CRYAB monoclonal antibody, clone 2E8
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Specification
Product Description
Mouse monoclonal antibody raised against full length recombinant CRYAB.
Immunogen
Recombinant protein corresponding to amino acids 1-175 of human CRYAB.
Host
Mouse
Reactivity
Human, Mouse
Specificity
This antibody has the specificity against CRYAB, do not detect CRYAA.
Form
Liquid
Purification
Protein G purification
Isotype
IgG2b, kappa
Recommend Usage
ELISA
Immunocytochemistry (1:100)
Immunofluorescence (1:100)
Western Blot (1:1000)
The optimal working dilution should be determined by the end user.Storage Buffer
In PBS, pH 7.4 (10% glycerol, 0.02% sodium azide).
Storage Instruction
Store at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C.
Aliquot to avoid repeated freezing and thawing.Note
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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Applications
Western Blot (Tissue lysate)
Western blot analysis of mouse eye tissue lysate.Immunocytochemistry
Immunofluorescence
Immunofluorescence analysis of HeLa cells. The cell was stained with CRYAB monoclonal antibody, clone 2E8 (Cat# MAB1075) (1:100). The secondary antibody (green) was used Alexa Fluor 488. DAPI was stained the cell nucleus (blue).Enzyme-linked Immunoabsorbent Assay
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Gene Info — CRYAB
Entrez GeneID
1410GeneBank Accession#
NM_001885Protein Accession#
NP_001876Gene Name
CRYAB
Gene Alias
CRYA2, CTPP2, HSPB5
Gene Description
crystallin, alpha B
Gene Ontology
HyperlinkGene Summary
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
Other Designations
alpha crystallin B chain|heat-shock 20 kD like-protein
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Interactome
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Disease
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Publication Reference
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The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation.
Kamradt MC, Chen F, Sam S, Cryns VL.
The Journal of Biological Chemistry 2002 Oct; 277(41):38731.
Application:IF, WB-Ce, Mouse, C2C12 myoblasts.
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Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro.
Reddy GB, Narayanan S, Reddy PY, Surolia I.
FEBS Letters 2002 Jul; 522(1-3):59.
Application:Added, Recombinant protein.
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Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes.
Ito H, Kamei K, Iwamoto I, Inaguma Y, Garcia-Mata R, Sztul E, Kato K.
Journal of Biochemistry 2002 Apr; 131(4):593.
Application:IF, WB, Human, HeLa, U373 MG cells.
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The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation.
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