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Anti-alpha B-crystallin, clone aB1788G7G6, Cat. No. MABN2552, is a highly specific mouse monoclonal antibody that targets Alpha-crystallin B chain and has been tested for use in ELISA, Immunofluorescence, Immunohistochemistry, Inhibition Assay, and Western Blotting.
More>>Anti-alpha B-crystallin, clone aB1788G7G6, Cat. No. MABN2552, is a highly specific mouse monoclonal antibody that targets Alpha-crystallin B chain and has been tested for use in ELISA, Immunofluorescence, Immunohistochemistry, Inhibition Assay, and Western Blotting. Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Alpha-crystallin B chain (UniProt: P02511; also known as Alpha(B)-crystallin, Heat shock protein beta-5, HspB5, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component) is encoded by the CRYAB (also known as CRYA2, HSOB5) gene (Gene ID: 1410) in human. Alpha-crystallin is a small heat shock protein that is composed of A and B subunits that display about 55% sequence homology. They both serve as molecular chaperones. They are generally present in a molar ratio of 3:1 (alphaA:alphaB). AlphaB is a stress-inducible form that is present in lens, retina, heart and skeletal muscle, and kidney. However, alpha, which is non-stress inducible form is present mainly in lens. Higher expression of alphaB has also been reported in several cancers, including gliomas, renal cell carcinoma, and metaplastic breast carcinomas. Phosphorylation of alphaB is shown to reduce its oligomerization and its anti-apoptotic activities. As a negative regulator of inflammation, it is shown to protect against multiple sclerosis and block ischemic injury, brain stroke, and spinal cord contusion injury in animal models. Mutations in CRYAB gene is reported to cause myofibrillar myopathies characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils. (Ref.: Nahomi, RB., et al. (2019). J. Immunol. Methods. 467; 37-47).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG1 in PBS without preservatives.
Applications
Application
Anti-alpha B-crystallin, clone aB1788G7G6, Cat. No. MABN2552, is a highly specific mouse monoclonal antibody that targets Alpha-crystallin B chain and has been tested for use in ELISA, Immunofluorescence, Immunohistochemistry, Inhibition Assay, and Western Blotting.
Key Applications
ELISA
Immunofluorescence
Immunohistochemistry
Inhibition
Western Blotting
Application Notes
Western Blotting Analysis: A 1:1,000 dilution from a representative lot detected alpha B-crystallin in mouse eye and human retina tissue lysate.
Immunohistochemistry Analysis: A representative lot detected alpha B-crystallin in Immunohistochemistry applications (Nahomi, R.B., et. al. (2019). J. Immunol. Methods. 467; 37-47).
ELISA Analysis: A representative lot detected alpha B-crystallin in ELISA applications (Nahomi, R.B., et. al. (2019). J. Immunol. Methods. 467; 37-47).
Inhibition Analysis: A representative lot inhibited the chaperone and anti-apoptotic activities of alpha B-crystallin. (Nahomi, R.B., et. al. (2019). J. Immunol. Methods. 467; 37-47).
Immunofluorescence Analysis: A representative lot detected alpha B-crystallin in Immunofluorescence applications (Nahomi, R.B., et. al. (2019). J. Immunol. Methods. 467; 37-47).
Western Blotting Analysis: A representative lot detected alpha B-crystallin in Western Blotting applications (Nahomi, R.B., et. al. (2019). J. Immunol. Methods. 467; 37-47).
Biological Information
Immunogen
KLH-conjugated linear peptide corresponding to 21 amino acids from the N-terminal half of human Alpha(B)-crystallin.
Clone
aB1788G7G6
Concentration
Please refer to lot specific datasheet.
Host
Mouse
Specificity
Clone aB1788G7G6 is a mouse monoclonal antibody that detects Alpha(B)-crystallin. It targets an epitope within 21 amino acids within the N-terminal half.
Isotype
IgG1κ
Species Reactivity
Human
Mouse
Species Reactivity Note
Human, Mouse. Predicted to react with Bovine, Monkey, Rat based on 100% sequence homology.
~20 kDa observed; 20.16 kDa calculated. Uncharacterized bands may be observed in some lysate(s).
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in mouse retina tissue lysate.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected alpha B-crystallin in mouse retina tissue lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
A monoclonal antibody targeted to the functional peptide of αB-crystallin inhibits the chaperone and anti-apoptotic activities. Nahomi, RB; Nandi, SK; Nagaraj, RH J Immunol Methods
467
37-47
2019
αB-Crystallin is a member of the small heat shock protein family. It is a molecular chaperone and an anti-apoptotic protein. Previous studies have shown that the peptide (73DRFSVNLDVKHFSPEELKVKV93, hereafter referred to as peptain-1) from the core domain of αB-crystallin exhibits both chaperone and anti-apoptotic properties similar to the parent protein. We developed a mouse monoclonal antibody against peptain-1 with the aim of blocking the functions of αB-crystallin. The antibody reacted with peptain-1, it did not react with the chaperone peptide of αA-crystallin. The antibody strongly reacted with human recombinant αB-crystallin but weakly with Hsp20; it did not react with αA-crystallin or Hsp27. The antibody specifically reacted with αB-crystallin in human and mouse lens proteins but not with αA-crystallin. The antibody reacted with αB-crystallin in human lens epithelial cells, human retinal endothelial cells, and with peptain-1 in peptain-1-transduced cells. Unlike the commercial antibodies against αB-crystallin, the antibody against peptain-1 inhibited the chaperone and anti-apoptotic activities of peptain-1. The antibody might find use in inhibiting αB-crystallin's chaperone and anti-apoptotic activities in diseases where αB-crystallin is a causative or contributing factor.