Myelin Proteolipid Protein antibody | plpc1
PLP encodes the major protein components of compact CNS myelin and mutations in the PLP gene can lead to severe dysmyelinating disease (Hudson et al. 1989).
Mouse anti myelin proteolipid protein, clone plpc1 has proved a useful immunohistochemical tool for the study of central nervous system injury in patients with multiple sclerosis (Seewan et al. 2011, Huizinga et al. 2011)
- Target Species
- Species Cross-Reactivity
Target Species Cross Reactivity Human Tenerife lizard (Gallotia galloti)
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
0.09% Sodium Azide
- Synthetic peptide GRGTKF corresponding to C terminal region of myelin proteolipid protein.
- Approx. Protein Concentrations
- IgG concentration 1 mg/ml
- Fusion Partners
- Spleen cells from immunised BALB/c mice were fused with cells of the mouse SP2/0 myeloma cell line.
- 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.
- 12 months from date of despatch
- Entrez Gene
- GO Terms
- GO:0016021 integral to membrane
- For research purposes only
Applications of Myelin Proteolipid Protein antibody
|Application Name||Verified||Min Dilution||Max Dilution|
|Immunohistology - Frozen|
|Immunohistology - Paraffin|
Secondary Antibodies Available
Negative Isotype Controls Available
|Description||Product Code||Applications||Pack Size||List Price||Quantity|
|Mouse IgG2a Negative Control||MCA929||F||100 Tests|
Application Based External Images
Immunohistology - Frozen
Immunohistology - Paraffin
Product Specific References
References for Myelin Proteolipid Protein antibody
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Moharregh-Khiabani, D. et al. (2010) Effects of fumaric acids on cuprizone induced central nervous system de- and remyelination in the mouse.
PLoS One. 5:e11769.
Bramow, S. et al. (2010) Demyelination versus remyelination in progressive multiple sclerosis.
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Jaśkiewicz, E. et al. (2005) Expression of recombinant forms of human 21.5 kDa myelin basic protein and proteolipid protein in CHO cells.
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Coulpier, F. et al. (2010) CNS/PNS boundary transgression by central glia in the absence of Schwann cells or Krox20/Egr2 function.
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Haider, L. et al. (2011) Oxidative damage in multiple sclerosis lesions.
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Geurts, J.J. et al. (2007) Extensive hippocampal demyelination in multiple sclerosis.
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Kooi, E.J. et al. (2011) Cholinergic imbalance in the multiple sclerosis hippocampus.
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van Horssen, J. et al. (2006) NAD(P)H:quinone oxidoreductase 1 expression in multiple sclerosis lesions.
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van Horssen, J. et al. (2010) Nrf2 and DJ1 are consistently upregulated in inflammatory multiple sclerosis lesions.
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Janssen, K. et al. (2016) Absence of CCL2 and CCL3 Ameliorates Central Nervous System Grey Matter But Not White Matter Demyelination in the Presence of an Intact Blood-Brain Barrier.
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van Horssen, J. et al. (2012) Clusters of activated microglia in normal-appearing white matter show signs of innate immune activation.
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Maccarrone, G. et al. (2016) MALDI imaging mass spectrometry analysis-A new approach for protein mapping in multiple sclerosis brain lesions.
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van Horssen, J. et al. (2016) Human endogenous retrovirus W in brain lesions: Rationale for targeted therapy in multiple sclerosis.
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Shakhbazau, A. et al. (2016) Demyelination induces transport of ribosome-containing vesicles from glia to axons: evidence from animal models and MS patient brains.
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Clarner, T. et al. (2015) CXCL10 triggers early microglial activation in the cuprizone model.
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Nakajima, M. et al. (2016) Auraptene induces oligodendrocyte lineage precursor cells in a cuprizone-induced animal model of demyelination.
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