A disintegrin and metalloproteinase with thrombospondin motifs 7 Recombinant Protein | ADAMTS7 recombinant protein

Recombinant Human A disintegrin and metalloproteinase with thrombospondin motifs 7

Cat. Num. AAA1312785

• Gene Names: ADAMTS7; ADAM-TS7; ADAMTS-7; ADAM-TS 7
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: A disintegrin and metalloproteinase with thrombospondin motifs 7; Recombinant Human A disintegrin and metalloproteinase with thrombospondin motifs 7; COMPase; ADAMTS7 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: 242-593aa; Partial
• Sequence: KWVETLVVADAKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHITIVRLVLLEDEEEDLKITHHADNTLKSFCKWQKSINMKGDAHPLHHDTAILLTRKDLCAAMNRPCETLGLSHVAGMCQPHRSCSINEDTGLPLAFTVAHELGHSFGIQHDGSGNDCEPVGKRPFIMSPQLLYDAAPLTWSRCSRQYITRFLDRGWGLCLDDPPAKDIIDFPSVPPGVLYDVSHQCRLQYGAYSAFCEDMDNVCHTLWCSVGTTCHSKLDAAVDGTRCGENKWCLSGECVPVGFRPEAVDGGWSGWSAWSICSRSCGMGVQSAERQCTQPTPKYKGRYCVGERKRFRLCNLQACP

• 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 ADAMTS7 recombinant protein

Metalloprotease that may play a role in the degradation of COMP.

Product Categories/Family for ADAMTS7 recombinant protein

Cell Biology

References

ADAMTS-7 a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein.Liu C.-J., Kong W., Ilalov K., Yu S., Xu K., Prazak L., Fajardo M., Sehgal B., Di Cesare P.E.FASEB J. 20:988-990(2006) ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases.Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.J. Biol. Chem. 274:25555-25563(1999) ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domain.Somerville R.P.T., Longpre J.-M., Apel E.D., Lewis R.M., Wang L.W., Sanes J.R., Leduc R., Apte S.S.J. Biol. Chem. 279:35159-35175(2004)

NCBI and Uniprot Product Information

• NCBI GI #: 38683827
• NCBI GeneID: 11173
• NCBI Accession #: NP_055087.2
• NCBI GenBank Nucleotide #: NM_014272.3
• UniProt Accession #: Q9UKP4; Q14F51; Q6P7J9
• Molecular Weight: 41.1 kDa
• NCBI Official Full Name: A disintegrin and metalloproteinase with thrombospondin motifs 7 preproprotein
• NCBI Official Synonym Full Names: ADAM metallopeptidase with thrombospondin type 1 motif 7
• NCBI Official Symbol: ADAMTS7
• NCBI Official Synonym Symbols: ADAM-TS7; ADAMTS-7; ADAM-TS 7
• NCBI Protein Information: A disintegrin and metalloproteinase with thrombospondin motifs 7
• UniProt Protein Name: A disintegrin and metalloproteinase with thrombospondin motifs 7
• Protein Family: A disintegrin and metalloproteinase with thrombospondin motifs
• UniProt Gene Name: ADAMTS7
• UniProt Synonym Gene Names: ADAM-TS 7; ADAM-TS7; ADAMTS-7
• UniProt Entry Name: ATS7_HUMAN

NCBI Description

The protein encoded by this gene is a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family. Members of this family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The protein encoded by this gene contains two C-terminal TS motifs. [provided by RefSeq, Jul 2008]

Uniprot Description

ADAMTS7: Metalloprotease that may play a role in the degradation of COMP.

Protein type: Motility/polarity/chemotaxis; EC 3.4.24.-; Secreted, signal peptide; Cell surface; Protease; Secreted

Chromosomal Location of Human Ortholog: 15q24.2

Cellular Component: cell surface; endoplasmic reticulum lumen; proteinaceous extracellular matrix

Molecular Function: metalloendopeptidase activity; metallopeptidase activity; protein binding; zinc ion binding

Biological Process: cellular protein metabolic process; negative regulation of chondrocyte differentiation; post-translational protein modification; protein amino acid O-linked glycosylation; proteolysis involved in cellular protein catabolic process