Mouse Alpha B Crystallin Monoclonal Antibody | anti-CRYAB antibody

Anti-Alpha B Crystallin Monoclonal Antibody

Cat. Num. AAA190505

• Gene Names: CRYAB; CRYA2; CTPP2; HSPB5
• Reactivity: Human, bovine
• Applications: ELISA, Immunoblot, Western Blot
• Synonyms: Alpha B Crystallin; Monoclonal Antibody; Anti-Alpha B Crystallin Monoclonal Antibody; anti-CRYAB antibody

• Host: Mouse
• Reactivity: Human, bovine
• Clonality: Monoclonal
• Isotype: IgG1
• Clone Number: 1A7.D5
• Specificity: Alpha B Crystallin; 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.
• Form/Format: 100ug in PBS, pH 7.4, purified by Protein G affinity chromatography.

• Applicable Applications for anti-CRYAB antibody: ELISA; Immunoblot
• Application Notes: Immunoblotting: use at 0.5-1ug/ml. A band of ~20-21 kDa is detected. ELISA: use at 1ug/ml. These are recommended concentrations. User should determine optimal concentrations for their application. Positive control: Purified alpha B crystallin.
• Antigen: Native alpha B crystallin
• Preservative: None
• Dilution Instructions: Dilute in PBS or medium which is identical to that used in the assay system.
• Preparation and Storage: This antibody is stable for at least one (1) year at -20 degree C. Avoid repeated freezing and thawing.

Related Product Information for anti-CRYAB antibody

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 overexpressed in cells subjected to stress conditions and in several neurological disorders.

NCBI and Uniprot Product Information

• NCBI GI #: 4503057
• NCBI GeneID: 1410
• NCBI Accession #: NP_001876.1
• NCBI GenBank Nucleotide #: NM_001885.1
• UniProt Accession #: P02511; O43416; Q9UC37; Q9UC38; Q9UC39; Q9UC40; Q9UC41; B0YIX0
• Molecular Weight: 20,159 Da
• NCBI Official Full Name: alpha-crystallin B chain
• NCBI Official Synonym Full Names: crystallin, alpha B
• NCBI Official Symbol: CRYAB
• NCBI Official Synonym Symbols: CRYA2; CTPP2; HSPB5
• NCBI Protein Information: alpha-crystallin B chain; OTTHUMP00000234278; OTTHUMP00000234282; OTTHUMP00000234283; OTTHUMP00000234284; OTTHUMP00000234287; OTTHUMP00000234289; alpha B crystallin; alpha(B)-crystallin; alpha crystallin B chain; heat shock protein beta-5; rosenthal fiber component; heat-shock 20 kD like-protein; renal carcinoma antigen NY-REN-27
• UniProt Protein Name: Alpha-crystallin B chain
• Protein Family: Alpha-crystallin
• UniProt Gene Name: CRYAB
• UniProt Synonym Gene Names: CRYA2
• UniProt Entry Name: CRYAB_HUMAN

NCBI Description

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]

Uniprot Description

CRYAB: a major structural protein of the eye lens. A member of the small heat shock protein (sHSP also known as the HSP20) family. Alpha-B is expressed in the lens as well as other tissues. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.

Protein type: Heat shock protein; Chaperone

Chromosomal Location of Human Ortholog: 11q22.3-q23.1

Cellular Component: microtubule cytoskeleton; Golgi apparatus; cell surface; mitochondrion; cytoplasm; actin filament bundle; plasma membrane; Z disc; nucleus; cytosol

Molecular Function: identical protein binding; protein binding; protein homodimerization activity; metal ion binding; microtubule binding; unfolded protein binding; structural constituent of eye lens

Biological Process: lens development in camera-type eye; muscle development; protein folding; stress-activated MAPK cascade; microtubule polymerization or depolymerization; negative regulation of caspase activity; response to estradiol stimulus; tubulin folding; muscle contraction; negative regulation of intracellular transport; response to hydrogen peroxide; response to hypoxia; negative regulation of cell growth; protein homooligomerization; aging; negative regulation of apoptosis

Disease: Cataract 16, Multiple Types; Myopathy, Myofibrillar, Fatal Infantile Hypertonic, Alpha-b Crystallin-related; Myopathy, Myofibrillar, 2; Cardiomyopathy, Dilated, 1ii