alpha crystallin B, Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 11; NC_000011.9 (111779350..111782473, complement). Location: 11q22.3-q23.1

E.coli

Greater than 95% as determined by SDS-PAGE and RP-HPLC.

Sterile-filtered colorless solution contains 20mM Tris-HCl, pH 7.5, 50mM NaCl and 1mM EDTA. Purified by proprietary chromatographic techniques.

1.0 mg/ml (lot specific)

Store at 4°C if entire vial will be used within 2-4 weeks. Store at or below -20°C for longer periods of time. For long term storage, addition of a carrier protein (0.1% HSA or BSA) is recommended.

Small volumes of CRYAB recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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. Alpha crystalline B is expressed in many tissues and is associated with many neurological diseases.

Recombinant Human CRYAB produced in E. coli is a single, non-glycosylated polypeptide chain containing 175 amino acids with a molecular weight of 20.2kDa.

crystallin, alpha B

alpha-crystallin B chain; OTTHUMP00000234278; OTTHUMP00000234282; OTTHUMP00000234283; OTTHUMP00000234284; OTTHUMP00000234287; OTTHUMP00000234289; alpha B crystallin; alpha(B)-crystallin; alpha crystallin B chain; heat shock protein beta-5; rosenthal fiber component; heat-shock 20 kD like-protein; renal carcinoma antigen NY-REN-27

Alpha-crystallin B chain

CRYA2  [Similar Products]

CRYAB_HUMAN

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. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq]

CRYAB: a major structural protein of the eye lens. A member of the small heat shock protein (sHSP also known as the HSP20) family. Alpha-B is expressed in the lens as well as other tissues. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.

Protein type: Heat shock protein; Chaperone

Chromosomal Location of Human Ortholog: 11q22.3-q23.1

Cellular Component: microtubule cytoskeleton; Golgi apparatus; cell surface; mitochondrion; cytoplasm; actin filament bundle; plasma membrane; cytosol; Z disc; nucleus

Molecular Function: identical protein binding; protein binding; protein homodimerization activity; microtubule binding; metal ion binding; unfolded protein binding; structural constituent of eye lens

Biological Process: lens development in camera-type eye; muscle development; protein folding; stress-activated MAPK cascade; microtubule polymerization or depolymerization; negative regulation of caspase activity; response to estradiol stimulus; tubulin folding; muscle contraction; negative regulation of intracellular transport; response to hydrogen peroxide; response to hypoxia; negative regulation of cell growth; protein homooligomerization; negative regulation of apoptosis; aging

Disease: Cataract 16, Multiple Types; Myopathy, Myofibrillar, Fatal Infantile Hypertonic, Alpha-b Crystallin-related; Myopathy, Myofibrillar, 2; Cardiomyopathy, Dilated, 1ii

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