CRYAB (Human) Recombinant Protein (P01)
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More Files
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Specifications
Product Description
Human CRYAB full-length ORF ( AAH07008, 1 a.a. - 175 a.a.) recombinant protein with GST-tag at N-terminal.
Sequence
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLPEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKRVSGPERTIPITREEKPAVTAAPKK
Host
Wheat Germ (in vitro)
Theoretical MW (kDa)
44.99
Preparation Method
Purification
Glutathione Sepharose 4 Fast Flow
Quality Control Testing
12.5% SDS-PAGE Stained with Coomassie Blue.
Storage Buffer
50 mM Tris-HCI, 10 mM reduced Glutathione, pH=8.0 in the elution buffer.
Storage Instruction
Store at -80°C. Aliquot to avoid repeated freezing and thawing.
Note
Best use within three months from the date of receipt of this protein.
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Applications
Enzyme-linked Immunoabsorbent Assay
Western Blot (Recombinant protein)
Antibody Production
Protein Array
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Gene Info — CRYAB
Entrez GeneID
1410GeneBank Accession#
BC007008Protein Accession#
AAH07008Gene Name
CRYAB
Gene Alias
CRYA2, CTPP2, HSPB5
Gene Description
crystallin, alpha B
Gene Ontology
HyperlinkGene 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. 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
Other Designations
alpha crystallin B chain|heat-shock 20 kD like-protein
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Interactomes
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Diseases
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