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BRAND / VENDOR: CST

CST, 9681S, Acetylated-Lysine (Ac-K-103) Mouse Monoclonal Antibody

CATALOG NUMBER: 9681S
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Product Description
Monoclonal Antibody for studying . Validated for Western Blotting,Peptide ELISA (DELFIA). Available in 2 sizes. Highly specific and rigorously validated in-house, Acetylated-Lysine (Ac-K-103) Mouse Monoclonal Antibody (CST #9681) is ready to ship. Product Usage Information Western Blotting: 1:1000 Peptide ELISA (DELFIA): 1:1000 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at -20°C. Do not aliquot the antibody. For a carrier free (BSA and azide free) version of this product see product # 66284 . Protocol Available protocols: Western Blotting Specificity / Sensitivity Acetylated-Lysine (Ac-K-103) Mouse Monoclonal Antibody detects proteins only when posttranslationally modified by acetylation on the epsilon-amine groups of lysine residues. Detection of acetylated lysine by this antibody is largely independent of surrounding amino acid sequence. This antibody has been shown to recognize acetylated proteins including histones, p53, CBP, PCAF and chemically acetylated BSA. Species Reactivity: All Species Expected Source / Purification Monoclonal antibody is produced by immunizing animals with a synthetic acetylated lysine-containing peptide. Background Acetylation of lysine, like phosphorylation of serine, threonine or tyrosine, is an important reversible modification controlling protein activity. The conserved amino-terminal domains of the four core histones (H2A, H2B, H3, and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (1). Signaling resulting in acetylation/deacetylation of histones, transcription factors, and other proteins affects a diverse array of cellular processes including chromatin structure and gene activity, cell growth, differentiation, and apoptosis (2-6). Recent proteomic surveys suggest that acetylation of lysine residues may be a widespread and important form of post-translational protein modification that affects thousands of proteins involved in control of cell cycle and metabolism, longevity, actin polymerization, and nuclear transport (7,8). The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases (9), and HDACs have become promising targets for anti-cancer drugs currently in development (10). Specification REACTIVITY: All SENSITIVITY: Endogenous Source/Isotype: Mouse IgG2a

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