The poly (ADP-ribose) polymerase (PARP) is involved in cell recovery from DNA damage, such as methylation of N3-adenine, which activates the base excision repair process. PARP [Poly (ADP-ribose) polymerase] is a 116 kDa nuclear chromatin-associated enzyme that is cleaved during apoptosis by caspase-3 into a 24 kDa fragment containing the DNA binding domain and an 89 kDa fragment containing the catalytic and automodification domains. The 24 kDa-fragment irreversibly bind to DNA and may contribute to the irreversibility of apoptosis by blocking the access of DNA repair enzymes to DNA strand breaks.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
FAQs for PARP Antibody (NBP2-27335). (Showing 1 - 2 of 2 FAQs).
I was wondering if you would mind letting me know which product would you recommend for immunochemistry of the retina of the rat and mouse by poly (ADP-ribose) polymerase (PARP) and calpain. There are many different calpain antibodies in your website. The samples are 12-um vertical cryostst sections (fixed by PFA).
For PARP, I would recommend either NB120-2168 or NB100-64828. Bear in mind that they are both mouse monoclonals, and you may have to take extra steps to reduce mouse-on-mouse background.
Do you have any 100 coda or bigger controls?
I can recommend a couple of high weight antibodies that are conserved in most samples. Please verify the presence of the protein before using as a loading control. PARP1 or PARP is approximately 113kDa, and you may view the products we offer to PARP using this link. Vinculin is approximately 116kDa, and you may view the products we offer to Vinculin using this link.
Caspase 7: The Cell's Suicide Switch Caspase 7 (also known as CASP7, Mch3, ICE-LAP3, CMH-1) is a member of caspase family of cysteine proteases. It is an apoptosis-related cystein peptidase encoded by the CASP7 gene in humans. CASP7 homologous sequences have been identified in nearly all... Read full blog post.
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