CST, 71630SF, Poly/Mono-ADP Ribose (E6F6A) Rabbit Monoclonal Antibody (BSA and Azide Free)

Monoclonal Antibody for studying . Validated for Western Blotting. Highly specific and rigorously validated in-house, Poly/Mono-ADP Ribose (E6F6A) Rabbit Monoclonal Antibody (BSA and Azide Free) (CST #71630) is ready to ship. Product Usage Information This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us . Optimal dilutions/concentrations should be determined by the end user. BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity. Formulation Supplied in 1X PBS (10 mM Na 2 HPO 4 , 3 mM KCl, 2 mM KH 2 PO 4 , and 140 mM NaCl (pH 7.8)). BSA and Azide Free. Storage Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance. Specificity / Sensitivity Poly/Mono-ADP Ribose (E6F6A) Rabbit Monoclonal Antibody (BSA and Azide Free) recognizes endogenous levels of ADP ribosylated proteins and does not cross-react with other post translational modifications. Species Reactivity: All Species Expected Source / Purification Monoclonal antibody is produced by immunizing animals with KLH modified on lysines with ADP ribose. Background ADP-ribosylation is a post-translational modification that has been described to occur on the side chain of several acceptor residues (lysine, arginine, glutamate, aspartate, cysteine, serine) and protein amino termini as well as on DNA and tRNA (1). ADP-ribosyl transferases (ADPRTs) catalyze the transfer of ADP-ribose from β-NAD and release nicotinamide in the process. Mono-ADP-ribosyl transferases (MARTs, or monoPARPs) comprise the vast majority of the ADPRTs. These monoenzymes, which include the sirtuins and many of the PARP (ARTD) and ART proteins, transfer a single ADP-ribose unit to the target residue (MARylation). The poly-ADP-ribose polymerases (polyPARPs) or polyenzymes, which include human PARP1, 2, 5a and 5b, are the most widely studied and can polymerize linear or branched chains of up to ~200 ADPR units (2). Specificity is determined primarily, but not exclusively, by a nonconsecutive catalytic triad motif, with some exceptions. Those containing the R-S-E motif like Cholera toxin are arginine-directed transferases, while those containing the H-Y-E triad tend to exhibit polymerase activity (3,4). ADP-ribosylation is reversible and can be degraded down to a single ADP-ribose unit by poly-ADP-ribose glycohydrolase (PARG) or ADP-ribosylhydrolase 3 (ARH3) or completely removed from the target residue by ARH1, TARG1, MacroD1 or MacroD2 (5). ADP-ribosylation is involved in a variety of cellular processes, including mitotic spindle formation, chromatin decondensation, cell stress response, retroviral silencing, RNA biology, and transcription, but the most well-known function of ADP-ribose chains is to serve as a scaffold for recruiting DNA repair proteins that contain PAR-binding modules to sites of DNA damage (6). X-ray repair cross-complementing protein 1 (XRCC1), histone macroH2A1, RNF146 (Iduna) an E3 ubiquitin ligase, and many of the PARPs themselves, among others, contain PAR-binding motifs (PBMs) or domains: WWE, PAR-binding zinc-finger (PBZ), or macrodomains (7). PARylation has a central role in cell survival, and is tightly regulated. PARP deficiency can leave a cell vulnerable to DNA damage-induced apoptosis, while hyper PARylation can lead to parthanatos, a unique form of cell death (8). The role of PARylation in DNA repair has inspired great interest in developing candidate drug inhibitors for PARP, in particular to treat breast, prostate and small cell lung cancers with mutations in DNA repair genes like BRCA1/2, CHK2 or ATM. Stat1, PERK, p53, G-actin and Ras are just a few examples of proteins that are functionally modulated by ADP-ribosylation (6,7). Modification by ADP-ribose can block protein interactions or, in the case of P2X7, cause a conformational change that in the presence of ART2 expression sensitizes naive murine T-cells to extracellular NAD leading to apoptosis (9). Specification REACTIVITY: All SENSITIVITY: Endogenous Source/Isotype: Rabbit IgG