Matrix Metalloproteinase 9 Pro Monomer Active Protein | MMP9 active protein

Matrix Metalloproteinase 9 Pro Monomer (MMP-9, Collagenase 4, Gelatinase B)

Cat. Num. AAA634907

• Gene Names: MMP9; GELB; CLG4B; MMP-9; MANDP2
• Purity: Highly Purified; > 95% of total protein. MMP-9 monomer appears as a major band at 92kD in non-reducing SDS-PAGE.
• Synonyms: Matrix Metalloproteinase 9 Pro Monomer; Matrix Metalloproteinase 9 Pro Monomer (MMP-9; Collagenase 4; Gelatinase B); MMP9 active protein

• Purity/Purification: Highly Purified; > 95% of total protein. MMP-9 monomer appears as a major band at 92kD in non-reducing SDS-PAGE.
• Form/Format: Supplied as a liquid in 50mM Tris-HCl, pH 7.0, 200mM sodium chloride, 5mM CaCl2,,1mM ZnCl2, 0.05% Brij-35, 0.05% sodium azide.

• Specific Activity: The specific activity of activated MMP-9 after trypsin activation is 450mU/mg, where 1U is the activity that hydrolyzes 1umol peptide (7-methoxycoumarin-4-yl) acetyl-Pro-Leu-Gly-Leu-(3-[2, 4- dinitrophenyl]-L-2, 3-diamino-propionyl)- Ala-Arg-NH3 (Mca-Pro-Leu-Gly-Leu-Dpa- Ala-Arg) within 1 minute under the assay conditions described by Knight, et al.
• Preparation and Storage: Aliquot to avoid repeated freezing and thawing, and freeze at -70 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 6 months.

Related Product Information for MMP9 active protein

Human MMP-9 consists of 668aa with a calculated Mrof 76,240D. Due to N- and O-linked glycosylated the Mr in SDS-PAGE is about 92kD. Within the protein sequence, the following structural domains can be distinguished: An N-terminal propeptide, which confers latency to the proenzyme, a Ca2+ and Zn2+ ion-binding catalytic domain containing an insertion of three repeats homologous to type II repeats in the gelatin-binding region of fibronectin, and a C-terminal hemopexin-like domain. Catalytic and hemopexin domains are connected by a proline-rich sequence with homology to sequences in collagens. The gelatin-binding region and the hemopexin domain confer specific macromolecular substrate binding to MMP-9. The hemopexin domain of the latent enzyme binds TIMP-1.

Product Categories/Family for MMP9 active protein

Molecular Biology; MB-Matrix Metalloproteinases

NCBI and Uniprot Product Information

• NCBI GI #: 269849668
• NCBI GeneID: 4318
• UniProt Accession #: P14780; Q3LR70; Q8N725; Q9H4Z1; Q9UCJ9; Q9UCL1; Q9UDK2; B2R7V9
• Molecular Weight: 78,458 Da
• NCBI Official Full Name: Matrix metalloproteinase-9
• NCBI Official Synonym Full Names: matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
• NCBI Official Symbol: MMP9
• NCBI Official Synonym Symbols: GELB; CLG4B; MMP-9; MANDP2
• NCBI Protein Information: matrix metalloproteinase-9; 92 kDa gelatinase; type V collagenase; macrophage gelatinase; 92 kDa type IV collagenase; matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
• 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_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: Secreted; Secreted, signal peptide; Motility/polarity/chemotaxis; Protease; EC 3.4.24.35

Chromosomal Location of Human Ortholog: 20q13.12

Cellular Component: proteinaceous extracellular matrix; extracellular space; 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; skeletal development; leukocyte migration; embryo implantation

Disease: Metaphyseal Anadysplasia 2