Basigin Recombinant Protein | BSG recombinant protein

Recombinant Human Basigin

Cat. Num. AAA953577

• Gene Names: BSG; M6; OK; 5F7; TCSF; CD147; EMMPRIN
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Basigin; Recombinant Human Basigin; 5F7; Collagenase stimulatory factor; Extracellular matrix metalloproteinase inducer; EMMPRIN; Leukocyte activation antigen M6OK blood group antigen; Tumor cell-derived collagenase stimulatory factor; TCSF; CD147; BSG recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 138-321aa; Partial
• Sequence: EPGTVFTTVEDLGSKILLTCSLNDSATEVTGHRWLKGGVVLKEDALPGQKTEFKVDSDDQWGEYSCVFLPEPMGTANIQLHGPPRVKAVKSSEHINEGETAMLVCKSESVPPVTDWAWYKITDSEDKALMNGSESRFFVSSSQGRSELHIENLNMEADPGQYRCNGTSSKGSDQAIITLRVRSH
• Sequence Length: 205

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for BSG recombinant protein

Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to the plasma membrane. Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Ses to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes.

Product Categories/Family for BSG recombinant protein

Cancer

References

Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule.Kasinrerk W., Fiebiger E., Stefanova I., Baumruker T., Knapp W., Stockinger H.J. Immunol. 149:847-854(1992) The basigin group of the immunoglobulin superfamily complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen.Miyauchi T., Masuzawa Y., Muramatsu T.J. Biochem. 110:770-774(1991) The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily.Biswas C., Zhang Y., Decastro R., Guo H., Nakamura T., Kataoka H., Nabeshima K.Cancer Res. 55:434-439(1995) Wakasugi H., Scamps C., Yang G., Vancong N., Bernheim A., Tursz T., Harada N.Decastro R., Zhang Y., Kataoka H., Coon J., Biswas C.Characterization of the gene for human EMMPRIN, a tumor cell surface inducer of matrix metalloproteinases.Guo H., Majmudar G., Jensen T.C., Biswas C., Toole B.P., Gordon M.K.Gene 220:99-108(1998) Regulation of EMMPRIN/CD147 expression and its function of controlling matrix metalloproteinases production and cell-surface localization in co-culture of human uterine cervical carcinoma SKG-II cells and human uterine cervical fibroblasts.Sato T., Takita M., Noguchi Y., Hirata M., Sakai T., Ito A.Kim D., Kanai Y., Choi H., Shin H., Kim J., Teraoka H., Shigeta Y., Chairoungdua A., Babu E., Anzai N., Iribe Y., Endou H.Retina-specific expression of 5A11/Basigin-2, a member of the immunoglobulin gene superfamily.Ochrietor J.D., Moroz T.P., van Ekeris L., Clamp M.F., Jefferson S.C., deCarvalho A.C., Fadool J.M., Wistow G., Muramatsu T., Linser P.J.Invest. Ophthalmol. Vis. Sci. 44:4086-4096(2003) Characterization of basigin isoforms and the inhibitory function of basigin-3 in human hepatocellular carcinoma proliferation and invasion.Liao C.G., Kong L.M., Song F., Xing J.L., Wang L.X., Sun Z.J., Tang H., Yao H., Zhang Y., Wang L., Wang Y., Yang X.M., Li Y., Chen Z.N.Mol. Cell. Biol. 31:2591-2604(2011) The secreted protein discovery initiative (SPDI) , a large-scale effort to identify novel human secreted and transmembrane proteins a bioinformatics assessment.Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.Genome Res. 13:2265-2270(2003) SeattleSNPs variation discovery resourceThe DNA sequence and biology of human chromosome 19.Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.Nature 428:529-535(2004) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Signal peptide prediction based on analysis of experimentally verified cleavage sites.Zhang Z., Henzel W.J.Protein Sci. 13:2819-2824(2004) Partial sequencing and characterization of the tumor cell-derived collagenase stimulatory factor.Nabeshima K., Lane W.S., Biswas C.Arch. Biochem. Biophys. 285:90-96(1991) Basigin (CD147) a multifunctional transmembrane protein involved in reproduction, neural function, inflammation and tumor invasion.Muramatsu T., Miyauchi T.Histol. Histopathol. 18:981-987(2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.Zhang H., Li X.-J., Martin D.B., Aebersold R.Nat. Biotechnol. 21:660-666(2003) Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60.Pushkarsky T., Yurchenko V., Vanpouille C., Brichacek B., Vaisman I., Hatakeyama S., Nakayama K.I., Sherry B., Bukrinsky M.I.J. Biol. Chem. 280:27866-27871(2005) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.J. Proteome Res. 5:3135-3144(2006) The role of charged residues in the transmembrane helices of monocarboxylate transporter 1 and its ancillary protein basigin in determining plasma membrane expression and catalytic activity.Manoharan C., Wilson M.C., Sessions R.B., Halestrap A.P.Mol. Membr. Biol. 23:486-498(2006) junction protein shrew-1 influences cell invasion and interacts with invasion-promoting protein CD147.Schreiner A., Ruonala M., Jakob V., Suthaus J., Boles E., Wouters F., Starzinski-Powitz A.Mol. Biol. Cell 18:1272-1281(2007) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.Nat. Biotechnol. 27:378-386(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Crystal structure of HAb18G/CD147 implications for immunoglobulin superfamily homophilic adhesion.Yu X.-L., Hu T., Du J.-M., Ding J.-P., Yang X.-M., Zhang J., Yang B., Shen X., Zhang Z., Zhong W.-D., Wen N., Jiang H., Zhu P., Chen Z.-N.J. Biol. Chem. 283:18056-18065(2008) Structure of the EMMPRIN N-terminal domain 1 dimerization via beta-strand swapping.Luo J., Teplyakov A., Obmolova G., Malia T., Wu S.-J., Beil E., Baker A., Swencki-Underwood B., Zhao Y., Sprenkle J., Dixon K., Sweet R., Gilliland G.L.Proteins 77:1009-1014(2009) The Ok(a) blood group antigen is a marker for the M6 leukocyte activation antigen, the human homolog of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily molecule that is widely expressed in human cells and tissues.Spring F.A., Holmes C.H., Simpson K.L., Mawby W.J., Mattes M.J., Okubo Y., Parsons S.F.Eur. J. Immunol. 27:891-897(1997) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 38372919
• NCBI GeneID: 682
• NCBI Accession #: NP_001719.2
• NCBI GenBank Nucleotide #: NM_001728.3
• UniProt Accession #: P35613; Q7Z796; Q8IZL7; A6NJW1; D3YLG5
• Molecular Weight: 24.2 kDa
• NCBI Official Full Name: basigin isoform 1
• NCBI Official Synonym Full Names: basigin (Ok blood group)
• NCBI Official Symbol: BSG
• NCBI Official Synonym Symbols: M6; OK; 5F7; TCSF; CD147; EMMPRIN
• NCBI Protein Information: basigin
• UniProt Protein Name: Basigin
• Protein Family: Basigin
• UniProt Gene Name: BSG
• UniProt Synonym Gene Names: EMMPRIN; TCSF
• UniProt Entry Name: BASI_HUMAN

NCBI Description

The protein encoded by this gene is a plasma membrane protein that is important in spermatogenesis, embryo implantation, neural network formation, and tumor progression. The encoded protein is also a member of the immunoglobulin superfamily. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

BSG: Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). May target monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to plasma membranes of retinal pigment epithelium and neural retina. Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes. Enriched on the surface of tumor cells. Up-regulated in gliomas. Its expression levels correlate with malignant potential of the tumor. Forms homooligomers in a cis-dependent manner on the plasma membrane. Forms a complex with MMP1 at the tumor cell surface. Interacts with SLC16A1 and SLC1A3; probably a BSG dimer is associated with a monocarboxylate transporter dimer. Interacts with ATP1B2, MAG and L1CAM. Interacts with AJAP1. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Membrane protein, integral; Immunoglobulin superfamily

Chromosomal Location of Human Ortholog: 19p13.3

Cellular Component: acrosomal membrane; focal adhesion; Golgi membrane; integral to plasma membrane; lipid raft; melanosome; membrane; mitochondrion; plasma membrane; sarcolemma

Molecular Function: mannose binding; protein binding

Biological Process: blood coagulation; cell surface receptor linked signal transduction; cellular metabolic process; decidualization; embryo implantation; extracellular matrix disassembly; extracellular matrix organization and biogenesis; leukocyte migration; odontogenesis of dentine-containing teeth; pyruvate metabolic process; response to cAMP; response to mercury ion; response to peptide hormone stimulus

Disease: Blood Group--ok