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BAG4 Antibody (C-term) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession O95429
Clone Names 100528268
Peptide ID 100528268
Additional Information
Other Names BAG family molecular chaperone regulator 4, BAG-4, Bcl-2-associated athanogene 4, Silencer of death domains, BAG4, SODD
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 BAG4
Synonyms SODD
Function Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity). Prevents constitutive TNFRSF1A signaling. Negative regulator of PRKN translocation to damaged mitochondria.
Cellular Location Cytoplasm.
Tissue Location Ubiquitous. EMBL; AF095194; AAD16123.2; -; mRNA EMBL; AF111116; AAD05226.1; -; mRNA EMBL; AK304072; BAG64979.1; -; mRNA EMBL; AC084024; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; BC038505; AAH38505.2; -; mRNA CCDS; CCDS56533.1; -. [O95429-2] CCDS; CCDS6104.1; -. [O95429-1] RefSeq; NP_001191807.1; NM_001204878.1. [O95429-2] RefSeq; NP_004865.1; NM_004874.3. [O95429-1] UniGene; Hs.194726; - PDB; 1M62; NMR; -; A=376-457 PDB; 1M7K; NMR; -; A=358-456 PDBsum; 1M62; - PDBsum; 1M7K; - ProteinModelPortal; O95429; - SMR; O95429; - BioGrid; 114906; 89 IntAct; O95429; 137 MINT; O95429; - STRING; 9606.ENSP00000287322; - iPTMnet; O95429; - PhosphoSitePlus; O95429; - BioMuta; BAG4; - EPD; O95429; - MaxQB; O95429; - PaxDb; O95429; - PeptideAtlas; O95429; - PRIDE; O95429; - ProteomicsDB; 50875; - ProteomicsDB; 50876; -. [O95429-2] DNASU; 9530; - Ensembl; ENST00000287322; ENSP00000287322; ENSG00000156735. [O95429-1] Ensembl; ENST00000432471; ENSP00000393298; ENSG00000156735. [O95429-2] GeneID; 9530; - KEGG; hsa:9530; - UCSC; uc003xky.3; human. [O95429-1] CTD; 9530; - DisGeNET; 9530; - EuPathDB; HostDB:ENSG00000156735.10; - GeneCards; BAG4; - HGNC; HGNC:940; BAG4 HPA; CAB013716; - HPA; HPA018951; - MIM; 603884; gene neXtProt; NX_O95429; - OpenTargets; ENSG00000156735; - PharmGKB; PA25240; - eggNOG; KOG4361; Eukaryota eggNOG; ENOG4111WNH; LUCA GeneTree; ENSGT00530000063256; - HOGENOM; HOG000290673; - HOVERGEN; HBG004809; - InParanoid; O95429; - KO; K09558; - OMA; PAETTWP; - OrthoDB; EOG091G08LY; - PhylomeDB; O95429; - TreeFam; TF102013; - Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response Reactome; R-HSA-5655302; Signaling by FGFR1 in disease Reactome; R-HSA-75893; TNF signaling Reactome; R-HSA-8853336; Signaling by plasma membrane FGFR1 fusions SIGNOR; O95429; - ChiTaRS; BAG4; human EvolutionaryTrace; O95429; - GeneWiki; BAG4; - GenomeRNAi; 9530; - PRO; PR:O95429; - Proteomes; UP000005640; Chromosome 8 Bgee; ENSG00000156735; - CleanEx; HS_BAG4; - ExpressionAtlas; O95429; baseline and differential Genevisible; O95429; HS GO; GO:0005829; C:cytosol; IDA:UniProtKB GO; GO:0005634; C:nucleus; IDA:UniProtKB GO; GO:0005886; C:plasma membrane; IDA:UniProtKB GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; TAS:Reactome GO; GO:0051087; F:chaperone binding; IEA:InterPro GO; GO:0003723; F:RNA binding; HDA:UniProtKB GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc GO; GO:2001145; P:negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:Ensembl GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl GO; GO:0006457; P:protein folding; TAS:ProtInc GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome GO; GO:0097178; P:ruffle assembly; IEA:Ensembl GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome Gene3D;; -; 1 InterPro; IPR036533; BAG_dom_sf InterPro; IPR003103; BAG_domain Pfam; PF02179; BAG; 1 SMART; SM00264; BAG; 1 SUPFAM; SSF63491; SSF63491; 1 PROSITE; PS51035; BAG; 1 1: Evidence at protein level; 3D-structure; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Methylation; Phosphoprotein; Reference proteome CHAIN 1 457 BAG family molecular chaperone regulator 4 /FTId=PRO_0000088870 DOMAIN 379 456 BAG. {ECO:0000255|PROSITE- ProRule:PRU00369} MOD_RES 7 7 Phosphoserine MOD_RES 40 40 Omega-N-methylarginine MOD_RES 53 53 Omega-N-methylarginine MOD_RES 108 108 Omega-N-methylarginine MOD_RES 185 185 Omega-N-methylarginine VAR_SEQ 90 125 Missing (in isoform 2) /FTId=VSP_042741 MUTAGEN 414 414 E->A: Reduces interaction with HSP70 MUTAGEN 424 424 D->A: Abolishes interaction with HSP70 MUTAGEN 438 439 RK->AA: Reduces interaction with HSP70 MUTAGEN 446 446 Q->A: Abolishes interaction with HSP70 HELIX 380 399 {ECO:0000244|PDB:1M62} HELIX 407 423 {ECO:0000244|PDB:1M62} HELIX 432 456 {ECO:0000244|PDB:1M62} SEQUENCE 457 AA; 49594 MW; B89D59E8118684A3 CRC64; MSALRRSGYG PSDGPSYGRY YGPGGGDVPV HPPPPLYPLR PEPPQPPISW RVRGGGPAET TWLGEGGGGD GYYPSGGAWP EPGRAGGSHQ EQPPYPSYNS NYWNSTARSR APYPSTYPVR PELQGQSLNS YTNGAYGPTY PPGPGANTAS YSGAYYAPGY TQTSYSTEVP STYRSSGNSP TPVSRWIYPQ QDCQTEAPPL RGQVPGYPPS QNPGMTLPHY PYGDGNRSVP QSGPTVRPQE DAWASPGAYG MGGRYPWPSS APSAPPGNLY MTESTSPWPS SGSPQSPPSP PVQQPKDSSY PYSQSDQSMN RHNFPCSVHQ YESSGTVNND DSDLLDSQVQ YSAEPQLYGN ATSDHPNNQD QSSSLPEECV PSDESTPPSI KKIIHVLEKV QYLEQEVEEF VGKKTDKAYW LLEEMLTKEL LELDSVETGG QDSVRQARKE AVCKIQAILE KLEKKGL
Research Areas
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BAG4 is a member of theBAG1-related protein family. BAG1 is an anti-apoptotic protein thatfunctions through interactions with a variety of cell apoptosis andgrowth related proteins including BCL-2, Raf-protein kinase,steroid hormone receptors, growth factor receptors and members ofthe heat shock protein 70 kDa family. This protein contains a BAGdomain near the C-terminus, which could bind and inhibit thechaperone activity of Hsc70/Hsp70. This protein was found to beassociated with the death domain of tumor necrosis factor receptortype 1 (TNF-R1) and death receptor-3 (DR3), and thereby negativelyregulates downstream cell death signaling. The regulatory role ofthis protein in cell death was demonstrated in epithelial cellswhich undergo apoptosis while integrin mediated matrix contacts arelost.


Bailey, S.D., et al. Diabetes Care (2010) In press :Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)Tao, H.F., et al. Zhongguo Shi Yan Xue Ye Xue Za Zhi 15(3):501-505(2007)Riley, B.M., et al. Am. J. Med. Genet. A 143A (8), 846-852 (2007) :Yang, Z.Q., et al. Cancer Res. 66(24):11632-11643(2006)

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$ 99.00
Cat# BP16332b
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