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RBBP5 Antibody

Purified Mouse Monoclonal Antibody (Mab)

     
  • 1 - RBBP5 Antibody AP52860
    Western blot detection of RBBP5 in C2C12,THP-1,PC12 and 3T3 cell lysates using RBBP5 mouse mAb (1:1000 diluted).Predicted band size:70KDa.Observed band size:70KDa.
  • 8 - RBBP5 Antibody AP52860
    Immunofluorescent analysis of Hela cells fixed with 4% Paraformaldehyde and using anti-RBBP5 mouse mAb (dilution 1:100). DAPI was used to stain nucleus(blue).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, ICC
Primary Accession Q15291
Reactivity Human, Mouse
Host Mouse
Clonality Monoclonal
Isotype IgG2a
Calculated MW 70 KDa
Additional Information
Other Names RBBP 5; RBBP-5; RBBP5; RBBP5_HUMAN; RBQ 3; RBQ3; Retinoblastoma binding protein 5; Retinoblastoma binding protein RBQ3; Retinoblastoma binding protein5; Retinoblastoma-binding protein 5; Retinoblastoma-binding protein RBQ-3; SWD1; SWD1, Set1c WD40 repeat protein, homolog.
Dilution WB~~1:1000
ICC~~1:100
Format PBS(pH 7.4) containing with 0.02% sodium azide and 50% glycerol.
Storage Store at -20 °C.Stable for 12 months from date of receipt
Protein Information
Name RBBP5
Synonyms RBQ3
Function In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.
Cellular Location Nucleus.
Tissue Location Ubiquitously expressed. EMBL; X85134; CAA59446.1; -; mRNA EMBL; AK290137; BAF82826.1; -; mRNA EMBL; AC093422; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AL583832; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; CH471067; EAW91537.1; -; Genomic_DNA EMBL; CH471067; EAW91538.1; -; Genomic_DNA EMBL; BC037284; AAH37284.1; -; mRNA EMBL; BC053856; AAH53856.1; -; mRNA EMBL; BC075059; AAH75059.1; -; mRNA EMBL; BC075060; AAH75060.1; -; mRNA CCDS; CCDS30983.1; -. [Q15291-1] CCDS; CCDS53463.1; -. [Q15291-2] PIR; A57624; A57624 RefSeq; NP_001180201.1; NM_001193272.1. [Q15291-2] RefSeq; NP_001180202.1; NM_001193273.1 RefSeq; NP_005048.2; NM_005057.3. [Q15291-1] UniGene; Hs.519230; - PDB; 3P4F; X-ray; 2.35 A; B=371-381 PDB; 4X8N; X-ray; 2.10 A; B=347-356 PDB; 4X8P; X-ray; 2.20 A; B=344-355 PDB; 5F6K; X-ray; 2.41 A; D/F=330-356 PDB; 5F6L; X-ray; 1.90 A; J=330-356 PDBsum; 3P4F; - PDBsum; 4X8N; - PDBsum; 4X8P; - PDBsum; 5F6K; - PDBsum; 5F6L; - ProteinModelPortal; Q15291; - SMR; Q15291; - BioGrid; 111864; 89 CORUM; Q15291; - DIP; DIP-29224N; - IntAct; Q15291; 50 MINT; Q15291; - STRING; 9606.ENSP00000264515; - BindingDB; Q15291; - ChEMBL; CHEMBL3137282; - iPTMnet; Q15291; - PhosphoSitePlus; Q15291; - BioMuta; RBBP5; - DMDM; 209572664; - EPD; Q15291; - jPOST; Q15291; - MaxQB; Q15291; - PaxDb; Q15291; - PeptideAtlas; Q15291; - PRIDE; Q15291; - ProteomicsDB; 60517; - ProteomicsDB; 60518; -. [Q15291-2] DNASU; 5929; - Ensembl; ENST00000264515; ENSP00000264515; ENSG00000117222. [Q15291-1] Ensembl; ENST00000367164; ENSP00000356132; ENSG00000117222. [Q15291-2] GeneID; 5929; - KEGG; hsa:5929; - UCSC; uc001hbu.3; human. [Q15291-1] CTD; 5929; - DisGeNET; 5929; - EuPathDB; HostDB:ENSG00000117222.13; - GeneCards; RBBP5; - H-InvDB; HIX0023636; - HGNC; HGNC:9888; RBBP5 HPA; HPA049042; - HPA; HPA058085; - MIM; 600697; gene neXtProt; NX_Q15291; - OpenTargets; ENSG00000117222; - PharmGKB; PA34252; - eggNOG; KOG1273; Eukaryota eggNOG; ENOG410XTA2; LUCA GeneTree; ENSGT00530000064100; - HOVERGEN; HBG054324; - InParanoid; Q15291; - KO; K14961; - OMA; NRLQWNS; - OrthoDB; 1001705at2759; - PhylomeDB; Q15291; - TreeFam; TF313289; - Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex Reactome; R-HSA-3214841; PKMTs methylate histone lysines Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function Reactome; R-HSA-8951664; Neddylation SignaLink; Q15291; - SIGNOR; Q15291; - ChiTaRS; RBBP5; human GeneWiki; RBBP5; - GenomeRNAi; 5929; - PRO; PR:Q15291; - Proteomes; UP000005640; Chromosome 1 Bgee; ENSG00000117222; Expressed in 179 organ(s), highest expression level in buccal mucosa cell ExpressionAtlas; Q15291; baseline and differential Genevisible; Q15291; HS GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB GO; GO:0044666; C:MLL3/4 complex; IDA:UniProtKB GO; GO:0005730; C:nucleolus; IDA:HPA GO; GO:0005654; C:nucleoplasm; TAS:Reactome GO; GO:0005634; C:nucleus; IDA:UniProtKB GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB GO; GO:0043687; P:post-translational protein modification; TAS:Reactome GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome GO; GO:0043627; P:response to estrogen; IDA:UniProtKB Gene3D; 2.130.10.10; -; 1 InterPro; IPR037850; RBBP5/Swd1 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf InterPro; IPR001680; WD40_repeat InterPro; IPR017986; WD40_repeat_dom PANTHER; PTHR44040; PTHR44040; 1 Pfam; PF00400; WD40; 1 SMART; SM00320; WD40; 5 PROSITE; PS50082; WD_REPEATS_2; 1 PROSITE; PS50294; WD_REPEATS_REGION; 1 1: Evidence at protein level; 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation; WD repeat CHAIN 1 538 Retinoblastoma-binding protein 5 /FTId=PRO_0000051194 REPEAT 22 63 WD 1 REPEAT 64 103 WD 2 REPEAT 148 188 WD 3 REPEAT 196 235 WD 4 REPEAT 249 291 WD 5 REPEAT 293 331 WD 6 MOD_RES 252 252 Phosphothreonine; by CDK1 MOD_RES 350 350 Phosphoserine MOD_RES 388 388 Phosphoserine MOD_RES 389 389 Phosphoserine MOD_RES 497 497 Phosphoserine; by CDK1 MOD_RES 525 525 Phosphoserine CROSSLNK 129 129 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) VAR_SEQ 492 529 Missing (in isoform 2) /FTId=VSP_035583 CONFLICT 206 206 F -> Y (in Ref. 2; BAF82826) CONFLICT 244 244 K -> E (in Ref. 1; CAA59446) CONFLICT 351 351 E -> G (in Ref. 1; CAA59446) TURN 349 352 {ECO:0000244|PDB:5F6L} SEQUENCE 538 AA; 59153 MW; 095CCB41613CBED9 CRC64; MNLELLESFG QNYPEEADGT LDCISMALTC TFNRWGTLLA VGCNDGRIVI WDFLTRGIAK IISAHIHPVC SLCWSRDGHK LVSASTDNIV SQWDVLSGDC DQRFRFPSPI LKVQYHPRDQ NKVLVCPMKS APVMLTLSDS KHVVLPVDDD SDLNVVASFD RRGEYIYTGN AKGKILVLKT DSQDLVASFR VTTGTSNTTA IKSIEFARKG SCFLINTADR IIRVYDGREI LTCGRDGEPE PMQKLQDLVN RTPWKKCCFS GDGEYIVAGS ARQHALYIWE KSIGNLVKIL HGTRGELLLD VAWHPVRPII ASISSGVVSI WAQNQVENWS AFAPDFKELD ENVEYEERES EFDIEDEDKS EPEQTGADAA EDEEVDVTSV DPIAAFCSSD EELEDSKALL YLPIAPEVED PEENPYGPPP DAVQTSLMDE GASSEKKRQS SADGSQPPKK KPKTTNIELQ GVPNDEVHPL LGVKGDGKSK KKQAGRPKGS KGKEKDSPFK PKLYKGDRGL PLEGSAKGKV QAELSQPLTA GGAISELL
Research Areas

BACKGROUND

In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.

REFERENCES

Saijo M.,et al.Genomics 27:511-519(1995).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Gregory S.G.,et al.Nature 441:315-321(2006).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Hughes C.M.,et al.Mol. Cell 13:587-597(2004).

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