This website uses cookies, which are necessary for the technical operation of the website and are always set. Other cookies, which increase the comfort when using this website, are used for direct advertising or to facilitate interaction with other websites and social networks, are only set with your consent.
Configuration
Technically required
These cookies are necessary for the basic functions of the shop.
"Allow all cookies" cookie
"Decline all cookies" cookie
CSRF token
Cookie preferences
Currency change
Customer-specific caching
FACT-Finder tracking
Individual prices
Selected shop
Session
Comfort functions
These cookies are used to make the shopping experience even more appealing, for example for the recognition of the visitor.
Note
Show the facebook fanpage in the right blod sidebar
Statistics & Tracking
Affiliate program
Conversion and usertracking via Google Tag Manager
Product information "Anti-Poly(ADP-ribose) [PAR], clone 10H"
Recognizes poly(ADP-ribose) synthesized by a broad range of PARPs (poly(ADP-ribose) polymerases), including human, mouse, rat or Drosophila PARP enzymes. Liquid. Purified from concentrated hybridoma tissue culture supernatant. Processes such as transcription, repair and replication that require efficient DNA recognition are dependent on modulation of chromatin structure. Chromatin relaxation is a critical event that occurs during DNA repair and is associated with the negatively charged polymer of adenosine 5'-diphosphate (ADP)-ribose (PAR). PAR is synthesized from nicotinamide adenine dinucleotide (NAD+) by the poly(ADP-ribose) polymerase protein family (PARPs), of which PARP-1 (and to a lesser extent PARP-2) respond to DNA-strand breaks. PARP-1 is selectively activated by DNA strand breaks to catalyze the addition of long branched chains of PAR to a variety of nuclear proteins, most notably PARP itself. The amount of PAR formed in living cells with DNA damage is commensurate with the extent of the damage. Under DNA damage conditions, PAR undergoes a rapid turnover, with a half-life in the range of minutes, as PAR is rapidly hydrolyzed and converted to free ADP-ribose by the enzyme poly(ADP-ribose)glycohydrolase (PARG). PAR regulates not only cell survival and cell-death programmes, but also an increasing number of other biological functions with which novel members of the PARP family have been associated. These include transcriptional regulation, cell division, intracellular trafficking, inflammation and energy metabolism.
This website uses cookies, which are necessary for the technical operation of the website and are always set. Other cookies, which increase the usability of this website, serve for direct advertising or simplify interaction with other websites and social networks, will only be used with your consent.
More information