MMP-9 recombinant protein

Recombinant Mouse MMP-9 Protein

Cat. Num. AAA2546916

• Gene Names: Mmp9; Clg4b; Gel B; MMP-9; B/MMP9; AW743869; pro-MMP-9
• Purity: > 95 % as determined by SDS-PAGE
• Synonyms: MMP-9; Recombinant Mouse MMP-9 Protein; RP23-61O3.10-001; AW743869; B/MMP9; Clg4b; pro-MMP-9; MMP-9 recombinant protein

• Host: Human Cells
• Purity/Purification: > 95 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 730

• Application Notes: The secreted pro form of recombinant mouse MMP9 consists of 710 amino acids and has a predicted molecular mass of 78.4 kDa. It migrates as an approximately 100 kDa band in SDS-PAGE under reducing conditions due to glycosylation.
• Predicted N Terminal: Pro 20
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for MMP-9 recombinant protein

Background: Matrix metalloproteinases (MMPs) are neutral proteinases that are involved in the breakdown and remodeling of the extracellular matrix (ECM) under a variety of physiological and pathological conditions, such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. MMP9, also known as 92-kDa gelatinase B/type IV collagenase, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. It plays an important role in tissue remodelling in normal and pathological inflammatory processes. MMP-9 is a major secretion product of macrophages and a component of cytoplasmic granules of neutrophils, and is particularly important in the pathogenesis of inflammatory, infectious, and neoplastic diseases in many organs including the lung. This enzyme is also secreted by lymphocytes and stromal cells upon stimulation by inflammatory cytokines, or upon delivery of bi-directional activation signals following integrin-mediated cell-cell or cell-extracellular matrix (ECM) contacts. Since the integrity of the tissue architecture is closely dependent of the delicate balance between MMPs and their inhibitors, excessive production of MMP-9 is linked to tissue damage and degenerative inflammatory disorders. As a consequence, regulation of gene transcription and tissue-specific expression of MMP-9 in normal and diseased states are being actively investigated to pave the way for new therapeutic targets. In addition, the dramatic overexpression of MMP-9 in cancer and various inflammatory conditions clearly points to the molecular mechanisms controlling its expression as a potential target for eventual rational therapeutic intervention.

Description: A DNA sequence encoding the mouse MMP9 (P41245-1) (Met 1-Pro 730) was expressed and purified.

NCBI and Uniprot Product Information

• NCBI GI #: 7305277
• NCBI GeneID: 17395
• NCBI Accession #: NP_038627.1
• NCBI GenBank Nucleotide #: NM_013599.4
• UniProt Accession #: P41245; Q06788; Q80XI8; Q9DC02
• Molecular Weight: 80,535 Da
• NCBI Official Full Name: matrix metalloproteinase-9 preproprotein
• NCBI Official Synonym Full Names: matrix metallopeptidase 9
• NCBI Official Symbol: Mmp9
• NCBI Official Synonym Symbols: Clg4b; Gel B; MMP-9; B/MMP9; AW743869; pro-MMP-9
• 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

This gene encodes a member of the matrix metalloproteinase family of extracellular matrix-degrading enzymes that are involved in tissue remodeling, wound repair, progression of atherosclerosis and tumor invasion. The encoded preproprotein undergoes proteolytic processing to generate a mature, zinc-dependent endopeptidase enzyme that degrades collagens of type IV, V and XI, and elastin. Mice lacking the encoded protein exhibit an abnormal pattern of skeletal growth plate vascularization and ossification, reduced keratinocyte hyperproliferation at all neoplastic stages, a decreased incidence of invasive tumors, and resistance to experimental autoimmune encephalomyelitis. [provided by RefSeq, Feb 2016]

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: 2 H3|2 85.27 cM

Cellular Component: extracellular space; protein complex

Molecular Function: endopeptidase activity; fibronectin binding; metalloendopeptidase activity; metallopeptidase activity; peptidase activity; protein complex binding; serine-type endopeptidase activity

Biological Process: collagen catabolic process; embryo implantation; extracellular matrix organization and biogenesis; heart development; negative regulation of apoptosis; negative regulation of fibroblast proliferation; positive regulation of angiogenesis; positive regulation of apoptosis; positive regulation of DNA binding; positive regulation of epidermal growth factor receptor signaling pathway; positive regulation of keratinocyte migration; positive regulation of leukocyte migration; positive regulation of protein amino acid phosphorylation; positive regulation of synaptic plasticity; protein oligomerization; proteolysis; response to drug; response to oxidative stress; skeletal development; tissue remodeling; transformation of host cell by virus