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>   home   >   Products   >   Peptides   >   Blocking Peptides   >   Parp12 Antibody (N-term) Blocking Peptide   

Parp12 Antibody (N-term) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession Q8BZ20
Other Accession NP_766481
Clone Names 71113051
Additional Information
Other Names Poly [ADP-ribose] polymerase 12, PARP-12, ADP-ribosyltransferase diphtheria toxin-like 12, ARTD12, Zinc finger CCCH domain-containing protein 1, Parp12, Zc3hdc1
Target/Specificity The synthetic peptide sequence used to generate the antibody AP6298a was selected from the N-term region of human Parp12. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name Parp12
Synonyms Zc3hdc1
Cellular Location Nucleus. EMBL; AK036886; BAC29622.1; -; mRNA EMBL; CH466533; EDL13617.1; -; Genomic_DNA EMBL; BC120733; AAI20734.1; -; mRNA EMBL; BC137645; AAI37646.1; -; mRNA EMBL; BC024579; AAH24579.1; -; mRNA EMBL; BC028906; AAH28906.1; -; mRNA EMBL; BC048927; AAH48927.1; -; mRNA CCDS; CCDS20019.1; - RefSeq; NP_766481.2; NM_172893.3 UniGene; Mm.268462; - ProteinModelPortal; Q8BZ20; - SMR; Q8BZ20; - BioGrid; 232556; 2 STRING; 10090.ENSMUSP00000039704; - iPTMnet; Q8BZ20; - PhosphoSitePlus; Q8BZ20; - MaxQB; Q8BZ20; - PaxDb; Q8BZ20; - PRIDE; Q8BZ20; - Ensembl; ENSMUST00000038398; ENSMUSP00000039704; ENSMUSG00000038507 GeneID; 243771; - KEGG; mmu:243771; - UCSC; uc009blg.2; mouse CTD; 64761; - MGI; MGI:2143990; Parp12 eggNOG; ENOG410IEI4; Eukaryota eggNOG; ENOG410ZFB8; LUCA GeneTree; ENSGT00760000119084; - HOGENOM; HOG000236279; - HOVERGEN; HBG050384; - InParanoid; Q8BZ20; - KO; K15259; - OMA; IKLHICQ; - OrthoDB; EOG091G14UY; - TreeFam; TF338389; - ChiTaRS; Parp12; mouse PRO; PR:Q8BZ20; - Proteomes; UP000000589; Chromosome 6 Bgee; ENSMUSG00000038507; - CleanEx; MM_PARP12; - Genevisible; Q8BZ20; MM GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-EC Gene3D; 3.30.720.50; -; 1 InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom InterPro; IPR004170; WWE-dom InterPro; IPR037197; WWE_dom_sf InterPro; IPR000571; Znf_CCCH Pfam; PF00644; PARP; 1 Pfam; PF02825; WWE; 1 Pfam; PF00642; zf-CCCH; 1 SMART; SM00356; ZnF_C3H1; 3 SUPFAM; SSF117839; SSF117839; 1 PROSITE; PS51059; PARP_CATALYTIC; 1 PROSITE; PS50918; WWE; 2 PROSITE; PS50103; ZF_C3H1; 4 1: Evidence at protein level; Complete proteome; Metal-binding; NAD; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger CHAIN 1 711 Poly [ADP-ribose] polymerase 12 /FTId=PRO_0000211342 DOMAIN 308 371 WWE 1. {ECO:0000255|PROSITE- ProRule:PRU00248} DOMAIN 374 468 WWE 2. {ECO:0000255|PROSITE- ProRule:PRU00248} DOMAIN 494 708 PARP catalytic. {ECO:0000255|PROSITE- ProRule:PRU00397} ZN_FING 103 128 C3H1-type 1. {ECO:0000255|PROSITE- ProRule:PRU00723} ZN_FING 164 188 C3H1-type 2. {ECO:0000255|PROSITE- ProRule:PRU00723} ZN_FING 189 211 C3H1-type 3. {ECO:0000255|PROSITE- ProRule:PRU00723} ZN_FING 280 307 C3H1-type 4. {ECO:0000255|PROSITE- ProRule:PRU00723} ZN_FING 281 306 C3H1-type 3. {ECO:0000255|PROSITE- ProRule:PRU00723} COMPBIAS 66 70 Poly-Ala MOD_RES 268 268 Phosphoserine CONFLICT 91 91 K -> I (in Ref. 1; BAC29622) CONFLICT 400 400 E -> K (in Ref. 1; BAC29622) SEQUENCE 711 AA; 79917 MW; 5172C6602CDDB4B9 CRC64; MAQAAVAVAE VTQLLCAAGG ALELAELRRR LRTSLGTDAL ERLLRDCGRF VVASRAVVAV GAGREAAAAA SERLVLAVSS LRLCRAHQGP KPGCTGLCAQ LHLCKFLIYG NCKFLKTGKN CRNGHNLKTD HNLSVLRTHG VDHLTYTELC QLLLQNDPSL LPDICLHYNK GDGPFGSCSF QKQCIKLHIC QYFLQGECKF GTSCKRSHEF TNSESLEQLE RLGLSSDLVS RLLSTYRNAY DIKNKGSALS KVSPSPAGPQ GSSERKDSSG PVSPGTPSQE ESEQICLYHI RKSCSFQEKC HRVHFHLPYR WQFLDGGKWK DLDNMELIEE AYSNPSKDRI VYTESAAGFH FDNLDFNSMK FGNTLARRLS TASSVTKPPH FILTTDWIWY WMDEFGSWQE YGRQGSGHPV TTISSSDVER AYLAFCAPGA DAQAATLKFQ AGKHNYELHF KAFLQKNLVY GTIRKVCRRP KYVSPQDVQM KQSCNTKLHG PKSIPDYWDP AALPDLGFKK ITLSSSSEEY QKVWNIFNRT LPFYFVQKIE RIQNMGLWEV YQWQKCQMQK QNGGKEVDER QLFHGTSANF VDAICQQNFD WRVCGLHGTS YGKGSYFARD AAYSHHYSKS DTHSHMMFLA RVLVGDFVRG STSFVRPPAK EGQSNAFYDS CVNSMSDPTI FVVFEKHQVY PEYLIQYSTS SKPPASPSIF VALGNLFTSR Q
Research Areas
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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.


Bailey,P.J., Exp. Cell Res. 312 (16), 3108-3119 (2006)Katoh,M., Int. J. Oncol. 23 (2), 541-547 (2003)

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$ 80.00
Cat# BP6298a
Availability: In Stock
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