CRYAB antibody
Quick Overview for CRYAB antibody (ABIN6655665)
Target
See all CRYAB AntibodiesReactivity
Host
Clonality
Conjugate
Application
Clone
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Supplier Product No.
- 200-301-e85
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Supplier
- Rockland
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Purpose
- Alpha B Crystallin Antibody
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Cross-Reactivity (Details)
- A BLAST analysis was used to suggest cross-reactivity with alpha B crystallin from Human and bovine based on 100 % homology with the immunizing sequence.
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Purification
- Anti-Alpha B Crystallin Antibody was purified by Protein G chromatography.
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Sterility
- Sterile filtered
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Immunogen
- Alpha B Crystallin Antibody was produced in mice by repeated immunizations with Native Alpha B Crystallin protein.
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Isotype
- IgG1
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Application Notes
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ELISA_Dilution: 1:200
Western_Blot_Dilution: 1:2000
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Comment
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Anti-Alpha B Crystallin Antibody has been tested in WB and IF and is recommended for use in ELISA. Expect a band approximately ~20kDa (Predicted mol. weight is ~21kDa) corresponding to αB-crystallin. Specific conditions for reactivity should be optimized by the end user.
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Restrictions
- For Research Use only
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Format
- Liquid
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Buffer
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Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Stabilizer: 50 % (v/v) Glycerol
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Storage
- 4 °C,-20 °C
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Storage Comment
- Store vial at -20° C prior to opening. Aliquot contents and freeze at -20° C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.
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Expiry Date
- 12 months
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- CRYAB (Crystallin, alpha B (CRYAB))
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Alternative Name
- Alpha B Crystallin
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Background
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Synonyms: AACRYA, CRYA2, CRYAB, CTPP2, HspB5, NY Ren 27 antigen antibody, alpha crystallin B antibody, Heat shock protein beta-5, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component
Background: The alpha-crystallins are major water-soluble lens structural proteins of the vertebrate eye that are related to the small heat shock protein family. The alpha-crystallins possess structural and functional similarities with Hsp25 and Hsp27. Mammalian lens cystallins are divided into alpha, beta and gamma families. Alpha and beta families are further divided into acidic and basic groups (Alpha-A and Alpha-B respectively). In the lens, alpha-crystallin primarily functions to maintain proper refractive index, however it can also function as a molecular chaperone that binds to the denatured proteins, keeping them in solution and thereby maintaining the translucency of the lens. When cellular stress occurs, alpha-crystallin enters its' phosphorylated state and may serve a structural control function and play a role in protein maintenance. In addition to their interaction with proteins, alpha-crystallins also interact with native molecules such as membrane proteins, Golgi matrix protein, structural proteins, nuclear proteins and DNA. Two other functions are an autokinase activity and participation in the intracellular architecture, and it has also been proven that both alpha-A and B prevent apoptosis by inhibiting caspases. Specifically, alpha-B cystallin is found in many cells and organs outside the lens, and alpha B is overexpressed in several neurological disorders and in cell lines under stress conditions.
Gene Name: CRYAB
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Gene ID
- 1410
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NCBI Accession
- NP_001876
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UniProt
- P02511
Target
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