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ELISA Kit for Rat Tyrosine-protein phosphatase non-receptor type substrate 1

SKU : BHE13811066

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E9001r
Alternative Names	Brain Ig-like molecule with tyrosine-based activation motifs ; Bit ; CD172 antigen-like family member A ; Inhibitory receptor SHPS-1 ; Macrophage fusion receptor ; Macrophage membrane protein MFP150 ; Signal-regulatory protein alpha-1 ; Sirp-alpha-1 ; CD172a ; Bit ; Mfr ; Ptpns1 ; Shps1 ; Sirp
Categories	Elisa
Function	Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function. Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. May play a role in the release of nitric oxide by macrophages.
Specificity	Natural and recombinant Rat Tyrosine-protein phosphatase non-receptor type substrate 1
Subcellular Location	Membrane Single-pass type I membrane protein
Entryname	SHPS1_RAT
Platform	PF07654
Protein Name	Tyrosine-protein phosphatase non-receptor type substrate 1
Sequence	50: MEPAGPAPGR ; LGPLLFCLLL ; SASCFCAGAS ; GKELKVTQAD ; KSVSVAAGDS ; 100: ATLNCTVSSL ; TPVGPIKWFK ; GEGQNRSPIY ; SFIGGEHFPR ; ITNVSDATKR ; 150: NNMDFSICIS ; NVTPEDAGTY ; YCVKFQKGIV ; EPDTEIKSGG ; GTTLYVLAKP ; 200: SSPEVSGPDS ; RGSPGQTVNF ; TCKSYGFSPR ; NITLKWLKDG ; KELSHLETTI ; 250: SSKSNVSYNI ; SSTVSVKLSP ; EDIHSRVICE ; VAHVTLEGRP ; LNGTANFSNI ; 300: IRVSPTLKIT ; QQPLTPASQV ; NLTCQVQKFY ; PKALQLNWLE ; NGNLSRTDKP ; 350: EHFTDNRDGT ; YNYTSLFLVN ; SSAHREDVVF ; TCQVEHDSQP ; AITENHTVRA ; 400: FAHSSSGGSM ; ETIPDNNAYY ; NWNVFIGVGV ; ACALLVVLLM ; AALYLLRIKQ ; 450: KKAKGSTSST ; RLHEPEKNAR ; EITQIQDTND ; INDITYADLN ; LPKEKKPAPR ; 500: VPEPNNHTEY ; ASIETGKLPR ; PEDTLTYADL ; DMVHLNRAQP ; TPKPEPSFSE ; 509: YASVQVQRK
Sequence Length	509
String	P97710
Sub Unit	Binds PTPN11 when tyrosine-phosphorylated, except in macrophages, where it primarily binds PTPN6. Binds GRB2 in vitro. Binds FGR. Binds JAK2 irrespective of its phosphorylation status and forms a stable complex. Binds SCAP1 and/or SCAP2. The resulting complex recruits FYB. Binds PTK2B.

Uniprot	P97710
Gene Name	Sirpa
Immunogen Species	Rattus norvegicus (Rat)
Kegg	rno:25528
Unigene	Rn.53971

Reference	1. "A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion." Fujioka Y., Matozaki T., Noguchi T., Iwamatsu A., Yamao T., Takahashi N., Tsuda M., Takada T., Kasuga M. Mol. Cell. Biol.16:6887-6899(1996) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 42-60; 68-91; 128-137; 150-158; 174-189; 192-202; 204-212; 218-237; 259-270; 279-282; 405-415 AND 446-453;GLYCOSYLATION;PHOSPHORYLATION AT TYROSINE RESIDUES;INTERACTION WITH PTPN6 AND PTPN11 tissue: Fetal fibroblast. 2. "BIT, an immune antigen receptor-like molecule in the brain." Sano S., Ohnishi H., Omori A., Hasegawa J., Kubota M. FEBS Lett.411:327-334(1997) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 32-48 AND 446-453;FUNCTION;PHOSPHORYLATION AT TYROSINE RESIDUES strain: Sprague-Dawley. tissue: Brain. 3. "MFR, a putative receptor mediating the fusion of macrophages." Saginario C., Sterling H., Beckers C., Kobayashi R., Solimena M., Ullu E., Vignery A. Mol. Cell. Biol.18:6213-6223(1998) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 99-107; 128-149; 192-217; 405-417; 419-429; 446-467 AND 496-506;GLYCOSYLATION;TISSUE SPECIFICITY strain: Fischer 344. tissue: Macrophage. 4. "Signal-regulatory protein is selectively expressed by myeloid and neuronal cells." Adams S., van der Laan L.J.W., Vernon-Wilson E., Renardel de Lavalette C., Doepp E.A., Dijkstra C.D., Simmons D.L., van den Berg T.K. J. Immunol.161:1853-1859(1998) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-419;TISSUE SPECIFICITY strain: WAG/Rij. tissue: Alveolar macrophage. 5. Lubec G., Kang S.U., Lubec S. Submitted (2007-09) to the UniProtKB [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 192-203; 218-226 AND 297-307;IDENTIFICATION BY MASS SPECTROMETRY strain: Sprague-Dawley. tissue: Brain. 6. "Epidermal growth factor stimulates the tyrosine phosphorylation of SHPS-1 and association of SHPS-1 with SHP-2, a SH2 domain-containing protein tyrosine phosphatase." Ochi F., Matozaki T., Noguchi T., Fujioka Y., Yamao T., Takada T., Tsuda M., Takeda H., Fukunaga K., Okabayashi Y., Kasuga M. Biochem. Biophys. Res. Commun.239:483-487(1997) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION IN RESPONSE TO EGF;INTERACTION WITH PTPN11 7. "Roles of the complex formation of SHPS-1 with SHP-2 in insulin-stimulated mitogen-activated protein kinase activation." Takada T., Matozaki T., Takeda H., Fukunaga K., Noguchi T., Fujioka Y., Okazaki I., Tsuda M., Yamao T., Ochi F., Kasuga M. J. Biol. Chem.273:9234-9242(1998) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT TYR-477 AND TYR-501;MUTAGENESIS OF TYR-436; TYR-460; TYR-477 AND TYR-501

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