MMP-9 recombinant protein

MMP-9; Active; human recombinant

Cat. Num. AAA845563

• Gene Names: MMP9; GELB; CLG4B; MMP-9; MANDP2
• Applications: SDS-Page
• Purity: >=95%
• Synonyms: MMP-9; Active; human recombinant; Matrix Metalloproteinase-9; Gelatinase B; 92 kDa Type IV Collagenase; MMP9; CLG4B; GELB; MANDP2; MMP-9 recombinant protein

• Host: E Coli; Source: Human
• Purity/Purification: >=95%
• Form/Format: Lyophilized from a proprietary buffer
• Sequence Length: 707

• Applicable Applications for MMP-9 recombinant protein: SDS-PAGE
• Tag Information: NT His Tag
• Results: > 70 U/ug
• Unit Definition: One unit (U) of the activity is defined as the amount of enzyme that releases 1 pmole of Mca from Mca-PLGL-Dpa-AR-NH2 per min. at 37 degree C.
• Reconstitution: Reconstitute with pre-chilled 30% Glycerol solution (in dH2O) to 10 U/ul and incubate on ice until it completely dissolves. Aliquot and store the reconstituted MMP-9 at-20 degree C. Stable for 2 months after reconstitution.
• Preparation and Storage: Store at -20 degree C for 12 months.; Centrifuge the vial prior to opening.

Testing Data

Related Product Information for MMP-9 recombinant protein

Matrix metallopeptidase 9 (MMP-9); also known as 92 kDa type IV collagenase; 92 kDa gelatinase or gelatinase B; is the mostly studied MMP; due to its fundamental role in cancer biology; autoimmune disease; and other conditions. This enzyme degrades various substrates including gelatin; collagen types IV and V; and elastin. MMP-9 is structurally a multi-domain metalloenzyme; composed of a prodomain; a catalytic domain; a gelatin binding domain; a metal-binding domain; and a carboxyl terminal hemopexin like domain. This active human MMP-9 is composed of the catalytic domain; a gelatin binding domain; and a metal binding domain (AA 107-457). The protein was expressed in E Coli and purified and refolded using proprietary techniques.

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: 39 kDa (aa 107-457)
• 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
• UniProt Gene Name: MMP9
• UniProt Synonym Gene Names: CLG4B; MMP-9; GELB

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; neutrophil degranulation; 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