Metalloproteinase inhibitor 2 Recombinant Protein | TIMP2 recombinant protein

Recombinant Human Metalloproteinase inhibitor 2

Cat. Num. AAA717271

• Gene Names: TIMP2; DDC8; CSC-21K
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Metalloproteinase inhibitor 2; Recombinant Human Metalloproteinase inhibitor 2; CSC-21K; Tissue inhibitor of metalloproteinases 2; TIMP-2; TIMP2 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: 30-220aa; Partial
• Sequence: SPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP
• Sequence Length: 220

• 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 TIMP2 recombinant protein

Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

Product Categories/Family for TIMP2 recombinant protein

Cardiovascular

References

Tissue inhibitor of metalloproteinases-2 (TIMP-2) mRNA expression in tumor cell lines and human tumor tissues.Stetler-Stevenson W.G., Brown P.D., Onisto M., Levy A.T., Liotta L.A.J. Biol. Chem. 265:13933-13938(1990) cDNA cloning and expression of a metalloproteinase inhibitor related to tissue inhibitor of metalloproteinases.Boone T.C., Johnson M.J., de Clerck Y.A., Langley K.E.Proc. Natl. Acad. Sci. U.S.A. 87:2800-2804(1990) Structure and characterization of the human tissue inhibitor of metalloproteinases-2 gene.Hammani K., Blakis A., Morsette D., Bowcock A., Schmutte C., Henriet P., Declerck Y.A.J. Biol. Chem. 271:25498-25505(1996) Malik K., Sejima H., Aoki T., Iwata K.Tissue inhibitor of metalloproteinase (TIMP-2) . A new member of the metalloproteinase inhibitor family.Stetler-Stevenson W.G., Krutzsch H.C., Liotta L.A.J. Biol. Chem. 264:17374-17378(1989) TIMP-2 identification and characterization of a new member of the metalloproteinase inhibitor family.Stetler-Stevenson W.G., Krutzsch H.C., Liotta L.A.Matrix Suppl. 1:299-306(1992) Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.Goldberg G.I., Marmer B.L., Grant G.A., Eisen A.Z., Wilhelm S., He C.Proc. Natl. Acad. Sci. U.S.A. 86:8207-8211(1989) Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid.Osthues A., Knaueper V., Oberhoff R., Reinke H., Tschesche H.FEBS Lett. 296:16-20(1992) Characterization of the promoter of the gene encoding human tissue inhibitor of metalloproteinases-2 (TIMP-2) .de Clerck Y.A., Darville M.I., Eeckhout Y., Rousseau G.G.Gene 139:185-191(1994) Binding of tissue inhibitor of metalloproteinases 2 to two distinct sites on human 72-kDa gelatinase. Identification of a stabilization site.Howard E.W., Banda M.J.J. Biol. Chem. 266:17972-17977(1991) Human cervical tumor cell (SiHa) surface alphavbeta3 integrin receptor has associated matrix metalloproteinase (MMP-2) activity.Chattopadhyay N., Mitra A., Frei E., Chatterjee A.J. Cancer Res. Clin. Oncol. 127:653-658(2001) Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family.Williamson R.A., Martorell G., Carr M.D., Murphy G., Docherty A.J.P., Freedman R.B., Feeney J.Biochemistry 33:11745-11759(1994) High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3.Muskett F.W., Frenkiel T.A., Feeney J., Freedman R.B., Carr M.D., Williamson R.A.J. Biol. Chem. 273:21736-21743(1998) Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1-A resolution.Tuuttila A., Morgunova E., Bergmann U., Lindqvist Y., Maskos K., Fernandez-Catalan C., Bode W., Tryggvason K., Schneider G.J. Mol. Biol. 284:1133-1140(1998) Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.Morgunova E., Tuuttila A., Bergmann U., Tryggvason K.Proc. Natl. Acad. Sci. U.S.A. 99:7414-7419(2002)

NCBI and Uniprot Product Information

• NCBI GI #: 4507511
• NCBI GeneID: 7077
• NCBI Accession #: NP_003246.1
• NCBI GenBank Nucleotide #: NM_003255.4
• UniProt Accession #: P16035; Q16121; Q93006; Q9UDF7
• Molecular Weight: 48.5 kDa
• NCBI Official Full Name: metalloproteinase inhibitor 2
• NCBI Official Synonym Full Names: TIMP metallopeptidase inhibitor 2
• NCBI Official Symbol: TIMP2
• NCBI Official Synonym Symbols: DDC8; CSC-21K
• NCBI Protein Information: metalloproteinase inhibitor 2
• UniProt Protein Name: Metalloproteinase inhibitor 2
• Protein Family: Metalloproteinase inhibitor
• UniProt Gene Name: TIMP2
• UniProt Synonym Gene Names: TIMP-2
• UniProt Entry Name: TIMP2_HUMAN

NCBI Description

This gene is a member of the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. In addition to an inhibitory role against metalloproteinases, the encoded protein has a unique role among TIMP family members in its ability to directly suppress the proliferation of endothelial cells. As a result, the encoded protein may be critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors, and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix. [provided by RefSeq, Jul 2008]

Uniprot Description

TIMP2: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19. Interacts (via the C-terminal) with MMP2 (via the C- terminal PEX domain); the interaction inhibits the MMP2 activity. Down-regulated by TGFB1. Belongs to the protease inhibitor I35 (TIMP) family.

Protein type: Secreted; Inhibitor; Motility/polarity/chemotaxis; Secreted, signal peptide; Extracellular matrix; Cell development/differentiation

Chromosomal Location of Human Ortholog: 17q25

Cellular Component: basement membrane; cell soma; cell surface; extracellular region; extracellular space; growth cone; proteinaceous extracellular matrix

Molecular Function: enzyme activator activity; integrin binding; metal ion binding; metalloendopeptidase inhibitor activity; protease binding; protein binding

Biological Process: aging; central nervous system development; extracellular matrix disassembly; extracellular matrix organization and biogenesis; negative regulation of cell proliferation; negative regulation of membrane protein ectodomain proteolysis; negative regulation of metalloenzyme activity; negative regulation of mitotic cell cycle; negative regulation of Ras protein signal transduction; positive regulation of adenylate cyclase activity; positive regulation of MAPKKK cascade; positive regulation of neuron differentiation; regulation of Rap protein signal transduction; response to cytokine stimulus; response to drug; response to hormone stimulus