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Recombinant Mouse Beta-Nerve Growth Factor (Ngf)

Cat. No.AP2C538

Product TypeAnimal Proteins

Size

Product Overview

BioVenic's Recombinant Mouse Beta-Nerve Growth Factor (Ngf) is a recombinant protein expressed from E.coli. Its predicted molecular weight is 27.1 kDa. The purity is>90%.

Specifications

Type Recombinant Protein
Species Mouse
Expression System E.coli
Purity >90%
Endotoxin < 1.0 EU/μg
Predicted Molecular Weight 27.1 kDa
Physical State Lyophilized
Formulation 0.01 mol/L PBS (pH 7.2) containing 0.2% (w/v) Procline-300.

Target Information

Mouse Beta-Nerve Growth Factor (Ngf) is a neurotrophic factor in mice that is important for the development and maintenance of sensory and sympathetic neurons. It is involved in the regulation of growth and differentiation of these neurons. Ngf also acts in the central nervous system as a trophic factor for basal forebrain cholinergic neurons. The biological activities of Ngf are mediated through binding and activation of two types of receptors, TrkA and NGF receptor. Ngf is crucial for neuroprotection and repair processes in the nervous system. Researchers study Ngf to understand its role in neuronal survival, pain perception, and various neurological disorders. This knowledge can lead to strategies for managing neurodegenerative diseases and improving nervous system health in mice.

Protein Mouse Beta-Nerve Growth Factor (Ngf)
Protein Synonym Beta-NGF; Ngf; Ngfb
Gene ID 18049
UniProt ID P01139

Shipping and Storage

This product is shipped with ice packs. Lyophilized protein can be stored at -20°C for 1 year. After reconstitution, the protein solution can be stored at 2-8°C for 2-7 days.

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

User Note

  1. Always centrifuge tubes before opening. Avoid mixing by vortexing or pipetting. Aliquot the reconstituted solution to minimize freeze-thaw cycles.

References

  1. Sørensen, E S. et al.Posttranslational modifications of bovine osteopontin: identification of twenty-eight phosphorylation and three O-glycosylation sites.Protein science : a publication of the Protein Society. 2017, 31,1: 21-34.
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