CRYAB antibody (AA 1-175)

Catalog No. ABIN1724688

This anti-CRYAB antibody is a Mouse Monoclonal antibody detecting CRYAB in ELISA and IHC. Suitable for Human. This Primary Antibody has been cited in 1 publication.

Quick Overview for CRYAB antibody (AA 1-175) (ABIN1724688)

Target: CRYAB (Crystallin, alpha B (CRYAB))

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This CRYAB antibody is un-conjugated

Application: ELISA, Immunohistochemistry (IHC)

Clone: 1D11C6E6

Product Details anti-CRYAB Antibody

Binding Specificity: AA 1-175

Purpose: CRYAB Antibody

Purification: Ascitic fluid

Immunogen: Purified recombinant fragment of CRYAB (aa1-175) expressed in E. Coli.

Isotype: IgG2a

Application Details

Application Notes: ELISA: 1/10000

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: Ascitic fluid containing 0.03 % sodium azide.

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: 4 °C,-20 °C

Storage Comment: Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.

References for anti-CRYAB antibody (ABIN1724688)

Ghosh, Shenoy, Clark: "N- and C-Terminal motifs in human alphaB crystallin play an important role in the recognition, selection, and solubilization of substrates." in: Biochemistry, Vol. 45, Issue 46, pp. 13847-54, (2006) (PubMed).

Target Details for CRYAB

Target: CRYAB (Crystallin, alpha B (CRYAB))

Alternative Name: CRYAB

Background: Crystallin, alpha B. 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.

UniProt: P02511