protein

Recombinant Human Matrix Metalloproteinase-2, HEK

MBS145374

0.002 mg

140 USD

Recombinant Protein

Recombinant Human Matrix Metalloproteinase-2, HEK

[Matrix Metalloproteinase-2]

[MMP-2 Human, HEK; Matrix Metalloproteinase-2 Human Recombinant, HEK; 72 kDa type IV collagenase; 72 kDa gelatinase; Gelatinase A; Matrix metalloproteinase-2; MMP-2; TBE-1; MMP2; CLG4A; CLG4; MONA; MMP-II; MMP 2 HEK]

[72 kDa type IV collagenase isoform 2; 72 kDa type IV collagenase; 72 kDa type IV collagenase; collagenase type IV-A; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); matrix metalloproteinase-2; matrix metalloproteinase-II; neutrophil gelatinase; matrix metallopeptidase 2; 72 kDa gelatinase; Gelatinase A; Matrix metalloproteinase-2; MMP-2; TBE-1PEX]

[MMP 2]

[MMP2; MMP2; CLG4; MONA; CLG4A; MMP-2; TBE-1; MMP-II; CLG4A; MMP-2]

MMP2_HUMAN

610

Greater than 95% as determined by SDS-PAGE.

The MMP-2 (0.83 mg/mL) is supplied as a 0.2 um filtered solution in 20mM Tris-HCl, 150mM NaCl and 0.05% Brij 35, pH 7.4.

0.83mg/ml

Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

Source: HEK293 Cells. Physical Appearance: Sterile Filtered colorless solution.

Biological Activity: The activity was measured by its ability to cleave fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH 2 (RND)., The specific activity is > 1,000 pmoles/min/ ug. Recombinant Human MMP-2 protein pro form needs to be activated with p-aminophenylmercuric acetate (APMA). Activation Protocol:. 1. Dilute MMP2 to 100 ug/ml in the Assay Buffer: 50mM Tris, 10mM CaCl 2 , 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5. 2. Activate MMP2 by adding APMA to a final concentration of 1mM. (Sigma) and 100mM stock in DMSO. 3. Incubate at 37°C for 1 hour.

ENZYMES; Enzymes; Matrix Metalloproteinase

Description: MMP-2 Human Recombinant produced in HEK293 cells is a proform of the Human MMP-2 (Ala30-Cys660) and fused with a ployhistide tag at the C-terminus, having an Mw of 71kDa. MMP-2 is purified by proprietary chromatographic techniques. Introduction: Matrix metalloproteinase-2 (MMP-2) is a type IV collagenase, which is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).

189217853

NP_001121363.1

NM_001127891.2

P08253

68,831 Da

AGE/RAGE Pathway (698754); ATF-2 Transcription Factor Network Pathway (138006); Activation Of Matrix Metalloproteinases Pathway (576264); Angiopoietin Receptor Tie2-mediated Signaling Pathway (137917); Axon Guidance Pathway (105688); Bladder Cancer Pathway (83115); Bladder Cancer Pathway (527); Collagen Degradation Pathway (730309); Degradation Of The Extracellular Matrix Pathway (576263); Developmental Biology Pathway (477129)

This gene is a member of the matrix metalloproteinase (MMP) gene family, that are zinc-dependent enzymes capable of cleaving components of the extracellular matrix and molecules involved in signal transduction. The protein encoded by this gene is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. Unlike most MMP family members, activation of this protein can occur on the cell membrane. This enzyme can be activated extracellularly by proteases, or, intracellulary by its S-glutathiolation with no requirement for proteolytical removal of the pro-domain. This protein is thought to be involved in multiple pathways including roles in the nervous system, endometrial menstrual breakdown, regulation of vascularization, and metastasis. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Oct 2014]

MMP2: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly- -Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Interacts (via the C-terminal hemopexin-like domains- containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B. Aspirin appears to inhibit expression. Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. Inhibited by histatin-3 1/24 (histatin-5). Belongs to the peptidase M10A family. Protein type: Protease; Apoptosis; Motility/polarity/chemotaxis; Secreted, signal peptide; Cell development/differentiation; Secreted; EC 3.4.24.24. Chromosomal Location of Human Ortholog: 16q12.2. Cellular Component: proteinaceous extracellular matrix; extracellular space; sarcomere; mitochondrion; plasma membrane; extracellular region; nucleus. Molecular Function: protein binding; zinc ion binding; metalloendopeptidase activity; serine-type endopeptidase activity. Biological Process: collagen catabolic process; extracellular matrix disassembly; axon guidance; extracellular matrix organization and biogenesis; intramembranous ossification; cellular protein metabolic process; positive regulation of innate immune response; response to hypoxia; ephrin receptor signaling pathway; angiogenesis; proteolysis; blood vessel maturation; embryo implantation. Disease: Multicentric Osteolysis, Nodulosis, And Arthropathy

0.002 mg

140 USD

0.01 mg

205

1 mg

4585