CRYAB purified MaxPab mouse polyclonal antibody (B01P)
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More Files
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Specifications
Product Description
Mouse polyclonal antibody raised against a full-length human CRYAB protein.
Immunogen
CRYAB (AAH07008.1, 1 a.a. ~ 175 a.a) full-length human protein.
Sequence
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
Host
Mouse
Reactivity
Human
Quality Control Testing
Antibody reactive against mammalian transfected lysate.
Storage Buffer
In 1x PBS, pH 7.4
Storage Instruction
Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing.
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Applications
Western Blot (Transfected lysate)
Western Blot analysis of CRYAB expression in transfected 293T cell line (H00001410-T02) by CRYAB MaxPab polyclonal antibody.
Lane 1: CRYAB transfected lysate(20.20 KDa).
Lane 2: Non-transfected lysate.
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Gene Info — CRYAB
Entrez GeneID
1410GeneBank Accession#
BC007008.1Protein Accession#
AAH07008.1Gene 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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