CRYAB Human, His
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Sterile filtered colorless solution.
Greater than 90% as determined by SDS-PAGE.
Description
CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Product Specs
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.
Product Science Overview
CRYAB is a small heat shock protein with a molecular weight of approximately 21.2 kDa . It consists of 183 amino acids and is often produced in Escherichia coli (E. coli) as a recombinant protein fused with an 8 amino acid His-tag at the C-terminus . This His-tag facilitates purification through affinity chromatography.
The protein forms oligomeric complexes, which are dynamic and can reach sizes of 800 kDa or more . These complexes exhibit subunit exchanges and organizational plasticity, contributing to the functional diversity of CRYAB .
CRYAB functions primarily as a molecular chaperone. It binds to improperly folded proteins, preventing their aggregation and maintaining cellular proteostasis . Unlike true chaperones, CRYAB does not renature proteins but stabilizes them to prevent irreversible aggregation .
Additionally, CRYAB is involved in various cellular processes, including:
CRYAB is induced by various stress conditions such as heat shock, ischemia, and oxidative stress . Its chaperone activity is crucial in protecting cells from stress-induced damage. Phosphorylation of serine residues in CRYAB occurs during development and in response to stress, usually decreasing oligomer size and modulating chaperone activity .
Mutations or dysregulation of CRYAB have been implicated in several diseases, including neurodegenerative disorders and cataracts. Its role in preventing protein aggregation makes it a potential target for therapeutic interventions in protein misfolding disorders .
The recombinant form of CRYAB, with a His-tag, is widely used in biomedical research. It provides a controlled platform to study the structural and functional properties of CRYAB, as well as its interactions with other proteins. This research aims to deepen our understanding of cellular proteostasis and explore novel therapeutic avenues for diseases associated with protein misfolding .
