ProMatrix Metalloproteinase-9 Recombinant Protein | ProMMP 9 recombinant protein

Recombinant Human ProMatrix Metalloproteinase-9

Cat. Num. AAA143694

• Gene Names: MMP9; GELB; CLG4B; MMP-9; MANDP2
• Purity: Greater than 95.0% as determined by SDS-PAGE.
• Synonyms: ProMatrix Metalloproteinase-9; Recombinant Human ProMatrix Metalloproteinase-9; Matrix metalloproteinase-9; MMP-9; 92 kDa type IV collagenase; 92 kDa gelatinase; Gelatinase B; GELB; MMP9; CLG4B.; ProMMP 9 recombinant protein

• Host: E Coli
• Purity/Purification: Greater than 95.0% as determined by SDS-PAGE.
• Form/Format: Pro-MMP-9 protein is supplied in 1x PBS and 50% glycerol.
• Sequence Length: 707

• Appearance: Sterile Filtered clear solution
• Preparation and Storage: Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. Please avoid freeze thaw cycles.

Related Product Information for ProMMP 9 recombinant protein

Description: Pro-MMP-9 Human Recombinant produced in E Coli is single, a non-glycosylated, Polypeptide chain containing 688 amino acids fragment (20-707) corresponding to the pro form of the protein minus the signal peptide, having a total molecular mass of 78.59kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Pro-MMP-9 is purified by proprietary chromatographic techniques.

Introduction: Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).

Product Categories/Family for ProMMP 9 recombinant protein

Enzymes; Matrix Metalloproteinase

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; macrophage gelatinase; matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); type V collagenase
• UniProt Protein Name: Matrix metalloproteinase-9
• 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: Protease; EC 3.4.24.35; Motility/polarity/chemotaxis; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 20q13.12

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

Molecular Function: collagen binding; identical protein binding; protein binding; zinc ion binding; metalloendopeptidase activity; endopeptidase activity

Biological Process: positive regulation of keratinocyte migration; collagen catabolic process; axon guidance; extracellular matrix disassembly; ossification; extracellular matrix organization and biogenesis; macrophage differentiation; positive regulation of apoptosis; ephrin receptor signaling pathway; proteolysis; leukocyte migration; skeletal development; embryo implantation

Disease: Metaphyseal Anadysplasia 2