ELISA/assay

Human Matrix metalloproteinase 2/Gelatinase A, MMP-2 ELISA Kit

MBS703890

96 Strip Wells

690 USD

ELISA Kit

Human Matrix metalloproteinase 2/Gelatinase A, MMP-2 ELISA Kit

matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)

Human Matrix metalloproteinase 2/Gelatinase A; MMP-2 ELISA kit; CLG4; CLG4A; MMP-II; MONA; TBE-1; collagenase type IV-A; matrix metalloproteinase 2; matrix metalloproteinase-II; neutrophil gelatinase; matrix metallopeptidase 2 (gelatinase A; 72kDa gelatinase; 72kDa type IV collagenase)

72 kDa type IV collagenase isoform b; 72 kDa type IV collagenase; 72 kDa type IV collagenase; MMP-2; gelatinase A; 72 kDa gelatinase; 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

MMP2

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

MMP2_HUMAN

Human

610

This assay has high sensitivity and excellent specificity for detection of Human MMP2. No significant cross-reactivity or interference between Human MMP2 and analogues was observed.

Unopened test kits should be stored at 2 to 8 degree C upon receipt. Please refer to pdf manual for further storage instructions.

Intra-assay Precision: Intra-assay Precision (Precision within an assay): CV% is less than 8%. Three samples of known concentration were tested twenty times on one plate to assess. Inter-assay Precision (Precision between assays): CV% is less than 10%. Three samples of known concentration were tested in twenty assays to assess. Sample Type: serum, plasma, cell culture supernates, tissue homogenates. Detection Range: 0.78 ng/ml-50 ng/ml. Detection Wavelength: 450 nm. Sensitivity: 0.195 ng/ml

Sample Volume: 50-100ul. Protein Biological Process 1: Angiogenesis. Protein Biological Process 3: Angiogenesis

Introduction: Matrix metalloproteinases (MMPs), also called matrixins, constitute a family of zinc and calcium-dependent endopeptidases that function in the breakdown of extracellular matrix and in the processing of a variety of biological molecules. They play an important role in many normal physiological processes such as embryonic development, morphogenesis, reproduction and tissue remodeling . They also participate in many pathological processes such as arthritis, cancer and cardiovascular disease . While the amounts of newly synthesized MMPs are regulated mainly at the levels of transcription, the proteolytic activities of existing MMPs are controlled through both the activation of proenzymes or zymogens and the inhibition of active enzymes by endogenous inhibitors such as alpha2-macroglobulins and tissue inhibitors of metalloproteinases (TIMPs). MMP-2 (gelatinase A) is primarily expressed in mesenchymal cells (mainly fibroblasts) during development and tissue regeneration. It is highly expressed in stromal cells surrounding the invading front of metastasizing tumors and associated with many connective tissue cells as well as neutrophils, macrophages and monocytes. It is required for the switch to the angiogenic phenotype in a tumor model and its levels are elevated in tumor endothelium and in urine of patients with a variety of cancers. Together with MMP-9 (gelatinase B), it degrades type IV collagen, the major component of basement membranes and gelatin (denatured collagen). It can also degrade other types of collagens (V, VII and X) as well as elastin and fibronectin. It processes many other molecules, modulating their functions in different pathways. Human and mouse MMP-2 are secreted as 72 kDa proenzymes of 631 and 662 amino acids, respectively. The removal of the pro domain can be initiated by membrane-type MMPs or by serine proteases such as thrombin and activated protein C. The resulting mature and active enzyme consists of a catalytic domain, which is interrupted by three contiguous fibronectin type II-like domains, and a C-terminal, hemopexin-like domain. TIMPs inhibit active MMP-2 through tight, but non-covalent binding of their N-terminal domains to the catalytic domain of MMP-2 in a 1:1 stoichiometry. In addition, TIMP-2 can bind to the proenzyme through interaction between the C-terminal domains of both proteins. Principle of the Assay: This assay employs the quantitative sandwich enzyme immunoassay technique. Antibody specific for MMP-2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any MMP-2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for MMP-2 is added to the wells. After washing, avidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of MMP-2 bound in the initial step. The color development is stopped and the intensity of the color is measured.

189217853

NP_001121363.1

NM_001127891.1

P08253

73,882 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

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. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Function: 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. Involved in the formation of the fibrovascular tissues in association with MMP14.8 PublicationsManual assertion based on experiment in:Ref.13. Catalytic activity: Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly- -Ile-Ala-Gly-Gln. Cofactor: Binds 4 calcium ions per subunit. Enzyme regulation: Inhibited by histatin-3 1/24 (histatin-5).1 PublicationManual assertion based on experiment in:Ref.17

96 Strip Wells

690 USD