MMP-9 Recombinant Protein | MMP9 recombinant protein

MMP-9 Protein, Mouse, Recombinant

Cat. Num. AAA8122822

• Gene Names: Mmp9; Clg4b; MMP-9; B/MMP9; AW743869; pro-MMP-9
• Purity: >85% as determined by SDS-PAGE
• Synonyms: MMP-9; MMP-9 Protein; Mouse; Recombinant; Mouse MMP-9 Protein; AW743869 Protein; B/MMP9 Protein; Clg4b Protein; pro-MMP-9 Protein; matrix metallopeptidase 9; MMP9 recombinant protein

• Host: HEK293 Cells
• Purity/Purification: >85% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Met1-Pro730

• Species: Mouse
• Endotoxin: <1.0EU per ug of the protein as determined by the LAL method
• Predicted N Terminal: Pro 20
• Tag: Native
• Protein Construction: A DNA sequence encoding the mouse MMP9 (P41245-1)(Met 1-Pro 730) was expressed and purified.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

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Related Product Information for MMP9 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 some 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 remodeling 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 on 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. Besides, the dramatic overexpression of MMP-9 in cancer and various inflammatory conditions points to the molecular mechanisms controlling its expression as a potential target for eventual rational therapeutic intervention.

Product Categories/Family for MMP9 recombinant protein

Cancer Drug Targets; IL17 signaling pathway

References

St-Pierre Y, et al. (2003) Emerging features in the regulation of MMP-9 gene expression for the development of novel molecular targets and therapeutic strategies. Curr Drug Targets Inflamm Allergy. 2(3): 206-15.St-Pierre Y, et al. (2004) Regulation of MMP-9 gene expression for the development of novel molecular targets against cancer and inflammatory diseases. Expert Opin Ther Targets. 8(5): 473-89.Chakrabarti S, et al. (2005) Matrix metalloproteinase-2 (MMP-2) and MMP-9 in pulmonary pathology. Exp Lung Res. 31(6): 599-621.

NCBI and Uniprot Product Information

• NCBI GI #: 341940960
• NCBI GeneID: 17395
• UniProt Accession #: P41245; Q06788; Q80XI8; Q9DC02
• Molecular Weight: 80,535 Da
• NCBI Official Full Name: Matrix metalloproteinase-9
• NCBI Official Synonym Full Names: matrix metallopeptidase 9
• NCBI Official Symbol: Mmp9
• NCBI Official Synonym Symbols: Clg4b; MMP-9; B/MMP9; AW743869; pro-MMP-9
• NCBI Protein Information: matrix metalloproteinase-9; GELB; Gel B; gelatinase B; 92kD gelatinase; 92kDa gelatinase; 92 kDa gelatinase; collagenase type IVB; 92kD type IV collagenase; 92kDa type IV collagenase; 92 kDa type IV collagenase; 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_MOUSE

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

Cellular Component: extracellular matrix; extracellular space; proteinaceous extracellular matrix; protein complex; extracellular region

Molecular Function: peptidase activity; identical protein binding; zinc ion binding; hydrolase activity; metallopeptidase activity; fibronectin binding; metal ion binding; metalloendopeptidase activity; endopeptidase activity; protein complex binding

Biological Process: positive regulation of keratinocyte migration; response to drug; ossification; extracellular matrix organization and biogenesis; positive regulation of apoptosis; positive regulation of leukocyte migration; tissue remodeling; positive regulation of synaptic plasticity; proteolysis; protein oligomerization; collagen catabolic process; positive regulation of angiogenesis; negative regulation of fibroblast proliferation; response to oxidative stress; leukocyte migration; skeletal development; embryo implantation; transformation of host cell by virus