Recombinant Human CRYAB protein

• Cat.No.: CRYAB-9158H
• Product Overview: Recombinant Human CRYAB(1-175 aa) was expressed in E. coli.

Specification

• Description: Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein(sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of alpha-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.
• Source: E. coli
• Species: Human
• Form: Liquid. In 20 mM Tris-HCl buffer (pH 7.5) containing 50mM NaCl, 1mM EDTA
• Molecular Mass: 20.1kDa (175aa)
• AA Sequence: MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK
• Purity: > 95% by SDS - PAGE
• Storage: Can be stored at +4 centigrade short term (1-2 weeks). For long term storage, aliquot and store at -20 centigrade or -70 centigrade. Avoid repeated freezing and thawing cycles.
• Concentration: 1 mg/ml (determined by Bradford assay)
• Tag: Non
• Protein length: 1-175 a.a.

Gene Information

• Gene Name: CRYAB crystallin, alpha B [ Homo sapiens ]
• Official Symbol: CRYAB
• Synonyms: CRYAB; crystallin, alpha B; CRYA2; alpha-crystallin B chain; HSPB5; heat shock protein beta-5; rosenthal fiber component; heat-shock 20 kD like-protein; renal carcinoma antigen NY-REN-27; CTPP2
• Gene ID: 1410
• mRNA Refseq: NM_001885
• Protein Refseq: NP_001876
• MIM: 123590
• UniProt ID: P02511
• Chromosome Location: 11q22.3-q23.1
• Pathway: Protein processing in endoplasmic reticulum, organism-specific biosystem; Protein processing in endoplasmic reticulum, conserved biosystem
• Function: protein binding; protein homodimerization activity; structural constituent of eye lens; unfolded protein binding