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PIPPIN Antibody (Center) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession Q9Y534
Clone Names 80917136
Peptide ID 80917136
Additional Information
Other Names Cold shock domain-containing protein C2, RNA-binding protein PIPPin, CSDC2, PIPPIN
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 CSDC2
Synonyms PIPPIN
Function RNA-binding factor which binds specifically to the very 3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity).
Cellular Location Nucleus. Cytoplasm. Note=PIPPin-RNA complexes are located to the nucleus. EMBL; AB027011; BAA84704.1; -; mRNA EMBL; CR456457; CAG30343.1; -; mRNA EMBL; AL834417; CAD39079.2; -; mRNA EMBL; AL023553; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; BC067113; AAH67113.1; -; mRNA CCDS; CCDS14019.1; - RefSeq; NP_055275.1; NM_014460.3 UniGene; Hs.310893; - ProteinModelPortal; Q9Y534; - SMR; Q9Y534; - BioGrid; 118102; 2 IntAct; Q9Y534; 5 STRING; 9606.ENSP00000302485; - iPTMnet; Q9Y534; - PhosphoSitePlus; Q9Y534; - BioMuta; CSDC2; - DMDM; 32129852; - EPD; Q9Y534; - MaxQB; Q9Y534; - PaxDb; Q9Y534; - PeptideAtlas; Q9Y534; - PRIDE; Q9Y534; - ProteomicsDB; 86281; - DNASU; 27254; - Ensembl; ENST00000306149; ENSP00000302485; ENSG00000172346 GeneID; 27254; - KEGG; hsa:27254; - UCSC; uc003bak.2; human CTD; 27254; - EuPathDB; HostDB:ENSG00000172346.14; - GeneCards; CSDC2; - HGNC; HGNC:30359; CSDC2 HPA; HPA003073; - HPA; HPA076549; - MIM; 617689; gene neXtProt; NX_Q9Y534; - OpenTargets; ENSG00000172346; - PharmGKB; PA142672071; - eggNOG; KOG3070; Eukaryota eggNOG; COG1278; LUCA GeneTree; ENSGT00390000000022; - HOGENOM; HOG000059524; - HOVERGEN; HBG050947; - InParanoid; Q9Y534; - OMA; WPTFPFQ; - OrthoDB; EOG091G0TYX; - PhylomeDB; Q9Y534; - TreeFam; TF324381; - GeneWiki; CSDC2; - GenomeRNAi; 27254; - PRO; PR:Q9Y534; - Proteomes; UP000005640; Chromosome 22 Bgee; ENSG00000172346; - CleanEx; HS_CSDC2; - ExpressionAtlas; Q9Y534; baseline and differential Genevisible; Q9Y534; HS GO; GO:0005737; C:cytoplasm; IBA:GO_Central GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell GO; GO:0003677; F:DNA binding; IEA:InterPro GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central GO; GO:0003723; F:RNA binding; NAS:UniProtKB GO; GO:0008134; F:transcription factor binding; IEA:Ensembl GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro CDD; cd04458; CSP_CDS; 1 InterPro; IPR019844; Cold-shock_CS InterPro; IPR011129; CSD InterPro; IPR002059; CSP_DNA-bd InterPro; IPR012340; NA-bd_OB-fold Pfam; PF00313; CSD; 1 SMART; SM00357; CSP; 1 SUPFAM; SSF50249; SSF50249; 1 PROSITE; PS00352; CSD_1; 1 PROSITE; PS51857; CSD_2; 1 1: Evidence at protein level; Complete proteome; Cytoplasm; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding CHAIN 1 153 Cold shock domain-containing protein C2 /FTId=PRO_0000100351 DOMAIN 68 135 CSD MOD_RES 19 19 Phosphoserine {ECO:0000250|UniProtKB:Q63430} SEQUENCE 153 AA; 16786 MW; F0CB947289356E93 CRC64; MTSESTSPPV VPPLHSPKSP VWPTFPFHRE GSRVWERGGV PPRDLPSPLP TKRTRTYSAT ARASAGPVFK GVCKQFSRSQ GHGFITPENG SEDIFVHVSD IEGEYVPVEG DEVTYKMCPI PPKNQKFQAV EVVLTQLAPH TPHETWSGQV VGS
Research Areas
Citations (0)

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RNA-binding factor which binds specifically to the very 3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity).


Wu, C., et al. Proteomics 7(11):1775-1785(2007)Collins, J.E., et al. Genome Biol. 5 (10), R84 (2004) :Schafer, C., et al. Am. J. Physiol. Gastrointest. Liver Physiol. 285 (4), G726-G734 (2003) :Raimondi, L., et al. J. Cell. Mol. Med. 7(1):35-42(2003)Nastasi, T., et al. Neuroreport 11(10):2233-2236(2000)

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$ 80.00
Cat# BP14318c
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