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Goat Anti-SODD Antibody

Peptide-affinity purified goat antibody

     
  • WB - Goat Anti-SODD Antibody AF2023a
    AF2023a (1 µg/ml) staining of HEK293 lysate (35 µg protein in RIPA buffer). Primary incubation was 1 hour. Detected by chemiluminescence.
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB, E
Primary Accession O95429
Other Accession NP_004865, 9530
Reactivity Human
Host Goat
Clonality Polyclonal
Concentration 100ug/200ul
Isotype IgG
Additional Information
Other Names BAG family molecular chaperone regulator 4, BAG-4, Bcl-2-associated athanogene 4, Silencer of death domains, BAG4, SODD
Format 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsGoat Anti-SODD Antibody is for research use only and 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; 1.20.58.120; -; 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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$ 335.00
Cat# AF2023a
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