Parp12 Antibody | 62-235

Parp12 Antibody | 62-235 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human

Homology: N/A

Immunogen: This Parp12 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 454-483 amino acids from the C-terminal region of human Parp12.

Research Area: Other

Tested Application: WB

Application: For WB starting dilution is: 1:1000

Specificiy: N/A

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: 80 kDa

Validation: N/A

Isoform: N/A

Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis

Clonality: Polyclonal

Clone: N/A

Isotype: Rabbit Ig

Conjugate: Unconjugated

Physical State: Liquid

Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.

Concentration: batch dependent

Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Alternate Name: Poly [ADP-ribose] polymerase 12, PARP-12, ADP-ribosyltransferase diphtheria toxin-like 12, ARTD12, Zinc finger CCCH domain-containing protein 1, Parp12, Zc3hdc1

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: Poly (ADP-ribosyl) ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins that contributes to the survival of injured proliferating cells. Poly (ADP-ribose) polymerases (PARPs) now constitute a large family of 18 proteins, encoded by different genes and displaying a conserved catalytic domain in which PARP-1 (113 kDa) , the founding member, and PARP-2 (62 kDa) are so far the sole enzymes whose catalytic activity has been shown to be immediately stimulated by DNA strand breaks. A large repertoire of sequences encoding novel PARPs now extends considerably the field of poly (ADP-ribosyl) ation reactions to various aspects of the cell biology including cell proliferation and cell death. Some of these new members interact with each other, share common partners and common subcellular localizations suggesting possible fine tuning in the regulation of this post-translational modification of proteins.