MMP-9 / CLG4B recombinant protein

Recombinant Human MMP-9 / CLG4B Protein (His tag)

Cat. Num. AAA2546335

• Gene Names: MMP9; GELB; CLG4B; MMP-9; MANDP2
• Purity: > 98 % as determined by SDS-PAGE
• Synonyms: MMP-9 / CLG4B; Recombinant Human MMP-9 / CLG4B Protein (His tag); MMP9; CLG4B; GELB; MMP-9; MMP-9 / CLG4B recombinant protein

• Host: Human Cells
• Purity/Purification: > 98 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 707

• Application Notes: The recombinant human MMP9 consisting of 699 amino acids has a predicted molecular mass of 77.7 kDa. The apparent molecular mass of rhMMP9 is approximately 80-95 kDa in SDS-PAGE due to glycosylation.
• Predicted N Terminal: Ala 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 / CLG4B 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 pro form of human MMP9 enzyme (NP_004985.2) (Met 1-Asp 707) was expressed with a C-terminal polyhistidine tag.

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: 78,458 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: 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; 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