Crystallin-αB (phospho Ser59) rabbit pAb

Sizes: 50μL, 100μL

Catalogue Numbers: ES4832-50, ES4832-100

Citations, Manuals and MSDS Available upon request.

Background: Mammalian lens crystallins are divided into alpha, beta, and gamma families. 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 (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. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distin

Alternate Name: CRYAB; CRYA2; Alpha-crystallin B chain; Alpha (B)-crystallin; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component

Source: Rabbit

Applications: IHC; IF; ELISA

Dilution: Immunohistochemistry: 1/100 - 1/300. ELISA: 1/5000. Not yet tested in other applications.

Reactivity: Human; Mouse; Rat

Immunogen: The antiserum was produced against synthesized peptide derived from human CRYAB/Crystallin-alpha-B around the phosphorylation site of Ser59. AA range:31-80

Storage and Stability: -20°C/1 year

Clonality: Polyclonal

Isotype: IgG

Concentration: 1 mg/ml

Human Gene ID: 1410

Human SWISS Prot NO: P02511

Subcellular Location: Cytoplasm. Nucleus. Secreted. Lysosome. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles (PubMed:19464326). Localizes at the Z-bands and the intercalated disk in cardiomyocytes (PubMed:28493373). Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059).

Research Use Only