Collagenase 3 Recombinant Protein | MMP13 recombinant protein

Recombinant Human Collagenase 3

Cat. Num. AAA114036

• Gene Names: MMP13; CLG3; MANDP1; MMP-13
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Collagenase 3; N/A; Recombinant Human Collagenase 3; Matrix metalloproteinase-13; MMP-13; MMP13 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 104-471. Full Length of Mature Protein
• Sequence: YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPANSILWC

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our or email to for more details.
• 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 MMP13 recombinant protein

Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CTGF. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CTGF. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.

Product Categories/Family for MMP13 recombinant protein

Developmental Biology

References

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Chem. 269:16766-16773(1994) A matrix metalloproteinase gene expressed in human T lymphocytes is identical with collagenase 3 from breast carcinomas.Willmroth F., Peter H.H., Conca W.Immunobiology 198:375-384(1998) 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) NIEHS SNPs program Biochemical characterization of human collagenase-3.Knaeuper V., Lopez-Otin C., Smith B., Knight G., Murphy G.J. Biol. Chem. 271:1544-1550(1996) Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme.Knaeuper V., Will H., Lopez-Otin C., Smith B., Atkinson S.J., Stanton H., Hembry R.M., Murphy G.J. Biol. Chem. 271:17124-17131(1996) Degradation of cartilage aggrecan by collagenase-3 (MMP-13) .Fosang A.J., Last K., Knaeuper V., Murphy G., Neame P.J.FEBS Lett. 380:17-20(1996) Cytokine control of interstitial collagenase and collagenase-3 gene expression in human chondrocytes.Borden P., Solymar D., Sucharczuk A., Lindman B., Cannon P., Heller R.A.J. Biol. Chem. 271:23577-23581(1996) Collagenase-3 (MMP-13) is expressed by hypertrophic chondrocytes, periosteal cells, and osteoblasts during human fetal bone development.Johansson N., Saarialho-Kere U., Airola K., Herva R., Nissinen L., Westermarck J., Vuorio E., Heino J., Kaehaeri V.M.3.0.CO;2-E>Dev. Dyn. 208:387-397(1997) The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction.Knaeuper V., Cowell S., Smith B., Lopez-Otin C., O'Shea M., Morris H., Zardi L., Murphy G.J. Biol. Chem. 272:7608-7616(1997) A secreted tyrosine kinase acts in the extracellular environment.Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr., Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M., Dixon J.E., Yeo C.Y., Whitman M.Cell 158:1033-1044(2014) The helping hand of collagenase-3 (MMP-13) 2.7 A crystal structure of its C-terminal haemopexin-like domain.Gomis-Rueth F.-X., Gohlke U., Betz M., Knaeuper V., Murphy G., Lopez-Otin C., Bode W.J. Mol. Biol. 264:556-566(1996) Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors.Lovejoy B., Welch A.R., Carr S., Luong C., Broka C., Hendricks R.T., Campbell J.A., Walker K.A., Martin R., Van Wart H., Browner M.F.Nat. Struct. Biol. 6:217-221(1999) Solution structure of the catalytic domain of human collagenase-3 (MMP-13) complexed to a potent non-peptidic sulfonamide inhibitor binding comparison with stromelysin-1 and collagenase-1.Zhang X., Gonnella N.C., Koehn J., Pathak N., Ganu V., Melton R., Parker D., Hu S.I., Nam K.Y.J. Mol. Biol. 301:513-524(2000) High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor.Moy F.J., Chanda P.K., Chen J.M., Cosmi S., Edris W., Levin J.I., Powers R.J. Mol. Biol. 302:671-689(2000) Potent pyrimidinetrione-based inhibitors of MMP-13 with enhanced selectivity over MMP-14.Blagg J.A., Noe M.C., Wolf-Gouveia L.A., Reiter L.A., Laird E.R., Chang S.P., Danley D.E., Downs J.T., Elliott N.C., Eskra J.D., Griffiths R.J., Hardink J.R., Haugeto A.I., Jones C.S., Liras J.L., Lopresti-Morrow L.L., Mitchell P.G., Pandit J., Robinson R.P., Subramanyam C., Vaughn-Bowser M.L., Yocum S.A.Bioorg. Med. Chem. Lett. 15:1807-1810(2005) Structural basis for the highly selective inhibition of MMP-13.Engel C.K., Pirard B., Schimanski S., Kirsch R., Habermann J., Klingler O., Schlotte V., Weithmann K.U., Wendt K.U.Chem. Biol. 12:181-189(2005) Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects.Johnson A.R., Pavlovsky A.G., Ortwine D.F., Prior F., Man C.F., Bornemeier D.A., Banotai C.A., Mueller W.T., McConnell P., Yan C., Baragi V., Lesch C., Roark W.H., Wilson M., Datta K., Guzman R., Han H.K., Dyer R.D.J. Biol. Chem. 282:27781-27791(2007) Flexibility and variability of TIMP binding X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2.Maskos K., Lang R., Tschesche H., Bode W.J. Mol. Biol. 366:1222-1231(2007) Discovery of potent, selective, and orally active carboxylic acid based inhibitors of matrix metalloproteinase-13.Monovich L.G., Tommasi R.A., Fujimoto R.A., Blancuzzi V., Clark K., Cornell W.D., Doti R., Doughty J., Fang J., Farley D., Fitt J., Ganu V., Goldberg R., Goldstein R., Lavoie S., Kulathila R., Macchia W., Parker D.T., Melton R., O'Byrne E., Pastor G., Pellas T., Quadros E., Reel N., Roland D.M., Sakane Y., Singh H., Skiles J., Somers J., Toscano K., Wigg A., Zhou S., Zhu L., Shieh W.C., Xue S., McQuire L.W.J. Med. Chem. 52:3523-3538(2009) Discovery of (pyridin-4-yl) -2H-tetrazole as a novel scaffold to identify highly selective matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis.Schnute M.E., O'Brien P.M., Nahra J., Morris M., Howard Roark W., Hanau C.E., Ruminski P.G., Scholten J.A., Fletcher T.R., Hamper B.C., Carroll J.N., Patt W.C., Shieh H.S., Collins B., Pavlovsky A.G., Palmquist K.E., Aston K.W., Hitchcock J., Rogers M.D., McDonald J., Johnson A.R., Munie G.E., Wittwer A.J., Man C.F., Settle S.L., Nemirovskiy O., Vickery L.E., Agawal A., Dyer R.D., Sunyer T.Bioorg. Med. Chem. Lett. 20:576-580(2010) Orally active MMP-1 sparing alpha-tetrahydropyranyl and alpha-piperidinyl sulfone matrix metalloproteinase (MMP) inhibitors with efficacy in cancer, arthritis, and cardiovascular disease.Becker D.P., Barta T.E., Bedell L.J., Boehm T.L., Bond B.R., Carroll J., Carron C.P., Decrescenzo G.A., Easton A.M., Freskos J.N., Funckes-Shippy C.L., Heron M., Hockerman S., Howard C.P., Kiefer J.R., Li M.H., Mathis K.J., McDonald J.J., Mehta P.P., Munie G.E., Sunyer T., Swearingen C.A., Villamil C.I., Welsch D., Williams J.M., Yu Y., Yao J.J. Med. Chem. 53:6653-6680(2010) Simple pseudo-dipeptides with a P2' glutamate a novel inhibitor family of matrix metalloproteases and other metzincins.Devel L., Beau F., Amoura M., Vera L., Cassar-Lajeunesse E., Garcia S., Czarny B., Stura E.A., Dive V.J. Biol. Chem. 287:26647-26656(2012) Hydantoin based inhibitors of MMP13--discovery of AZD6605.De Savi C., Waterson D., Pape A., Lamont S., Hadley E., Mills M., Page K.M., Bowyer J., Maciewicz R.A.Bioorg. Med. Chem. Lett. 23:4705-4712(2013) Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain.Stura E.A., Visse R., Cuniasse P., Dive V., Nagase H.FASEB J. 27:4395-4405(2013) MMP13 mutation causes spondyloepimetaphyseal dysplasia, Missouri type (SEMD(MO) .Kennedy A.M., Inada M., Krane S.M., Christie P.T., Harding B., Lopez-Otin C., Sanchez L.M., Pannett A.A.J., Dearlove A., Hartley C., Byrne M.H., Reed A.A.C., Nesbit M.A., Whyte M.P., Thakker R.V.J. Clin. Invest. 115:2832-2842(2005) Mutations in MMP9 and MMP13 determine the mode of inheritance and the clinical spectrum of metaphyseal anadysplasia.Lausch E., Keppler R., Hilbert K., Cormier-Daire V., Nikkel S., Nishimura G., Unger S., Spranger J., Superti-Furga A., Zabel B.Am. J. Hum. Genet. 85:168-178(2009) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 4505209
• NCBI GeneID: 4322
• NCBI Accession #: NP_002418.1
• NCBI GenBank Nucleotide #: NM_002427.3
• UniProt Accession #: P45452; Q6NWN6; A8K846; B2RCZ3
• Molecular Weight: 58.3 kDa
• NCBI Official Full Name: collagenase 3 preproprotein
• NCBI Official Synonym Full Names: matrix metallopeptidase 13
• NCBI Official Symbol: MMP13
• NCBI Official Synonym Symbols: CLG3; MANDP1; MMP-13
• NCBI Protein Information: collagenase 3
• UniProt Protein Name: Collagenase 3
• UniProt Gene Name: MMP13
• UniProt Synonym Gene Names: MMP-13
• UniProt Entry Name: MMP13_HUMAN