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SIRPG Antibody (Center) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q9P1W8
Clone Names 100603074
Peptide ID 100603074
Additional Information
Other Names Signal-regulatory protein gamma, SIRP-gamma, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-b2, SIRP-beta-2, CD172g, SIRPG, SIRPB2
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 SIRPG
Synonyms SIRPB2
Function Probable immunoglobulin-like cell surface receptor. On binding with CD47, mediates cell-cell adhesion. Engagement on T- cells by CD47 on antigen-presenting cells results in enhanced antigen-specific T-cell proliferation and costimulates T-cell activation.
Cellular Location Membrane; Single-pass type I membrane protein
Tissue Location Detected in liver, and at very low levels in brain, heart, lung, pancreas, kidney, placenta and skeletal muscle. Expressed on CD4+ T-cells, CD8+ T-cells, CD56-bright natural killer (NK) cells, CD20+ cells, and all activated NK cells. Mainly present in the paracortical T-cell area of lymph nodes, with only sparse positive cells in the mantle and in the germinal center of B-cell follicles. In the thymus, primarily expressed in the medulla on mature T-lymphocytes that have undergone thymic selection. EMBL; AB042624; BAA95692.1; -; mRNA EMBL; AY748247; AAV88530.1; -; mRNA EMBL; AY748248; AAV88531.1; -; mRNA EMBL; AL109809; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AL138804; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; CH471133; EAX10616.1; -; Genomic_DNA EMBL; BC020629; AAH20629.2; -; mRNA EMBL; BC064532; AAH64532.1; -; mRNA CCDS; CCDS13020.2; -. [Q9P1W8-1] CCDS; CCDS13021.2; -. [Q9P1W8-3] CCDS; CCDS33434.1; -. [Q9P1W8-4] RefSeq; NP_001034597.1; NM_001039508.1. [Q9P1W8-4] RefSeq; NP_061026.2; NM_018556.3. [Q9P1W8-1] RefSeq; NP_543006.2; NM_080816.2. [Q9P1W8-3] RefSeq; XP_011527588.1; XM_011529286.2. [Q9P1W8-2] UniGene; Hs.590883; - PDB; 2JJW; X-ray; 1.70 A; A=29-147 PDB; 4I2X; X-ray; 2.48 A; E/F=29-347 PDBsum; 2JJW; - PDBsum; 4I2X; - ProteinModelPortal; Q9P1W8; - SMR; Q9P1W8; - BioGrid; 120664; 3 IntAct; Q9P1W8; 1 STRING; 9606.ENSP00000305529; - iPTMnet; Q9P1W8; - PhosphoSitePlus; Q9P1W8; - BioMuta; SIRPG; - DMDM; 124053651; - EPD; Q9P1W8; - MaxQB; Q9P1W8; - PaxDb; Q9P1W8; - PeptideAtlas; Q9P1W8; - PRIDE; Q9P1W8; - ProteomicsDB; 83672; - ProteomicsDB; 83673; -. [Q9P1W8-2] ProteomicsDB; 83674; -. [Q9P1W8-3] ProteomicsDB; 83675; -. [Q9P1W8-4] DNASU; 55423; - Ensembl; ENST00000216927; ENSP00000216927; ENSG00000089012. [Q9P1W8-4] Ensembl; ENST00000303415; ENSP00000305529; ENSG00000089012. [Q9P1W8-1] Ensembl; ENST00000344103; ENSP00000342759; ENSG00000089012. [Q9P1W8-3] Ensembl; ENST00000381580; ENSP00000370992; ENSG00000089012. [Q9P1W8-2] Ensembl; ENST00000381583; ENSP00000370995; ENSG00000089012. [Q9P1W8-4] GeneID; 55423; - KEGG; hsa:55423; - UCSC; uc002wfm.1; human. [Q9P1W8-1] CTD; 55423; - DisGeNET; 55423; - EuPathDB; HostDB:ENSG00000089012.14; - GeneCards; SIRPG; - HGNC; HGNC:15757; SIRPG MIM; 605466; gene neXtProt; NX_Q9P1W8; - OpenTargets; ENSG00000089012; - PharmGKB; PA38034; - eggNOG; ENOG410IKYM; Eukaryota eggNOG; ENOG410YKK2; LUCA GeneTree; ENSGT00440000033339; - HOVERGEN; HBG056632; - InParanoid; Q9P1W8; - KO; K06551; - OMA; SCESHAF; - OrthoDB; EOG091G05RP; - PhylomeDB; Q9P1W8; - TreeFam; TF341862; - Reactome; R-HSA-202733; Cell surface interactions at the vascular wall Reactome; R-HSA-391160; Signal regulatory protein family interactions EvolutionaryTrace; Q9P1W8; - GeneWiki; SIRPG; - GenomeRNAi; 55423; - PRO; PR:Q9P1W8; - Proteomes; UP000005640; Chromosome 20 Bgee; ENSG00000089012; - CleanEx; HS_SIRPG; - Genevisible; Q9P1W8; HS GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO; GO:0005622; C:intracellular; IEA:GOC GO; GO:0016020; C:membrane; IDA:UniProtKB GO; GO:0005886; C:plasma membrane; TAS:Reactome GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc GO; GO:0050900; P:leukocyte migration; TAS:Reactome GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:UniProtKB GO; GO:0050870; P:positive regulation of T cell activation; IDA:UniProtKB Gene3D; 2.60.40.10; -; 3 InterPro; IPR007110; Ig-like_dom InterPro; IPR036179; Ig-like_dom_sf InterPro; IPR013783; Ig-like_fold InterPro; IPR003597; Ig_C1-set InterPro; IPR003599; Ig_sub InterPro; IPR013106; Ig_V-set Pfam; PF07654; C1-set; 2 Pfam; PF07686; V-set; 1 SMART; SM00409; IG; 2 SMART; SM00407; IGc1; 2 SMART; SM00406; IGv; 1 SUPFAM; SSF48726; SSF48726; 3 PROSITE; PS50835; IG_LIKE; 3 1: Evidence at protein level; 3D-structure; Alternative splicing; Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix SIGNAL 1 28 CHAIN 29 387 Signal-regulatory protein gamma /FTId=PRO_0000014957 TOPO_DOM 29 360 Extracellular. TRANSMEM 361 383 Helical. TOPO_DOM 384 387 Cytoplasmic. DOMAIN 29 137 Ig-like V-type DOMAIN 146 245 Ig-like C1-type 1 DOMAIN 252 340 Ig-like C1-type 2 CARBOHYD 243 243 N-linked (GlcNAc...) asparagine CARBOHYD 268 268 N-linked (GlcNAc...) asparagine CARBOHYD 309 309 N-linked (GlcNAc...) asparagine CARBOHYD 317 317 N-linked (GlcNAc...) asparagine DISULFID 53 119 {ECO:0000255|PROSITE-ProRule:PRU00114, ECO:0000269|PubMed:18657508} DISULFID 168 226 {ECO:0000255|PROSITE-ProRule:PRU00114} DISULFID 271 329 {ECO:0000255|PROSITE-ProRule:PRU00114} VAR_SEQ 1 33 Missing (in isoform 2) /FTId=VSP_007027 VAR_SEQ 144 360 Missing (in isoform 3) /FTId=VSP_007028 VAR_SEQ 250 360 Missing (in isoform 4) /FTId=VSP_026960 VARIANT 263 263 V -> A (in dbSNP:rs6043409) /FTId=VAR_049936 VARIANT 286 286 S -> L (in dbSNP:rs6034239) /FTId=VAR_049937 STRAND 39 43 {ECO:0000244|PDB:2JJW} STRAND 49 51 {ECO:0000244|PDB:2JJW} STRAND 54 56 {ECO:0000244|PDB:2JJW} STRAND 64 71 {ECO:0000244|PDB:2JJW} STRAND 75 82 {ECO:0000244|PDB:2JJW} STRAND 88 92 {ECO:0000244|PDB:2JJW} STRAND 104 106 {ECO:0000244|PDB:2JJW} HELIX 111 113 {ECO:0000244|PDB:2JJW} STRAND 115 123 {ECO:0000244|PDB:2JJW} STRAND 126 128 {ECO:0000244|PDB:4I2X} STRAND 130 134 {ECO:0000244|PDB:2JJW} STRAND 138 142 {ECO:0000244|PDB:2JJW} STRAND 150 152 {ECO:0000244|PDB:4I2X} STRAND 163 176 {ECO:0000244|PDB:4I2X} STRAND 179 184 {ECO:0000244|PDB:4I2X} STRAND 192 197 {ECO:0000244|PDB:4I2X} STRAND 205 214 {ECO:0000244|PDB:4I2X} STRAND 223 229 {ECO:0000244|PDB:4I2X} TURN 231 235 {ECO:0000244|PDB:4I2X} STRAND 238 243 {ECO:0000244|PDB:4I2X} HELIX 244 246 {ECO:0000244|PDB:4I2X} STRAND 253 260 {ECO:0000244|PDB:4I2X} STRAND 262 279 {ECO:0000244|PDB:4I2X} STRAND 281 287 {ECO:0000244|PDB:4I2X} STRAND 297 302 {ECO:0000244|PDB:4I2X} STRAND 308 317 {ECO:0000244|PDB:4I2X} STRAND 326 333 {ECO:0000244|PDB:4I2X} STRAND 339 344 {ECO:0000244|PDB:4I2X} SEQUENCE 387 AA; 42498 MW; 0F5099BE1DE35AC8 CRC64; MPVPASWPHP PGPFLLLTLL LGLTEVAGEE ELQMIQPEKL LLVTVGKTAT LHCTVTSLLP VGPVLWFRGV GPGRELIYNQ KEGHFPRVTT VSDLTKRNNM DFSIRISSIT PADVGTYYCV KFRKGSPENV EFKSGPGTEM ALGAKPSAPV VLGPAARTTP EHTVSFTCES HGFSPRDITL KWFKNGNELS DFQTNVDPTG QSVAYSIRST ARVVLDPWDV RSQVICEVAH VTLQGDPLRG TANLSEAIRV PPTLEVTQQP MRVGNQVNVT CQVRKFYPQS LQLTWSENGN VCQRETASTL TENKDGTYNW TSWFLVNISD QRDDVVLTCQ VKHDGQLAVS KRLALEVTVH QKDQSSDATP GPASSLTALL LIAVLLGPIY VPWKQKT
Research Areas
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Background

The protein encoded by this gene is a member of thesignal-regulatory protein (SIRP) family, and also belongs to theimmunoglobulin superfamily. SIRP family members are receptor-typetransmembrane glycoproteins known to be involved in the negativeregulation of receptor tyrosine kinase-coupled signaling processes.Alternatively spliced transcript variants encoding differentisoforms have been described.

References

Barrett, J.C., et al. Nat. Genet. 41(6):703-707(2009)Kawasaki, M., et al. Clin. Exp. Rheumatol. 27(2):260-266(2009)Stefanidakis, M., et al. Blood 112(4):1280-1289(2008)Lamesch, P., et al. Genomics 89(3):307-315(2007)Barclay, A.N., et al. Nat. Rev. Immunol. 6(6):457-464(2006)

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