protein

Recombinant Human Thrombospondin-1 protein

MBS1265467

0.05 mg (E-Coli)

165 USD

Recombinant Protein

Recombinant Human Thrombospondin-1 protein

Thrombospondin-1

thrombospondin-1; Thrombospondin-1; thrombospondin-1; thrombospondin 1

THBS1

TSP; TSP1; THBS; THBS-1; TSP-1

THBS1; THBS1; TSP; THBS; TSP1; TSP-1; THBS-1; TSP; TSP1

TSP1_HUMAN

E Coli

19-350

1170

NRIPESGGDNSVFDIFELTGAARKGSGRRLVKGPDPSSP
AFRIEDANLIPPVPDDKFQDLVDAVRAEKGFLLLASLRQ
MKKTRGTLLALERKDHSGQVFSVVSNGKAGTLDLSLTVQ
GKQHVVSVEEALLATGQWKSITLFVQEDRAQLYIDCEKM
ENAELDVPIQSVFTRDLASIARLRIAKGGVNDNFQGVLQ
NVRFVFGTTPEDILRNKGCSSSTSVLLTLDNNVVNGSSP
AIRTNYIGHKTKDLQAICGIS

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Cell Adhesion

Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Binds heparin. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp. Ligand for CD36 mediating antiangiogenic properties. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors.

The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins.Lawler J., Hynes R.O.J. Cell Biol. 103:1635-1648(1986) Complete thrombospondin mRNA sequence includes potential regulatory sites in the 3' untranslated region.Hennessy S.W., Frazier B.A., Kim D.D., Deckwerth T.L., Baumgartel D.M., Rotwein P., Frazier W.A.J. Cell Biol. 108:729-736(1989) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Homo sapiens protein coding cDNA.Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Analysis of the DNA sequence and duplication history of human chromosome 15.Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.Nature 440:671-675(2006) Partial amino acid sequence of human thrombospondin as determined by analysis of cDNA clones homology to malarial circumsporozoite proteins.Kobayashi S., Eden-Mccutchan F., Framson P., Bornstein P.Biochemistry 25:8418-8425(1986) Characterization of a cDNA encoding the heparin and collagen binding domains of human thrombospondin.Dixit V.M., Hennessy S.W., Grant G.A., Rotwein P., Frazier W.A.Proc. Natl. Acad. Sci. U.S.A. 83:5449-5453(1986) Characterization of the promoter region of the human thrombospondin gene. DNA sequences within the first intron increase transcription.Laherty C.D., Gierman T.M., Dixit V.M.J. Biol. Chem. 264:11222-11227(1989) Expression of thrombospondin in chronic inflammation neutrophils from synovial fluids synthesize a novel 3.9 kb TSP mRNA.la Fleur M., Jobin C., Gauthier J., Kreis C.G.Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding.Asch A.S., Silbiger S., Heimer E., Nachman R.L.Biochem. Biophys. Res. Commun. 182:1208-1217(1992) C-mannosylation and O-fucosylation of the thrombospondin type 1 module.Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J., Mosher D.F., Peter-Katalinic J.J. Biol. Chem. 276:6485-6498(2001) Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1.Simantov R., Febbraio M., Crombie R., Asch A.S., Nachman R.L., Silverstein R.L.J. Clin. Invest. 107:45-52(2001) Biophysical characterization, including disulfide bond assignments, of the anti-angiogenic type 1 domains of human thrombospondin-1.Huwiler K.G., Vestling M.M., Annis D.S., Mosher D.F.Biochemistry 41:14329-14339(2002) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.J. Proteome Res. 5:1493-1503(2006) Elucidation of N-glycosylation sites on human platelet proteins a glycoproteomic approach.Lewandrowski U., Moebius J., Walter U., Sickmann A.Mol. Cell. Proteomics 5:226-233(2006) 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) 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) 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 the TSP-1 type 1 repeats a novel layered fold and its biological implication.Tan K., Duquette M., Liu J.-H., Dong Y., Zhang R., Joachimiak A., Lawler J., Wang J.-H.J. Cell Biol. 159:373-382(2002) Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats.Kvansakul M., Adams J.C., Hohenester E.EMBO J. 23:1223-1233(2004) The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin.Tan K., Duquette M., Liu J.-H., Zhang R., Joachimiak A., Wang J.-H., Lawler J.Structure 14:33-42(2006) Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain.Tan K., Duquette M., Liu J.-H., Shanmugasundaram K., Joachimiak A., Gallagher J.T., Rigby A.C., Wang J.-H., Lawler J.J. Biol. Chem. 283:3932-3941(2008)

40317626

NP_003237.2

NM_003246.3

P07996

40kD

Bladder Cancer Pathway (83115); Bladder Cancer Pathway (527); ECM-receptor Interaction Pathway (83068); ECM-receptor Interaction Pathway (479); Extracellular Matrix Organization Pathway (1270244); Focal Adhesion Pathway (198795); Focal Adhesion Pathway (83067); Focal Adhesion Pathway (478); Hemostasis Pathway (1269340); Inflammatory Response Pathway (198766)

The protein encoded by this gene is a subunit of a disulfide-linked homotrimeric protein. This protein is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. This protein can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1. This protein has been shown to play roles in platelet aggregation, angiogenesis, and tumorigenesis. [provided by RefSeq, Jul 2008]

THBS1: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Binds heparin. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp. Ligand for CD36 mediating antiangiogenic properties. Belongs to the thrombospondin family. Protein type: Inhibitor; Motility/polarity/chemotaxis. Chromosomal Location of Human Ortholog: 15q15. Cellular Component: cell surface; endoplasmic reticulum; endoplasmic reticulum lumen; external side of plasma membrane; extracellular matrix; extracellular region; extracellular space; fibrinogen complex; sarcoplasmic reticulum; secretory granule. Molecular Function: calcium ion binding; fibroblast growth factor binding; fibronectin binding; glycoprotein binding; heparin binding; identical protein binding; integrin binding; laminin binding; low-density lipoprotein binding; phosphatidylserine binding; protein binding; proteoglycan binding; transforming growth factor beta binding. Biological Process: activation of MAPK activity; behavioral response to pain; blood coagulation; cell adhesion; cell cycle arrest; cell migration; cellular protein metabolic process; chronic inflammatory response; engulfment of apoptotic cell; extracellular matrix organization and biogenesis; immune response; inflammatory response; negative regulation of angiogenesis; negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; negative regulation of apoptosis; negative regulation of blood vessel endothelial cell migration; negative regulation of caspase activity; negative regulation of cell-matrix adhesion; negative regulation of dendritic cell antigen processing and presentation; negative regulation of endothelial cell proliferation; negative regulation of fibrinolysis; negative regulation of fibroblast growth factor receptor signaling pathway; negative regulation of focal adhesion formation; negative regulation of interleukin-12 production; peptide cross-linking; platelet activation; platelet degranulation; positive regulation of angiogenesis; positive regulation of blood coagulation; positive regulation of blood vessel endothelial cell migration; positive regulation of cell migration; positive regulation of chemotaxis; positive regulation of macrophage activation; positive regulation of phosphorylation; positive regulation of protein kinase B signaling cascade; positive regulation of transforming growth factor beta receptor signaling pathway; positive regulation of transforming growth factor-beta1 production; positive regulation of translation; positive regulation of tumor necrosis factor biosynthetic process; post-translational protein modification; protein amino acid O-linked glycosylation; regulation of cGMP metabolic process; response to calcium ion; response to drug; response to glucose stimulus; response to hypoxia; response to magnesium ion; response to progesterone stimulus; response to unfolded protein; sprouting angiogenesis

0.05 mg (E-Coli)

165 USD

0.2 mg (E-Coli)

275

0.5 mg (E-Coli)

515

1 mg (E-Coli)

755