Source:

Escherichia coli.

Molecular Weight:

16.7 kDa, observed by reducing SDS-PAGE.

Purity:

> 95% by SDS-PAGE and HPLC analyses.

Biological activity:

Bioassay data are not available.

AA Sequence:

MSESLVVCD VAEDLVEKLR KFRFRKETNN AAIIMKIDKD KRLVVLDEEL EGISPDELKD ELPERQPRFI VYSYKYQHDD GRVSYPLCFI FSSPVGCKPE QQMMYAGSKN KLVQTAELTK VFEIRNTEDL TEEWLREKLG FFH

Endotoxin:

< 0.2 EU/μg, determined by LAL method.

Formulation:

Lyophilized after extensive dialysis against PBS.

Background:

Glia Maturation Factor beta (GMF-beta) is a 17 kDa brain specific protein that belongs to the ADF/cofilin superfamily. It is a neurotrophin that induces maturation of neurons and glial cells. Unlike other neurotrophins, GMF-β lacks a leader sequence and can be phosphorylated by protein kinase A and protein kinase C suggesting its role in signal transduction. GMF-β is a prominent mediator of inflammation in the central nervous system and can activate several inflammation-related genes such as tumor necrosis factor-α and interleukin-1β. Researchers have shown there are significantly higher levels of GMF-β protein in all the effected regions of Alzheimer’s disease (AD) brains suggesting an important role of GMF-β in AD pathogenesisRecombinant human Glia Maturation Factor beta (rhGMF-beta) produced in E.coli is a single non-glycosylated polypeptide chain containing 142 amino acids. rhGMF-beta has a molecular mass of 16.7kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.

Usage:

This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only.

Physical Appearance:

Sterile Filtered White lyophilized (freeze-dried) powder.

Reconstitution:

Reconstituted in ddH2O at 100 μg/mL.

Storage:

Lyophilized recombinant human Glia Maturation Factor beta (rhGMF-beta) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhGMF-beta remains stable up to 2 weeks at 4°C or up to 3 months at -20°C.