Crystallin, alpha A, Bovine Protein | CRYAA protein

Crystallin, alpha A, Bovine

Cat. Num. AAA634694

• Gene Names: CRYAA; CRYA1; HSPB4; CTRCT9
• Applications: Western Blot
• Purity: Affinity Purified; 75% as determined by SDS-PAGE analysis. Purified by affinity chromatography.
• Synonyms: Crystallin; alpha A; Bovine; CRYAA protein

• Host: Bovine eye lens
• Purity/Purification: Affinity Purified; 75% as determined by SDS-PAGE analysis. Purified by affinity chromatography.
• Form/Format: Supplied as a liquid in PBS, pH 7.2, 0.05M phosphate buffer, 0.15M sodium chloride.

• Applicable Applications for CRYAA protein: Western Blot (WB)
• Application Notes: On a 15-well minigel system, 100ng of protein per lane should be sufficient when used in a colorimetric Western blot.
• Note: May contain small amounts of alphaB crystallin.
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, aliquot to avoid repeated freezing and thawing and freeze at -70 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 12 months.

Related Product Information for CRYAA protein

Alpha-crystallins composed of alpha-A (~19kD) and alpha-B (~19.2kDa) subunits, are major water-soluble proteins accounting for almost 50% of the total protein of the mammalian transparent eye lens and they are also found in a variety of other tissues (1). The alpha-crystallins have sequence homology as well as structural and functional similarities with the small heat shock proteins such as Hsp25 (2). The alpha-crystallins and Hsp25 have been shown to act as molecular chaperones by suppression of heat-induced aggregation of other proteins and are efficient inhibitors of elastase. The alpha-B subunit like Hsp25 was also found to be a substrate for protein cross-linking by tissue-type transglutaminase (2). The alpha-crystallins may be involved in metabolic pathways important for the development, maintenance, or pathology of the lens (3). They prevent destabilized proteins from precipitating out of solution by forming a soluble high-molecular-weight (HMW) complex (4). The bovine HMW protein form of the lens is composed mostly of alpha-crystallin in a highly aggregated state which has markedly reduced chaperone ability compared to alpha-crystallin. NMR spectroscopy of the naturally occurring HMW complex shows that the short C-terminal extension of alpha-B subunit in HMW has lost its flexibility whereas the alpha-A subunit extension is still flexible. These results suggest that depletion of alpha-crystallin with age as it is converted to HMW, could be one of the contributing factors to cataract formation in the lens (5).

Product Categories/Family for CRYAA protein

Molecular Biology; MB-Crystallins

NCBI and Uniprot Product Information

• NCBI GI #: 109731199
• NCBI GeneID: 1409
• UniProt Accession #: P02489; Q53X53; AAB33370
• Molecular Weight: 19,909 Da
• NCBI Official Full Name: Crystallin, alpha A
• NCBI Official Synonym Full Names: crystallin, alpha A
• NCBI Official Symbol: CRYAA
• NCBI Official Synonym Symbols: CRYA1; HSPB4; CTRCT9
• NCBI Protein Information: alpha-crystallin A chain; crystallin, alpha-1; heat shock protein beta-4; human alphaA-crystallin (CRYA1)
• UniProt Protein Name: Alpha-crystallin A chain
• Protein Family: Alpha-crystallin
• UniProt Gene Name: CRYAA
• UniProt Synonym Gene Names: CRYA1; HSPB4; HspB4
• UniProt Entry Name: CRYAA_HUMAN

NCBI Description

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, Jul 2008]

Uniprot Description

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: Heat shock protein; Chaperone

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