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Nerve Growth Factor 2.5S

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Purified Mouse Nerve Growth Factor 2.5S thumbnail image 1 Purified Mouse Nerve Growth Factor 2.5S thumbnail image 2
Purified Mouse Nerve Growth Factor 2.5S gallery image 1
Published customer image:
Mouse Nerve Growth Factor 2.5S (PMP04Z) used in vitro to stimulate the differentiation of PC12 cells.
Image caption:
SB203580 increases lysosomal localization and degradation of αSyn and modulates lysosomal distribution and function.
A, NGF-differentiated PC12-αSyn/p25α cells were treated with 1 μM SB203580 and protease inhibitors E64 (10 μM) and LP (50/67 μg/ml, respectively) for 2 days before indirect immunofluorescence to reveal αSyn (LB509 mAb) and LAMP-1. Note increased localization of αSyn in LAMP1-positive compartments in SB203580-treated cells (arrows). The images are representative of two independent experiments. Bar represents 10 μm.
B, NGF-differentiated PC12-αSyn/p25α cells were cultured 2 days with or without 1 μM SB203580 before homogenization and fractionation of equal protein loads by sucrose gradient centrifugation. Collected fractions were analyzed by Western blotting for αSyn, cathepsin D, and LC3. Note the increased distribution of &apha;Syn and cathepsin D in heavy lysosomal fractions in SB203580-treated cells. The bands in the LC3 blot represent LC3-I (upper band) and LC3-II (lower band). The shown blots are representative of two independent experiments.br>
From: Borland H, Rasmussen I, Bjerregaard-Andersen K, Rasmussen M, Olsen A, Vilhardt F.
α-synuclein buildup is alleviated via ESCRT-dependent endosomal degradation brought about by p38MAPK inhibition in cells expressing p25α.
J Biol Chem. 2022 Nov;298(11):102531.
doi: 10.1016/j.jbc.2022.102531.
This image is from an open access article distributed under terms of a Creative Commons Attribution License.
Purified Mouse Nerve Growth Factor 2.5S gallery image 2
Published customer image:
Mouse Nerve Growth Factor 2.5S (PMP04Z) used in vitro to stimulate the differentiation of PC12 cells.
Image caption:
SB203580 increases lysosomal localization and degradation of αSyn and modulates lysosomal distribution and function.
NGF-differentiated PC12-αSyn/p25α cells stably expressing LAMP1-GFP were treated for 2 days with 1 μM SB203580 before fixation and indirect immunofluorescence with rabbit anti-LAMP1 antibody followed by Alexa488-conjugated goat anti-rabbit antibodies. Bars represent 10 μm.

From: Borland H, Rasmussen I, Bjerregaard-Andersen K, Rasmussen M, Olsen A, Vilhardt F.
α-synuclein buildup is alleviated via ESCRT-dependent endosomal degradation brought about by p38MAPK inhibition in cells expressing p25α.
J Biol Chem. 2022 Nov;298(11):102531.
doi: 10.1016/j.jbc.2022.102531.
This image is from an open access article distributed under terms of a Creative Commons Attribution License.

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Purified Mouse Nerve Growth Factor 2.5S

Product Type
Purified Protein
Specificity
Nerve Growth Factor 2.5S

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PMP04Z
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Purified Mouse Nerve Growth Factor 2.5S is prepared form mouse submaxillary glands (Bocchini and Angeletti 1969) and has an apparent molecular mass of ~30 kDa. Nerve growth factor has a variety of effects on the growth and development of sensory and sympathetic neurons. In the peripheral nervous system, NGF is required for the development and maintenance of sympathetic nerve cells that use catecholamine neurotransmitters.

Purified Mouse Nerve Growth Factor 2.5S has been used to demonstrate the importance of NGF in regulation of neuronal function through the up-regulation of the transcription factor NFAT (Nuclear Factor of Activated T-cells) via activation of the PI3K/Akt pathway (Kim et al. 2014).

Target Species
Mouse
Species Cross-Reactivity
Target SpeciesCross Reactivity
Rat
N.B. Antibody reactivity and working conditions may vary between species.
Product Form
Purified natural murine nerve growth factor - lyophilized
Reconstitution
Reconstitute with 1.0 ml distilled water. Care should be taken during reconstitution as the protein may appear as a film at the bottom of the vial. Bio-Rad recommend that the vial is gently mixed after reconstitution.
Preparation
Murine nerve growth factor is prepared from the submaxillary glands of mice by sephadex and subsequent cellulose chromatography (Bocchini and Angeletti 1969).
Buffer Solution
Phosphate buffered saline
Preservative Stabilisers
None present
Purity
>98% by SDS PAGE
Approx. Protein Concentrations
1.0mg/ml
Protein Molecular Weight
Approximately 30 kDa
Regulatory
For research purposes only
Guarantee
3 months from date of reconstitution

Prior to reconstitution store at +4oC. Following reconstitution store at -20oC.

This product should be stored undiluted.

Storage in frost-free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the protein. Should this product contain a precipitate we recommend microcentrifugation before use.

This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Application Name Verified Min Dilution Max Dilution
Functional Assays
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.

References for Nerve Growth Factor 2.5S

  1. Rohn, T.A. et al. (2011) A Virus-Like Particle-Based Anti-Nerve Growth Factor Vaccine Reduces Inflammatory Hyperalgesia: Potential Long-Term Therapy for Chronic Pain.
    J Immunol. 186: 1769-80.
  2. Laursen, L.S. et al. (2011) Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K.
    J Cell Biol. 192: 797-811.
  3. Colbert, R.A. et al. (1994) Vasoactive intestinal peptide stimulates neuropeptide Y gene expression and causes neurite extension in PC12 cells through independent mechanisms.
    J Neurosci. 14: 7141-7.
  4. Smith-Thomas, L.C. et al. (1995) Increased axon regeneration in astrocytes grown in the presence of proteoglycan synthesis inhibitors.
    J Cell Sci. 108: 1307-15.
  5. Barrie, A.P. et al. (1997) Pituitary adenylyl cyclase-activating peptide stimulates extracellular signal-regulated kinase 1 or 2 (ERK1/2) activity in a Ras-independent, mitogen-activated protein Kinase/ERK kinase 1 or 2-dependent manner in PC12 cells.
    J Biol Chem. 272: 19666-71.
  6. Liu, N. et al. (2005) Enhancement of Schwann cell myelin formation by K252a in the Trembler-J mouse dorsal root ganglion explant culture.
    J Neurosci Res. 79: 310-7.
  7. Eibl, J.K. et al. (2010) Multipotent neurotrophin antagonist targets brain-derived neurotrophic factor and nerve growth factor.
    J Pharmacol Exp Ther. 332: 446-54.
  8. Vogelezang, M. et al. (2007) Neurite outgrowth on a fibronectin isoform expressed during peripheral nerve regeneration is mediated by the interaction of paxillin with alpha4beta1 integrins.
    BMC Neurosci. 8: 44.
    9. View The Latest Product References
  9. Seiberlich, V. et al. (2015) Downregulation of the microtubule associated protein Tau impairs process outgrowth and myelin basic protein mRNA transport in oligodendrocytes.
    Glia. 63 (9): 1621-35.
  10. von Büdingen, H.C. et al. (2015) The myelin oligodendrocyte glycoprotein directly binds nerve growth factor to modulate central axon circuitry.
    J Cell Biol. 210 (6): 891-8.
  11. Miyamoto, Y. et al. (2015) Involvement of the Tyro3 receptor and its intracellular partner Fyn signaling in Schwann cell myelination.
    Mol Biol Cell. 26 (19): 3489-503.
  12. Huang, J.K. et al. (2011) Retinoid X receptor gamma signaling accelerates CNS remyelination.
    Nat Neurosci. 14 (1): 45-53.
  13. Tsai, M.S. et al. (2018) Nerve growth factor upregulates sirtuin 1 expression in cholestasis: a potential therapeutic target.
    Exp Mol Med. 50 (1): e426.
  14. Lager, A.M. et al. (2018) Rapid functional genetics of the oligodendrocyte lineage using pluripotent stem cells.
    Nat Commun. 9 (1): 3708.
  15. Kim, S.M. (2022) NGF activates NFAT via the MEK1/2 pathway in PC12 cells
    All Life. 15 (1): 183-190.
  16. Borland, H. et al. (2022) α-synuclein buildup is alleviated via ESCRT-dependent endosomal degradation brought about by p38MAPK inhibition in cells expressing p25α.
    J Biol Chem. 298 (11): 102531.

Further Reading

  1. Bocchini V & Angeletti PU (1969) The nerve growth factor: purification as a 30,000-molecular-weight protein.
    Proc Natl Acad Sci U S A. 64 (2): 787-94.

Functional Assays

Synonyms
NGF BETA
UniProt
P01139
Entrez Gene
Ngf
GO Terms
GO:0005057 receptor signaling protein activity
GO:0005788 endoplasmic reticulum lumen
GO:0007422 peripheral nervous system development
GO:0008083 growth factor activity
GO:0019233 sensory perception of pain
GO:0043524 negative regulation of neuron apoptosis
GO:0045773 positive regulation of axon extension
GO:0046928 regulation of neurotransmitter secretion

PMP04Z

150036

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