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Anti-α B Crystallin Antibody

Mouse Monoclonal Antibody specific to α B Crystallin

Product Specifications

CAS Number

9007-83-4

Product Name Alternative

α(B-crystallin, Heat shock protein beta-5, HspB5, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component

Gene Name

CRYAB

Gene ID

1410

NCBI Gene ID

<a href="https://www.ncbi.nlm.nih.gov/gene/?term=CRYAB">CRYAB</a>

UniProt

P02511

Accession Number

NP_001276736

Cellular Locus

Cytoplasm, Nucleus, Secreted, Lysosome

Host

Mouse

Reactivity

Human, Bovine

Immunogen

Native alpha B crystallin

Target Antigen

α-crystallin B chain

Target

α B Crystallin

Clonality

Monoclonal

Isotype

IgG1

Type

Antibody

Applications

WB, ELISA

Field of Research

Heat Shock& Stress Proteins

Purification Method

Purified by Protein G affinity chromatography

Concentration

Lot Specific

Dilution

Dilute in PBS or medium which is identical to that used in the assay system.

Format

Purified

Form

Liquid

Buffer

Phosphate Buffered Saline

Function

May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity). {UniProtKB:P23927}.

Additionnal Information

Immunoblotting: use at 0.5-1ug/ml. A band of ~20-21 kDa is detected <br><br>ELISA: use at 1ug/ml. <br><br>These are recommended concentrations. User should determine optimal concentrations for their application. <br><br>Positive control: Purified alpha B crystallin.

Storage Conditions

This antibody is stable for at least one (1) year at -20°C.

Specificity

This antibody recognizes human and bovine alpha B crystallin. It does not cross-react with alpha A crystallin, beta- L crystallin, beta-H crystallin, gamma crystallin, Hsp25, Hsp27, or Hsp47 proteins.

Formulation

PBS, pH 7.4.

Buffer pH

pH 7.4

Target Background

Alpha crystallins are water-soluble lens proteins of the vertebrate eye that are related to the small heat shock protein family. Lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are further divided into acidic (Alpha A) and basic (Alpha B) groups. In the lens, alpha crystallin maintains proper refractive index, however it can also function as a molecular chaperone that binds to denatured proteins, keeping them in solution and maintaining the translucency of the lens. In response to cellular stress, alpha crystallin is phosphorlyated and may serve a structural control function and play a role in protein maintenance. Both alpha A and alpha B crystallin prevent apoptosis by inhibiting caspases. Alpha B crystallin is found in many cells and organs outside the lens and is over- expressed in cells subjected to stress conditions and in several neurological disorders.
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