MMP9 recombinant protein

Recombinant Human MMP9 Protein

Cat. Num. AAA286219

• Gene Names: MMP9; GELB; CLG4B; MMP-9; MANDP2
• Applications: Western Blot, ELISA, SDS-Page
• Purity: > 95% as determined by SDS-PAGE
• Synonyms: MMP9; Recombinant Human MMP9 Protein; GELB; Gelatinase B; CLG4B; CLG4-B; 92 KDa Gelatinase; 92kDa Type IV Collagenase; MMP9 recombinant protein

• Host: E. coli AA 210-346 (P14780).
• Purity/Purification: > 95% as determined by SDS-PAGE
• Form/Format: 58 mM Na₂HPO₄, 17 mM NaH₂PO₄, 68 mM NaCl, 300 mM Imidazole, pH 8.0,with 15% glycerol.
• Concentration: 1 mg/mL (varies by lot)
• Sequence: WSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTAN YDTDDRFGFCPSERLYTRDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYR WCATTANYDRDKLFGFCPTRADSTVMGGNSAGEL
• Sequence Length: 707

• Applicable Applications for MMP9 recombinant protein: Western Blot (WB), ELISA (EIA), SDS-PAGE, Antigen
• Source: Human
• Species: Human
• Protein Residues: with N-terminal 6×His-tag.
• Predicted Molecular Mass: Predicted MW: 21 kDa; Observed MW: 21 kDa
• USAGE: MMP9 Protein-Centrifuge the standard vial at 6000-10000rpm for 30s.
• Preparation and Storage: Store it under sterile conditions at -20°C upon receiving. Recommend to aliquot the protein into smaller quantities for optimal storage.; ; Stability: The recombinant protein is stable for up to 6 months from date of receipt at -80°C.

Testing data TD

(SDS-PAGE)

Related Product Information for MMP9 recombinant protein

MMP-9 (also known as gelatinase B) is secreted as a 92 kDa zymogen. Cleavage of pro-MMP-9 at or near residue 87 results in the active enzyme with a mass of approximately 82 kDa. MMP-9 has three fibronectin type II domains, a hemopexin-like domain and a proline-rich type V collagen-homologous domain. Pro-MMP-9 can be activated by MMP-3 or by certain bacterial proteinases. MMP-9 is inhibited by?2-macroglobulin or by TIMP-1, which binds to pro-MMP-9 as well as to active MMP-9.Pro-MMP-9 is secreted by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts, chondrocytes, skeletal muscle satellite cells, endothelial cells, and various tumor cells. Pro-MMP-9 expression is upregulated by TGF-?1, IL-1?, TGF-?, PDGF-AB.

NCBI and Uniprot Product Information

• NCBI GI #: 74272287
• NCBI GeneID: 4318
• NCBI Accession #: NP_004985.2
• NCBI GenBank Nucleotide #: NM_004994.2
• UniProt Accession #: P14780; Q3LR70; Q8N725; Q9H4Z1; Q9UCJ9; Q9UCL1; Q9UDK2; B2R7V9
• Molecular Weight: 21kDa
• NCBI Official Full Name: matrix metalloproteinase-9 preproprotein
• NCBI Official Synonym Full Names: matrix metallopeptidase 9
• NCBI Official Symbol: MMP9
• NCBI Official Synonym Symbols: GELB; CLG4B; MMP-9; MANDP2
• NCBI Protein Information: matrix metalloproteinase-9
• UniProt Protein Name: Matrix metalloproteinase-9
• Protein Family: Matrix metalloproteinase
• UniProt Gene Name: MMP9
• UniProt Synonym Gene Names: CLG4B; MMP-9; GELB
• UniProt Entry Name: MMP9_HUMAN

NCBI Description

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [provided by RefSeq, Jul 2008]

Uniprot Description

MMP9: May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1. Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. Produced by normal alveolar macrophages and granulocytes. Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. Belongs to the peptidase M10A family.

Protein type: EC 3.4.24.35; Motility/polarity/chemotaxis; Protease; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 20q13.12

Cellular Component: extracellular region; extracellular space

Molecular Function: collagen binding; endopeptidase activity; identical protein binding; metalloendopeptidase activity; metallopeptidase activity; protein binding; serine-type endopeptidase activity; zinc ion binding

Biological Process: collagen catabolic process; ephrin receptor signaling pathway; extracellular matrix disassembly; macrophage differentiation; negative regulation of apoptosis; positive regulation of cell migration; positive regulation of DNA binding; positive regulation of epidermal growth factor receptor signaling pathway; positive regulation of keratinocyte migration; positive regulation of protein amino acid phosphorylation; proteolysis

Disease: Metaphyseal Anadysplasia 2