmann HJ, White R (2015) SncRNA715 Inhibits Schwann Cell Myelin Basic Protein Synthesis.
PLoS ONE 10(8): e0136900.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the evaluation of myelin basic protein expression in mouse Schwann cell lysates by western blotting
Image caption:
Regulation of MBP levels by sncRNA715. Rat primary Schwann cells were differentiated as described and transfected with synthetic sncRNA715 (715-mimic) or control siRNA (c-siRNA). A, Representative Western Blots for MBP and GAPDH showing reduced MBP levels in 715-mimic transfected cells. B, Densitometric analysis of 7 experiments (n = 7) as shown in (A). Normalized MBP/GAPDH values related to control-siRNA transfected cells are plotted. P-value for 715-mimic: 0.0469. Bar graphs represent mean values ± s.e.m. (Wilcoxon signed-rank test, n = 7, *P< 0.05, GraphPad Prism5 was used for statistical analysis).
From: Müller C, Hochhaus NM, Fontana X, Luhmann HJ, White R (2015) SncRNA715 Inhibits Schwann Cell Myelin Basic Protein Synthesis.
PLoS ONE 10(8): e0136900.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of myelin basic protein by immunofluorescence on formalin fixed, paraffin embedded tissue sections.
Image caption:
Demyelination/remyelination and decreased P0 expression in dKO mice. (A) Electron micrographs of ultrathin cross sections of control, dKO, H1HTZ, H2HTZ, H1KO, and H2KO sciatic nerves, at 8 wk post-tamoxifen, and percentage of demyelinated/remyelinated axons (3 animals per group, at least 700 axons counted per mouse), identifying a demyelination/remyelination phenotype in dKO sciatic nerves. Asterisks indicate demyelinated axons and “M” macrophages. (B) CD68 (green) immunofluorescence in longitudinal cryosections of control and dKO sciatic nerves labeled with DAPI (blue = nuclei) showing increased presence of macrophages in dKO sciatic nerves, consistent with the demyelination phenotype. Arrows indicate macrophages. (C) In situ hybridization (ISH) of P0 on longitudinal cryosections of control and dKO sciatic nerves identifying a reduction of P0 at the transcript level at 5 wk post-tamoxifen, before the onset of demyelination and when macrophages are not present in the nerve. Pictures on the right are magnifications of black boxes depicted on the left. Black arrows show SC nuclei. (D) Western blot of P0 and quantification normalized to GAPDH (loading control) in sciatic nerve lysates of control and dKO mice at 8 wk post-tamoxifen (3 mice per group), showing reduced P0 protein levels in dKO sciatic nerves. (E) Confocal images of MBP (magenta) and P0 (red) coimmunofluorescence in paraffin cross sections of dKO mice at 8 wk post-tamoxifen, showing reduced P0 levels in most myelin rings, while MBP levels remain high. Nuclei are labeled in blue by DAPI. A single optical section is shown. White arrows indicate MBP positive/P0 negative myelin rings, the yellow arrowhead shows an MBP/P0 double negative SC, and blue arrowheads MBP/P0 double positive myelin rings. Three animals per group were used for each experiment. P-values (two-tailed unpaired (A) or paired (D) Student's t test): * = p < 0.05, ** = p < 0.01, *** = p < 0.001, error bars = SEM.
From: Brügger V, Engler S, Pereira JA, Ruff S, Horn M, Welzl H, et al. (2015)
HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol 13(9): e1002258.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of myelin basic protein by immunofluorescence.
Image caption:
P0 rescues myelination, Caspr, and neurofascins in plp-dKO DRG cultures. Confocal coimmunofluorescence images of (A) MBP (red) and neurofilament (NF, green), or (C) P0 (red) and MBP (green), or (D) Caspr (red), total neurofascins (NFasc, green), and MBP (white), or (F) MBP (red), NF (white), and either GFP, P0, or Myc (green), or (H) Caspr (red) and NFasc186 (false-colored green) in myelinated control and plp-dKO DRG cultures with (A,C,D,F,H) or without (A) tamoxifen. Briefly, A–D demonstrate demyelination, loss of P0 and paranodal/nodal defects in plp-dKO DRG cultures, mimicking the in vivo phenotype of dKO sciatic nerves. In (F,H), plp-dKO DRG cultures were transduced with doxycycline-inducible lentiviruses expressing either GFP, P0, or P0-myc. (B,G) Quantification of MBP fluorescence intensity normalized to NF. (E,I) Percentage of intact nodes/paranodes expressing Caspr and high levels of NFasc. F–I show that exogenously delivered P0 significantly rescues demyelination and paranodal/ nodal defects of plp-dKO DRG cultures. In (C), white arrows indicate MBP positive/P0 negative fibers, and magenta arrowheads MBP/P0 double positive fibers. Merges MBP/P0 (C) or Caspr/NFasc (D) appear yellow. In (D), dashed lines delineate the paranodal region. In (H), control and plp-dKO were transduced with lentiviruses expressing GFP, and plp-dKO + P0 with lentiviruses expressing P0 (white). Z-series projections (A,C,F) and single optical sections (D,H) are shown. In (D,H), arrows indicate heminodes or full nodes. Images on the right are magnifications of white boxes depicted on the left images. At least three control and three plp-dKO embryos were used for quantification (average of three coverslips per embryos), representative images are shown. Nuclei are labeled in blue with DAPI. P-values (unpaired [B,E,I] or paired [G] two-tailed Student's t test, unless stated otherwise in the figure): * = p < 0.05, *** = p < 0.001, error bars = SEM.
From: Brügger V, Engler S, Pereira JA, Ruff S, Horn M, Welzl H, et al. (2015) HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol 13(9): e1002258.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of myelin basic protein by immunofluorescence.
Image caption:
In contrast to the S49L P0 mutant, D32G and H52Y P0 mutants rescue myelination of HDAC1/2 plp-dKO DRG but not paranodal/nodal integrity. Coimmunofluorescence of MBP (red) and (A) neurofilament (NF, green), and Myc or GFP fluorescence (blue), or (C) neurofascins (NFasc, green), or (D) Caspr (green) in myelinated HDAC1/2 plp-dKO DRG cultures transduced with lentiviruses expressing either GFP, H52Y-myc, D32G-myc, S49L-myc or P0-myc, and treated with tamoxifen for 10 d after completion of myelination. A–B show that H52Y and D32G but not S49L P0 mutants are able to rescue myelination of plp-dKO DRG cultures, similarly to P0-myc, and C–D show that S49L, but not H52Y or D32G, P0 mutant is able to partially rescue paranodal/nodal defects of plp-dKO DRG cultures. In (C), pictures on the right are magnifications of the white boxes depicted on left images. Arrows indicate paranodes/nodes. In (B), quantification of MBP fluorescence intensity normalized to NF and compared to GFP or P0-myc (set to 1). DRG of six plp-dKO embryos were quantified (three plp-dKO embryos per graph, four coverslips per plp-dKO). In (C,D), DRG of three plp-dKO embryos were analyzed and representative pictures are shown. In (E), the graph represents the percentage of intact (Caspr-positive or high NFasc levels) nodes and heminodes. DRG of three plp-dKO embryos were quantified, four coverslips per plp-dKO, 80 to 300 nodes/heminodes counted per plp-dKO per virus. P-values (paired (B) and unpaired (E) two-tailed (unless stated otherwise in the figure) Student's t test): * = p < 0.05, ** = p < 0.01, error bars = SEM.
From: Brügger V, Engler S, Pereira JA, Ruff S, Horn M, Welzl H, et al. (2015) HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol 13(9): e1002258.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of myelin basic protein by western blotting.
Image caption:
No demyelination and unchanged MBP levels, but decreased P0 levels at 5 wk post-tamoxifen in dKO and at 8 wk post-tamoxifen in H2KO sciatic nerves. (A) Electron micrograph of ultrathin cross sections of dKO sciatic nerve at 5 wk post-tamoxifen. Sciatic nerves of 3 dKO mice were analyzed and no demyelinated or remyelinated axon or macrophage were found. (B–D) Western blot of P0 (B,C) and MBP (D) in control and dKO sciatic nerve lysates at 5 wk post-tamoxifen (B,D), and in control, H1HTZ, H1KO, H2HTZ, and H2KO at 8 wk post-tamoxifen (C), and quantification of protein levels normalized to the loading control GAPDH in mutants compared to controls (= 100%) (3 animals per genotype were used). In (B,D), the dashed lines indicate that lysates were run on the same gel but not on consecutive lanes. P-values (unpaired (B,C,D) or paired (C, HDAC2 single mutants) two-tailed (unless stated otherwise in the figure) Student's t test): * = p < 0.05, error bars = SEM.
From: Brügger V, Engler S, Pereira JA, Ruff S, Horn M, Welzl H, et al. (2015) HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol 13(9): e1002258.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of myelin basic protein by western blotting.
Image caption:
Further characterization of dKO phenotype at the molecular level. Western blots of MBP (A), Sox10 (B), Krox20 (C), MAG (D), and ABC (E) in lysates of control (Co) and dKO sciatic nerves at 8 wk post-tamoxifen, and quantification of protein levels normalized to GAPDH or beta-actin loading control in dKOs compared to controls (= 100%). For each experiment, three control and three dKO animals were used. P-values (paired two-tailed Student's t test): * = p < 0.05, error bars = SEM.
From: Brügger V, Engler S, Pereira JA, Ruff S, Horn M, Welzl H, et al. (2015) HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol 13(9): e1002258.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of murine myelin basic protein by immunofluorescence.
Image caption:
P0-myc rescues neurofascins in plp-dKO DRG cultures. Coimmunofluorescence of total neurofascins (NFasc, green) and MBP (red) in control or plp-dKO myelinated DRG cultures transduced with lentiviruses expressing GFP (Control and plp-dKO) or P0-myc (plp-dKO + P0-myc). Z-series projections of confocal stacks are shown. Images on the right are magnifications of white boxes depicted on the left images highlighting heminodes or nodes. DRG of three control and three plp-dKO embryos were analyzed and representative images are shown.
From: Brügger V, Engler S, Pereira JA, Ruff S, Horn M, Welzl H, et al. (2015) HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol 13(9): e1002258.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of murine myelin basic protein by immunofluorescence .
Image caption:
P0 localization in myelinated fibers of DRG cultures and in human sciatic nerves. (A) Confocal images (z-series projections) of P0 (red) and MBP (green) coimmunofluorescence in myelinated mouse DRG cultures. Overlay appears yellow. DRG cultures of six control embryos were analyzed, and a representative P0-positive fiber is shown. White dashed lines delineate MBP signal that is apparently restricted to internodes, whereas P0 signal extends further between two internodes. Scale bar = 5 μm. (B–C) Coimmunofluorescence of total neurofascins (NFasc, red) and P0 (green) (B) or of NFasc186 (blue), Contactin (red), and P0 (green) (C) on longitudinal cryosections of adult human peripheral nerves. Median, tibial, and/or sciatic nerves of three human individuals were analyzed and representative pictures of sciatic nerves are shown. P0 was abundant in all paranodal/nodal regions we observed. Z-series projections and single optical sections are shown. Asterisks mark the position (lateral dimension) of the node of Ranvier. Scale bars = 5 μm in (B) and 10 μm in (C).
From: Brügger V, Engler S, Pereira JA, Ruff S, Horn M, Welzl H, et al. (2015) HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol 13(9): e1002258.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of murine myelin basic protein by immunofluorescence.
Image caption:
Validation of Myc staining specificity in myelinated plp-dKO DRG cultures efficiently transduced with lentiviruses expressing GFP. Coimmunofluorescence of MBP (Magenta, rat antibody) and Myc (red, mouse antibody), and GFP fluorescence (green) in myelinated plp-dKO DRG cultures transduced with lentiviruses expressing GFP and treated with tamoxifen for 10 d. Even at high exposure, Myc staining did not cross-react with MBP staining. To avoid cross-reactivity, we used multiple labeling (adsorbed against many animal species, including rat for antimouse and mouse for antirat) secondary antimouse and antirat antibodies. Antibody concentrations and staining protocol (buffers, incubation times and temperature, washes) were the same as for stainings presented in Fig 9A. Nuclei are labeled in blue with DAPI. Pictures on the right (single optical sections) are magnifications of the white boxes depicted on left images (z-series projections). Arrows indicate Schwann cell nuclei of myelinated fibers, arrowheads indicate MBP staining. DRG of three plp-dKO embryos were analyzed. None of the MBP-positive fibers were labeled by Myc staining.
From: Brügger V, Engler S, Pereira JA, Ruff S, Horn M, Welzl H, et al. (2015) HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol 13(9): e1002258.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the detection of murine myelin basic protein by immunofluorescence.
Image caption:
No difference of MBP levels or of percentage of intact nodes/heminodes between control DRG cultures transduced with lentiviruses carrying GFP, H52Y, D32G, S49L P0 mutants, or P0-myc. Coimmunofluorescence of MBP (red) and (A) neurofilament (NF, green) and Myc or GFP fluorescence (blue), or (C) neurofascins (NFasc, green), or (D) Caspr (green) in myelinated HDAC1/2 control DRG cultures transduced with lentiviruses expressing either GFP, H52Y-myc, D32G-myc, S49L-myc, or P0-myc, and treated with tamoxifen for 10 d after completion of myelination. Arrows indicate paranodes/nodes. In (B), quantification of MBP fluorescence intensity normalized to NF and compared to GFP (set to 1). DRG of three control embryos were quantified, four coverslips per embryo were analyzed, and representative pictures are shown. In (E), the graph represents the percentage of intact (high NFasc levels) nodes and heminodes. DRG of three control embryos were quantified, four coverslips per control, 40 to 80 nodes/heminodes counted per control per virus. Error bars = SEM.
From: Brügger V, Engler S, Pereira JA, Ruff S, Horn M, Welzl H, et al. (2015) HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol 13(9): e1002258.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBPantibody, clone 12 (MCA409S) used for the evaluation of myelin basic protein expression in mouse brain by immunofluorescence.
Image caption:
Age-dependent loss of MBP and P25α signals in striosomes (patches). a A coronal brain section (6 μm, paraffin embedded) from a 12 month-old A53T α-Syn mouse, stained with anti-MBP antibody. Black square shows area of interest. b Higher magnification of the area of interest from (a) in a consecutive section, double stained with anti-MBP (red) and anti-tyrosine hydroxylase (TH, green) antibodies. Scale bar, 100 μm. c Quantification of MBP signal inside striosomes. Bars represent mean ± SD of n = 4 A53T and control mice at 2, 8 and 12 months of age. *, <0.05, one-way ANOVA. d Quantification of MBP signal in striosomes of Thy-1 α-Syn tg and age-matched control mouse brains determined at 2 and 8 months of age. Bars represent mean ± SD of n = 4 mice. *, &ly;0.05, one-way ANOVA. e Quantification of MBP signal in striosomes of 12 month-old 5XFAD and control mice. f Coronal brain sections containing rostral-dorsal striatum (6 μm, paraffin embedded) of 12 month-old A53T α-Syn mouse and age-matched control immunoreacted with anti-P25α antibody and showing a striosome. Scale bar, 10 μm. g Samples of high-speed supernatant (50 μg protein) obtained from whole Thy-1 α-Syn and control mouse brains at 2 and 10 months of age analyzed by Western blotting and immunoreacted with anti-P25α antibody. h Graph showing quantitation of blots obtained in (G) mean ± SD of n = 4 mice. *, <0.05, one-way ANOVA.
From: Grigoletto J, Pukaß K, Gamliel A, Davidi D, Katz-Brull R, Richter-Landsberg C, Sharon R.
Higher levels of myelin phospholipids in brains of neuronal α-Synuclein transgenic mice precede myelin loss.
Acta Neuropathol Commun. 2017 May 8;5(1):37.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBPantibody, clone 12 (MCA409S) used for the evaluation of myelin basic protein expression in mouse brain by western blotting.
Image caption:
Myelin proteins, membrane flotation and histology. a Western blot showing myelin proteins in preparations of purified myelin from A53T α-Syn and control mouse brains at 4–6 months of age (n = 5–6 mice). b Bars showing mean ± SD of the indicated myelin protein levels, in whole brain protein extracts, of A53T α-Syn at 12–14 months (n = 8–9 mice). Presented as a percent of control age-matched mouse brain, set at 100% (vertical line) *,<0.05, one-way ANOVA. c Flotation assay showing the distribution of detergent-soluble myelin membrane particles into a 8–25% nycodenz gradient. Purified myelin preparations of A53T α-Syn and control mouse brains at 12 months of age, analyzed in parallel. Aliquots of gradient fractions analyzed by Western blotting using the specified antibodies. Representative blot of n = 3. 2', 3'-cyclic nucleotide 3'-phosphodiesterase (CNPase); myelin associated glycoprotein (MAG); myelin basic protein (MBP); myelin oligodendrocyte glycoprotein (MOG); proteolipid protein (PLP). d The caudate nucleus in coronally sectioned human brain hemisphere (100 μm), including striosomes (dark strips) and matrix (light staining) of a 90-year old female without PD (non-PD) and a 68-year-old female PD patient with advanced disease (neuropathological stage 5). Sections were stained for myelin using a modified Pal-Weigert method. Scale bar, 500 μm. Stained brain sections were provided by the Braak laboratory (University of Ulm, Ulm, Germany). e Coronal brain sections (6 μm, paraffin embedded) of A53T α-Syn and control mice at 12 months of age stained with Luxol Fast Blue/Periodic Acid Schiff, showing the corpus callosum (cc) and striatum (st). Scale bar, 500 μm.
From: Grigoletto J, Pukaß K, Gamliel A, Davidi D, Katz-Brull R, Richter-Landsberg C, Sharon R.
Higher levels of myelin phospholipids in brains of neuronal α-Synuclein transgenic mice precede myelin loss.
Acta Neuropathol Commun. 2017 May 8;5(1):37.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBPantibody, clone 12 (MCA409S) used for the evaluation of myelin basic protein expression in mouse oligodendrocytes by immunofluorescence.
Image caption:
Effects of α-Syn on oligodendrocyte differentiation. Oligodendrocyte progenitor cells were either untreated (Co) or incubated with recombinant human (rh)α-Syn (10 μg/ml) 2 h after plating for the indicated time. Cells were subjected to indirect immunofluorescence staining using antibodies against α-tubulin (green) and MBP (red). Nuclei were stained with DAPI (blue). Scale bar: 20 μm.
From: Grigoletto J, Pukaß K, Gamliel A, Davidi D, Katz-Brull R, Richter-Landsberg C, Sharon R.
Higher levels of myelin phospholipids in brains of neuronal α-Synuclein transgenic mice precede myelin loss.
Acta Neuropathol Commun. 2017 May 8;5(1):37.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBPantibody, clone 12 (MCA409S) used for the evaluation of myelin basic protein expression in mouse oligodendrocytes by immunofluorescence and western blotting.
Image caption:
α-Syn impairs oligodendrocyte maturation. Oligodendrocyte progenitor cells were either untreated (Co) or incubated with rh α-Syn (10 μg/ml) 2 h after plating for 3 or 6 days. Cells were subjected to immunocytochemistry using antibodies: a anti-acetylated α-tubulin (green) and anti-MBP (red); b anti-proteoglycan NG-2 (green) and anti-MBP (red). Nuclei were stained with DAPI (blue). Scale bar: 20 μm. c Exogenously applied α-Syn led to an increase in NG-2 and a decrease in MBP levels. Western blot analysis of cell extracts was carried out with antibodies indicated on the right. Numbers on the right indicate molecular weights in kDa.
From: Grigoletto J, Pukaß K, Gamliel A, Davidi D, Katz-Brull R, Richter-Landsberg C, Sharon R.
Higher levels of myelin phospholipids in brains of neuronal α-Synuclein transgenic mice precede myelin loss.
Acta Neuropathol Commun. 2017 May 8;5(1):37.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBPantibody, clone 12 (MCA409S) used for the evaluation of myelin basic protein expression in mouse striatum by immunofluorescence.
Image caption:
Age-dependent accumulation of α-Syn toxicity in the striatum. a Coronal brain sections containing rostral-dorsal striatum (6 μm, paraffin embedded) of A53T α-Syn mouse at 2, 8 and 12 months of age, or control brain section at 12 months old, immunoreacted with anti-α-Syn antibody (syn - 303). Scale bar, 50 μm.
From: Grigoletto J, Pukaß K, Gamliel A, Davidi D, Katz-Brull R, Richter-Landsberg C, Sharon R.
Higher levels of myelin phospholipids in brains of neuronal α-Synuclein transgenic mice precede myelin loss.
Acta Neuropathol Commun. 2017 May 8;5(1):37.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the demonstration of MBP expression in mouse organotypic brain cultures by immunofluorescence.
Image caption:
Methylthioadenosine (MTA) dampens neuroinflammation, and prevents demyelination and axonal loss in mouse cerebellar cultures. A Organotypic cultures were treated with MTA (192 μM) or the placebo for 24 h at seven DIV and thereafter, they were stimulated with LPS (15 μg/ml) for 24 h. Immunofluorescent staining for NFL (red) and MBP (green) was analyzed in the slices, and in time-matched untreated control slices (arrow, axonal swelling; arrowhead, end bulb). Panels a, b and c scale bars: 50 μm. Panels d-i scale bar: μ μm.
From: Moreno, B et al. (2017)
Methylthioadenosine promotes remyelination by inducing oligodendrocyte differentiation.
Multiple Sclerosis and Demyelinating Disorders. 2: 3.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used to evaluate MBP expression in mouse brain by immunofluorescence and western blotting.
Image caption:
Myelination is delayed during postnatal brain development in the mdx mouse model of DMD. a Breeding strategy to generate litters with mdx males and heterozygous mdx/+ females (controls), b dystrophin isoform expression in oligodendrocytes and mdx mice, c western blot analysis of dystrophin protein content in lysates obtained from mdx and control cerebral cortices at postnatal day 8 (p8), p14, p21, 6 weeks, and 2 months. Comparable levels of Dp71 are found in both mdx and control lysates, while Dp427 is absent from mdx lysates. Cortical lysates from wildtype male and female mice (B6, Black 6) reveals that Dp427 and Dp71 levels are similar in males and females. Representative western blots are shown, including those for p115 as a loading control, d MBP immunohistochemistry of mdx and control coronal floating brain sections. Tiled confocal microscopy images reveal less MBP immunoreactivity in mdx cerebral cortices at postnatal day 21 (p21) but not at 2 months, e quantification of mean MBP densitometries from western blots comparing protein lysates from cerebral cortices of control and mdx mice at p14, p21, 6wks and 2 months. In addition, cortical lysates from wildtype mice (B6, Black 6) were analyzed to ensure that MBP levels did not differ by gender. Immunoblots to detect β-actin were used as loading controls. MBP levels in mdx cerebral cortices were decreased at p14, p21, and 6 weeks but were normal by 2 months (*p<0.05), f representative western blots of cortical lysates from postnatal day (p14) and 2 month old (2 mos) mdx and control mice
From: Aranmolate A, Tse N, Colognato H.
Myelination is delayed during postnatal brain development in the mdx mouse model of Duchenne muscular dystrophy.
BMC Neurosci. 2017 Aug 14;18(1):63.
This is from an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the demonstration of MBP expression by cells in the murine corpus callosum by immunofluorescence.
Image caption:
Activin receptor signaling regulates myelin membrane compaction/maturation. a Electron micrographs of myelinated axons in P16 Acvr1bfl/fl and PDGFRa-Cre; Acvr1bfl/fl mice. Scale bars 1 μm. b Average inner tongue thickness per axon diameter per animal in Acvr1bfl/fl (magenta) and PDGFRa-Cre; Acvr1bfl/fl mice (green). n = 3 mice per genotype. c Dot plot of inner tongue thickness per axon diameter for all myelinated axons for all animals, in Acvr1bfl/fl (magenta) and PDGFRa-Cre; Acvr1bfl/fl mice (green). d Myelin thickness versus axon diameter in Acvr1bfl/fl (magenta) and PDGFRa-Cre; Acvr1bfl/fl mice (green). Extra sum of squares F test between slopes, ***P = 0.0014. e Electron micrographs of compact myelin layers in P16 Acvr1bfl/fl and PDGFRa-Cre; Acvr1bfl/fl mice. f Images of myelin basic protein (MBP) in corpus callosum of Acvr1bfl/fl and PDGFRa-Cre; Acvr1bfl/fl mice at P16. Scale bar 25 μm. g MBP intensity in PDGFRa-Cre; Acvr1bfl/fl mice normalized to background and to levels in Acvr1bfl/fl mice. s.e.m. for variance in Acvr1bfl/fl samples indicated. One sample t test against theoretical mean of 1, **P = 0.0097. h Image of PDGFRa-Cre; Acvr1bfl/fl corpus callosum showing MAG+ (green), MBP negative (red) myelin sheaths (arrows). i Percentage of total axonal area (neurofilament (NF)+) co-localizing with compaction marker Caspr in caudal corpus callosum at P16 in Acvr1bfl/fl and PDGFRa-Cre; Acvr1bfl/fl mice. Two-tailed Student's t test, **P = 0.0038, n = 2–4 mice per group. Inset example of Caspr clusters (green) at paranodes along axon (NF+; purple) (arrow). j Images of cultured mature oligodendrocytes treated with vehicle control or activin-A (10 ng ml−1) stained with Phalloidin-Alexa-568 (red) and MBP (green). Scale bar 20 μm. k Phalloidin intensity (arbitrary units; A.U.) in MBP+ sheets of mature oligodendrocytes plotted against oligodendrocyte size (pixels squared; px2) in control (magenta) or activin-A (10 ng ml−1) treated (green) conditions
From: Dillenburg A, Ireland G, Holloway RK, Davies CL, Evans FL, Swire M, Bechler ME, Soong D, Yuen TJ, Su GH, Becher JC, Smith C, Williams A, Miron VE.
Activin receptors regulate the oligodendrocyte lineage in health and disease.
Acta Neuropathol. 2018 Feb 3 [Epub ahead of print].
This is an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the demonstration of MBP expression by cells in the murine corpus callosum by immunofluorescence.
Image caption:
Activin receptor signaling regulates myelin membrane compaction/maturation. a Electron micrographs of myelinated axons in P16 Acvr1bfl/fl and PDGFRa-Cre; Acvr1bfl/fl mice. Scale bars 1 μm. b Average inner tongue thickness per axon diameter per animal in Acvr1bfl/fl (magenta) and PDGFRa-Cre; Acvr1bfl/fl mice (green). n = 3 mice per genotype. c Dot plot of inner tongue thickness per axon diameter for all myelinated axons for all animals, in Acvr1bfl/fl (magenta) and PDGFRa-Cre; Acvr1bfl/fl mice (green). d Myelin thickness versus axon diameter in Acvr1bfl/fl (magenta) and PDGFRa-Cre; Acvr1bfl/fl mice (green). Extra sum of squares F test between slopes, ***P = 0.0014. e Electron micrographs of compact myelin layers in P16 Acvr1bfl/fl and PDGFRa-Cre; Acvr1bfl/fl mice. f Images of myelin basic protein (MBP) in corpus callosum of Acvr1bfl/fl and PDGFRa-Cre; Acvr1bfl/fl mice at P16. Scale bar 25 μm. g MBP intensity in PDGFRa-Cre; Acvr1bfl/fl mice normalized to background and to levels in Acvr1bfl/fl mice. s.e.m. for variance in Acvr1bfl/fl samples indicated. One sample t test against theoretical mean of 1, **P = 0.0097. h Image of PDGFRa-Cre; Acvr1bfl/fl corpus callosum showing MAG+ (green), MBP negative (red) myelin sheaths (arrows). i Percentage of total axonal area (neurofilament (NF)+) co-localizing with compaction marker Caspr in caudal corpus callosum at P16 in Acvr1bfl/fl and PDGFRa-Cre; Acvr1bfl/fl mice. Two-tailed Student's t test, **P = 0.0038, n = 2–4 mice per group. Inset example of Caspr clusters (green) at paranodes along axon (NF+; purple) (arrow). j Images of cultured mature oligodendrocytes treated with vehicle control or activin-A (10 ng ml−1) stained with Phalloidin-Alexa-568 (red) and MBP (green). Scale bar 20 μm. k Phalloidin intensity (arbitrary units; A.U.) in MBP+ sheets of mature oligodendrocytes plotted against oligodendrocyte size (pixels squared; px2) in control (magenta) or activin-A (10 ng ml−1) treated (green) conditions
From: Dillenburg A, Ireland G, Holloway RK, Davies CL, Evans FL, Swire M, Bechler ME, Soong D, Yuen TJ, Su GH, Becher JC, Smith C, Williams A, Miron VE.
Activin receptors regulate the oligodendrocyte lineage in health and disease.
Acta Neuropathol. 2018 Feb 3 [Epub ahead of print].
This is an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 (MCA409S) used for the demonstration of MBP expression by cells in organotypic cerebellar slice cultures by immunofluorescence.
Image caption:
Activin receptor signaling regulates remyelination. a Representative images of organotypic cerebellar slice cultures at 7 days post lysolecithin-induced demyelination, treated with vehicle control or activin receptor agonist activin-A during remyelination, immunostained against myelin basic protein (MBP; green), and axonal neurofilament-H (NF; red). Scale bar 50 μm. b Mean remyelination index ± s.e.m. in activin-A-treated explants at 7, 10, and 14 days post lysolecithin (dpl) normalized to vehicle control from the respective time point. n = 3 animals, one-sample t test compared to theoretical mean of 1 (control), **P = 0.0057. c Representative images of slice cultures at 14 dpl treated with vehicle control or an inhibitor of activin receptor signaling inhibin-A during remyelination, immunostained against myelin basic protein (MBP; green) and axonal neurofilament-H (NF; red). Scale bar 50 μm.
From: Dillenburg A, Ireland G, Holloway RK, Davies CL, Evans FL, Swire M, Bechler ME, Soong D, Yuen TJ, Su GH, Becher JC, Smith C, Williams A, Miron VE.
Activin receptors regulate the oligodendrocyte lineage in health and disease.
Acta Neuropathol. 2018 Feb 3 [Epub ahead of print].
This is an open access article distributed under the terms of the Creative Commons Attribution License.
Rat anti MBP antibody, clone 12 recognizes myelin basic protein from a wide range of species. The antibody reacts weakly with peptides ending in the Phe 91 where the 91-92 Phe-Phe bond is broken. Synthetic peptide 82-99 reacts very well, as does intact MBP. Further epitope analysis indicates binding to a region defined by amino acids 82-87 (DENPVV).
Rat anti MBP antibody, clone 12 has been reported as being suitable for use in Western blotting (Glynn et al. 1987).
Rat anti MBP antibody, clone 12 has been reported as being suitable for use in Western blotting (Glynn et al. 1987).
Product Details
- Target Species
- Bovine
- Species Cross-Reactivity
-
Target Species Cross Reactivity Mouse Rabbit Mammals Rat Guinea Pig Sheep Human Chicken Pig - N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Tissue Culture Supernatant - liquid
- Buffer Solution
- 0.1M TRIS
- Preservative Stabilisers
0.1% Sodium Azide - Immunogen
- Bovine MBP.
- Fusion Partners
- Spleen cells from an immunised outbred rat were fused with cells of the mouse NS0 myeloma cell line.
Storage Information
- Storage
- Store at +4oC or at -20oC if preferred.
This product should be stored undiluted.
Storage in frost free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use. - Guarantee
- 18 months from date of despatch.
More Information
- UniProt
- P02687 Related reagents
- Entrez Gene
- MBP Related reagents
- GO Terms
- GO:0005886 plasma membrane
- GO:0005515 protein binding
- GO:0019911 structural constituent of myelin sheath
- GO:0043209 myelin sheath
- Regulatory
- For research purposes only
Applications of MBP antibody
| Application Name | Verified | Min Dilution | Max Dilution |
|---|---|---|---|
| ELISA | |||
| Immunofluorescence | |||
| Radioimmunoassays | |||
| Western Blotting |
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.
Copyright © 2019 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
| Description | Product Code | Pack Size | Applications | List Price | Quantity |
|---|---|---|---|---|---|
| Goat anti Rat IgG:Alk. Phos. (Mouse Adsorbed) | STAR131A | 1 ml | C E P WB | ||
| Goat anti Rat IgG:Biotin (Mouse Adsorbed) | STAR131B | 0.5 mg | C E IF P WB | ||
| Rabbit F(ab')2 anti Rat IgG:Dylight®800 | STAR16D800GA | 0.1 mg | F IF WB | ||
| Rabbit F(ab')2 anti Rat IgG:FITC | STAR17B | 1 mg | F | ||
| Rabbit F(ab')2 anti Rat IgG:HRP | STAR21B | 1 mg | C E P RE | ||
| Goat F(ab')2 anti Rat IgG:FITC (Mouse Adsorbed) | STAR69 | 0.5 ml | F | ||
| Goat anti Rat IgG:Dylight®800 (Mouse Adsorbed) | STAR71D800GA | 0.1 mg | F IF WB | ||
| Goat anti Rat IgG:HRP (Mouse Adsorbed) | STAR72 | 0.5 mg | C E P | ||
| Goat F(ab')2 anti Rat IgG:RPE (Mouse Adsorbed) | STAR73 | 0.5 ml | F |
Product Specific References
References for MBP antibody
-
Groome, N.P. et al. (1986) Region-specific immunoassays for human myelin basic protein.
J Neuroimmunol. 12 (4): 253-64. -
Glynn, P. et al. (1987) Basic protein dissociating from myelin membranes at physiological ionic strength and pH is cleaved into three major fragments.
J Neurochem. 48 (3): 752-9. -
Hruby, S. et al. (1987) Monoclonal antibodies reactive with myelin basic protein.
Mol Immunol. 24 (12): 1359-64. -
Homchaudhuri L et al. (2009) Influence of membrane surface charge and post-translational modifications to myelin basic protein on its ability to tether the Fyn-SH3 domain to a membrane in vitro.
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Pohl, H.B. et al. (2011) Genetically induced adult oligodendrocyte cell death is associated with poor myelin clearance, reduced remyelination, and axonal damage.
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Laursen, L.S. et al. (2011) Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K.
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Müller, C. et al. (2015) SncRNA715 Inhibits Schwann Cell Myelin Basic Protein Synthesis.
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Brügger V et al. (2015) HDAC1/2-Dependent P0 Expression Maintains Paranodal and Nodal Integrity Independently of Myelin Stability through Interactions with Neurofascins.
PLoS Biol. 13 (9): e1002258. -
Natrajan, M.S. et al. (2015) Retinoid X receptor activation reverses age-related deficiencies in myelin debris phagocytosis and remyelination.
Brain. 138(Pt 12):3581-97 -
Fernandes, A.R. & Chari, D.M. (2016) Part I: Minicircle vector technology limits DNA size restrictions on ex vivo gene delivery using nanoparticle vectors: Overcoming a translational barrier in neural stem cell therapy.
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Friess, M. et al. (2016) Intracellular ion signaling influences myelin basic protein synthesis in oligodendrocyte precursor cells.
Cell Calcium. Jun 29. pii: S0143-4160(16)30100-2. [Epub ahead of print] -
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Crawford, A.H. et al. (2016) Pre-Existing Mature Oligodendrocytes Do Not Contribute to Remyelination following Toxin-Induced Spinal Cord Demyelination.
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Lim, J.L. et al. (2016) Protandim Protects Oligodendrocytes against an Oxidative Insult.
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Grigoletto, J. et al. (2017) Higher levels of myelin phospholipids in brains of neuronal α-Synuclein transgenic mice precede myelin loss.
Acta Neuropathol Commun. 5 (1): 37. -
Moreno, B. et al. (2017) Methylthioadenosine promotes remyelination by inducing oligodendrocyte differentiation
Multiple Sclerosis Demyelinating Disorders. 2 (1): . -
Qin, J. et al. (2017) GD1a Overcomes Inhibition of Myelination by Fibronectin via Activation of Protein Kinase A: Implications for Multiple Sclerosis.
J Neurosci. 37 (41): 9925-38. -
Aranmolate, A. et al. (2017) Myelination is delayed during postnatal brain development in the mdx mouse model of Duchenne muscular dystrophy.
BMC Neurosci. 18 (1): 63. -
Yu, Q. et al. (2017) Strain differences in cuprizone induced demyelination.
Cell Biosci. 7: 59. -
Dillenburg, A. et al. (2018) Activin receptors regulate the oligodendrocyte lineage in health and disease.
Acta Neuropathol. Feb 03 [Epub ahead of print]. -
Sekizar, S. & Williams, A. (2019) Ex Vivo Slice Cultures to Study Myelination, Demyelination, and Remyelination in Mouse Brain and Spinal Cord.
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Martinez-rachadell, L. et al. (2019) Cell-specific expression of insulin/insulin-like growth factor-I receptor hybrids in the mouse brain.
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