catalog number :
MBS197046
products type :
Recombinant Protein
products full name :
Recombinant Human Alpha Crystallin A (CRYAA)
products short name :
alpha crystallin A
other names :
alpha-crystallin A chain; Alpha-crystallin A chain; alpha-crystallin A chain; OTTHUMP00000109430; crystallin, alpha-1; heat shock protein beta-4; human alphaA-crystallin (CRYA1); crystallin, alpha A; Heat shock protein beta-4
other gene names :
CRYAA; CRYAA; CRYA1; HSPB4; CRYA1; HSPB4
uniprot entry name :
CRYAA_HUMAN
sequence :
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSGISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRLPSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS.
specificity :
Human alpha crystallin A
purity :
Greater than 95% as determined by SDS-PAGE and RP-HPLC.
form :
Sterile-filtered colorless solution contains 20mM Tris-HCl, pH 7.5, 50mM NaCl and 1mM EDTA. Purified by proprietary chromatographic techniques.
storage stability :
Store at 4 degree C if entire vial will be used within 2-4 weeks. Store at or below -20 degree C for longer periods of time. For long term storage, addition of a carrier protein (0.1% HSA or BSA) is recommended.
products description :
Alpha crystallins are composed of two gene products: alpha-A (acidic) and alpha-B (basic). Alpha crystallins are induced by heat shock and are members of the small heat shock protein family. They act as molecular chaperones. In addition, alpha crystallins have autokinase activity and play a role in intracellular architecture. The expression of alpha crystalline A is preferentially restricted to lens cells. Recombinant Human CRYAA produced in E. coli is a single, non-glycosylated polypeptide chain containing 173 amino acids with a molecular weight of 19.9kDa.
ncbi acc num :
NP_000385.1
ncbi gb acc num :
NM_000394.2
ncbi mol weight :
19,909 Da
ncbi pathways :
Protein Processing In Endoplasmic Reticulum Pathway (167325); Protein Processing In Endoplasmic Reticulum Pathway (167190)
ncbi summary :
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. 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) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC). [provided by RefSeq]
uniprot summary :
CRYA1: a major structural protein of the eye lens. A member of the small heat shock protein (sHSP, also known as the HSP20) family. Alpha-A is preferentially restricted to the lens. Protein type: Chaperone; Heat shock protein. Chromosomal Location of Human Ortholog: 21q22.3. Cellular Component: cytoplasm; nucleus. Molecular Function: identical protein binding; protein binding; metal ion binding; unfolded protein binding; structural constituent of eye lens. Biological Process: negative regulation of intracellular transport; visual perception; response to stimulus; protein refolding; protein homooligomerization; negative regulation of apoptosis. Disease: Cataract 9, Multiple Types