CRYAB (clone 1D11C6E6), anti-human
€443.00
In stock
SKU
252752
Catalog Nr.: 252752
Size: 0.1 ml
Isotype: Mouse IgG2a
Applications: WB, IHC
Size: 0.1 ml
Isotype: Mouse IgG2a
Applications: WB, IHC
Protein Family: Chaperones and folding catalysts
Pathway and Disease: Folding, Sorting and Degradation
Description:
CRYAB (Alpha B crystallin) is a molecular chaperone. 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.
Alternate Names: Alpha-crystallin B chain, Alpha(B)-crystallin, Heat shock protein beta-5, HspB5, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component, CRYA2, CTPP2, HSPB5, CRYAB
Application Notes: WB: 1:500-1:2000; IHC: 1:200-1:1000
Accession No.: P02511
Antigen: Purified recombinant fragment of CRYAB(aa1-175) expressed in E. coli.
Format: Each vial contains 0.1 ml ascitic fluid with 0.03% sodium azide.
Storage:
Store at 4°C for short term use only. Store at -20°C for storage over 1 month. Product is guaranteed 6 months from the date of shipment.
Pathway and Disease: Folding, Sorting and Degradation
Description:
CRYAB (Alpha B crystallin) is a molecular chaperone. 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.
Alternate Names: Alpha-crystallin B chain, Alpha(B)-crystallin, Heat shock protein beta-5, HspB5, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component, CRYA2, CTPP2, HSPB5, CRYAB
Application Notes: WB: 1:500-1:2000; IHC: 1:200-1:1000
Accession No.: P02511
Antigen: Purified recombinant fragment of CRYAB(aa1-175) expressed in E. coli.
Format: Each vial contains 0.1 ml ascitic fluid with 0.03% sodium azide.
Storage:
Store at 4°C for short term use only. Store at -20°C for storage over 1 month. Product is guaranteed 6 months from the date of shipment.
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