protein

Recombinant Human MMP-2

MBS695935

0.002 mg

125 USD

Recombinant Protein

Recombinant Human MMP-2

[MMP-2]

[Recombinant Human MMP-2]

[72 kDa type IV collagenase; 72 kDa type IV collagenase; 72 kDa type IV collagenase; collagenase type IV-A; neutrophil gelatinase; matrix metalloproteinase-2; matrix metalloproteinase-II; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); 72 kDa gelatinase; Gelatinase A; Matrix metalloproteinase-2; MMP-2; TBE-1Cleaved into the following chain:PEX]

[MMP-2]

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

MMP2_HUMAN

E.coli

Species Reactivity: Human

MYNFFPRKP KWDKNQITY RIIGYTPDL DPETVDDAF ARAFQVWSD VTPLRFSRI HDGEADIMI NFGRWEHGD GYPFDGKDG LLAHAFAPG TGVGGDSHF DDDELWTLG EGQVVRVKY GNADGEYCK FPFLFNGKE YNSCTDTGR SDGFLWCST TYNFEKDGK YGFCPHEAL FTMGGNAEG QPCKFPFRF QGTSYDSCT TEGRTDGYR WCGTTEDYD RDKKYGFCP ETAMSTVGG NSEGAPCVF PFTFLGNKY ESCTSAGRS DGKMWCATT ANYDDDRKW GFCPDQGYS LFLVAAHEF GHAMGLEHS QDPGALMAP IYTYTKNFR LSQDDIKGI QELYGASPD IDLGTGPTP TLGPVTPEI CKQDIVFDG IAQIRGEIF FFKDRFIWR TVTPRDKPM GPLLVATFW PELPEKIDA VYEAPQEEK AVFFAGNEY WIYSASTLE RGYPKPLTS LGLPPDVQR VDAAFNWSK NKKTYIFAG DKFWRYNEV KKKMDPGFP KLIADAWNA IPDNLDAVV DLQGGGHSY FFKGAYYLK LENQSLKSV KFGSIKSDW LGC

>= 98 by SDS-PAGE gel and HPLC analyses

Sterile filtered through a 0.2 micron filter. Lyophilized from 5mM Sodium Phosphate, pH 7.0 + 0.1 mM Calcium Chloride.

At -20 degree C

Biological Activity: MMP-2 activity was measured by its ability to cleave a chromogenic peptide MMP-2 substrate at room temperature. At an MMP-2 concentration of 2.5 mug/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes. Authenticity: Verified by N-terminal and Mass Spectrometry analyses (when applicable).

Endotoxin: Endotoxin level is <0.1 ng/ug of protein (<1EU/ug. Protein Content: Verified by UV Spectroscopy and/or SDS-PAGE. Reconstitution: Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.5-1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20 degree C to -80 degree C. Country of Origin: USA

Cancer; Angiogenesis; Bone Biology

Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Recombinant human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).

116856

P08253.2

P08253

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: Secreted; Secreted, signal peptide; Protease; EC 3.4.24.24; Motility/polarity/chemotaxis; Apoptosis; Cell development/differentiation. Chromosomal Location of Human Ortholog: 16q12.2. Cellular Component: extracellular space; proteinaceous extracellular matrix; sarcomere; mitochondrion; extracellular region; plasma membrane; nucleus. Molecular Function: protein binding; zinc ion binding; serine-type endopeptidase activity; metalloendopeptidase activity. Biological Process: collagen catabolic process; axon guidance; extracellular matrix disassembly; intramembranous ossification; extracellular matrix organization and biogenesis; 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

125 USD

0.01 mg

195

0.1 mg

840

0.5 mg

2410

1 mg

3960