CRYAB antibody

Catalog No. ABIN7235811

Product Details anti-CRYAB Antibody

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

Reactivity: Human, Rat, Mouse

Host: Rabbit

Clonality: Polyclonal

Conjugate: This CRYAB antibody is un-conjugated

Application: Western Blotting (WB), ELISA

Characteristics: Polyclonal Antibody

Purification: Affinity purification

Immunogen: Recombinant protein of human CRYAB

Isotype: IgG

Application Details

Application Notes: WB 1:500-1:2000

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 0.2 mg/mL

Buffer: PBS with 0.05 % sodium azide and 50 % glycerol, PH7.4

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: -20 °C

Storage Comment: Store at -20°C. Avoid freeze / thaw cycles.

Target Details for CRYAB

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

Alternative Name: Crystallin-alpha B (CRYAB Products)

Background: 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.

Molecular Weight: 20 kDa

UniProt: P02511