CRYAB polyclonal antibody
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Specifications
Product Description
Goat polyclonal antibody raised against synthetic peptide of CRYAB.
Immunogen
A synthetic peptide corresponding to human CRYAB.
Sequence
C-RLEKDRFSVNLD
Host
Goat
Theoretical MW (kDa)
20.2
Reactivity
Human, Mouse
Form
Liquid
Purification
Antigen affinity purification
Concentration
0.5 mg/mL
Quality Control Testing
Antibody Reactive Against Synthetic Peptide.
Recommend Usage
ELISA (1:128000)
Western Blot (0.01-0.03 ug/mL)
The optimal working dilution should be determined by the end user.Storage Buffer
In Tris saline, pH 7.3 (0.5% BSA, 0.02% sodium azide)
Storage Instruction
Store at -20°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)
CRYAB polyclonal antibody (Cat # PAB7394) (0.01 ug/mL) staining of mouse eye lysate (35 ug protein in RIPA buffer). Primary incubation was 1 hour. Detected by chemiluminescence.Enzyme-linked Immunoabsorbent Assay
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Gene Info — CRYAB
Entrez GeneID
1410Protein Accession#
NP_001876.1Gene 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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Interactomes
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Diseases
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Publication Reference
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Differences in atrial fibrillation-associated proteins between the left and right atrial appendages from patients with rheumatic mitral valve disease: A comparative proteomic analysis.
Liu H, Chen G, Zheng H, Qin H, Liang M, Feng K, Wu Z.
Molecular Medicine Reports 2016 Sep; 14(5):4232.
Application:WB-Ti, Human, the right atrial appendage (RAA) and left atrial appendage (LAA) in patients with rheumatic mitral valve disease.
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Protective and therapeutic role for alphaB-crystallin in autoimmune demyelination.
Ousman SS, Tomooka BH, van Noort JM, Wawrousek EF, O'Connor KC, Hafler DA, Sobel RA, Robinson WH, Steinman L.
Nature 2007 Jul; 448(7152):474.
Application:WB, Mouse, Primary astrocytes.
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Differences in atrial fibrillation-associated proteins between the left and right atrial appendages from patients with rheumatic mitral valve disease: A comparative proteomic analysis.
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