CRYAB antibody (AA 51-150) (Cy7)

Catalog No. ABIN707912

The Rabbit Polyclonal anti-CRYAB antibody has been validated for IF (cc) and IF (p). It is suitable to detect CRYAB in samples from Rat and Mouse.

Quick Overview for CRYAB antibody (AA 51-150) (Cy7) (ABIN707912)

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

Reactivity: Rat, Mouse

Host: Rabbit

Clonality: Polyclonal

Conjugate: This CRYAB antibody is conjugated to Cy7

Application: Immunofluorescence (Cultured Cells) (IF (cc)), Immunofluorescence (Paraffin-embedded Sections) (IF (p))

Product Details anti-CRYAB Antibody (Cy7)

Binding Specificity: AA 51-150

Cross-Reactivity: Mouse, Rat

Predicted Reactivity: Human,Dog,Cow,Pig,Horse

Purification: Purified by Protein A.

Immunogen: KLH conjugated synthetic peptide derived from human Alpha B Crystallin.

Isotype: IgG

Application Details

Application Notes: IF(IHC-P) 1:50-200
IF(IHC-F) 1:50-200
IF(ICC) 1:50-200

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 μg/μL

Buffer: Aqueous buffered solution containing 0.01M TBS ( pH 7.4) with 1 % BSA, 0.03 % Proclin300 and 50 % Glycerol.

Preservative: ProClin

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

Storage: -20 °C

Storage Comment: Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

Expiry Date: 12 months

Target Details for CRYAB

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

Alternative Name: Alpha B Crystallin

Background:

Synonyms: CRYAB, CRYA2, Alpha crystallin B chain, AACRYA, Alpha B crystalline, Alpha crystallin B chain, AlphaB crystalline, AlphaB-crystallin, Alpha-crystallin B chain, CRYAB_HUMAN, Crystallin alpha B, Crystallin alpha polypeptide 2, CTPP 2, CTPP2, Heat shock 20 kD like protein, Heat shock protein beta 5, Heat shock protein beta-5, HSPB5, NY REN 27 antigen, Renal carcinoma antigen NY REN 27, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component.

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. 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, Jul 2008].

Gene ID: 1410