跳转至内容
Merck
CN

SAE0175

Sigma-Aldrich

MMP-2 pre-activated human

recombinant, ≥1,000 pmol/min/μg, expressed in HEK 293 cells

别名:

72 kDa gelatinase, Gelatinase A, MMP-2, Matrix metalloproteinase-2, TBE-1

登录查看公司和协议定价


About This Item

UNSPSC代码:
12352202
NACRES:
NA.32

重组

expressed in HEK 293 cells

质量水平

比活

≥1000 pmol/min-μg

运输

dry ice

储存温度

−70°C

一般描述

Matrix Metalloproteinase-2 (MMP-2) is a member of the matrix metalloproteinase (MMP) family of proteins. MMPs participate in the breakdown of extracellular matrix in normal physiological processes like embryonic development, reproduction, and tissue remodeling, as well as in disease processes such as arthritis and metastasis. MMP-2 cleaves many substrates, including extracellular matrix components (collagens, fibronectin, and elastin), soluble metabolic mediators (e.g., apolipoproteins), secreted and extracellular matrix-anchored growth factors, and cytokines.

Along with MMP-9, MMP-2 is involved many pathophysiological processes, including leukocyte migration from the circulation into the tissue during inflammation, Chagas′ Cardiomyopathy, heart failure and chronic kidney disease. MMP-2 thus may be regarded as a potential therapeutic target.

As with most MMPs, MMP-2 is secreted as an inactive pro-protein, which becomes activated when cleaved by extracellular proteinases. This product was pre-activated in vitro using 4-aminophenylmercuric acetate (APMA). Thus, it is active and ready for use. The highly toxic APMA was removed from the final preparation.

This product is expressed in human HEK 293 cells as a glycoprotein with a calculated molecular mass of 72 kDa (amino acids 110-660). The DTT-reduced protein migrates as a 75-80 kDa polypeptide on SDS-PAGE because of glycosylation. This protein is produced in human cells, without the use of serum. The human cells expression system allows human like glycosylation and folding, and often supports higher specific activity of the protein. This recombinant protein is expressed without artificial tags.

特点和优势

  • Highly purified protein without artificial fusion tags
  • Expressed in human cells (HEK 293) for proper glycosylation
  • Pre-activated and ready to use
  • High substrate activity

外形

This product is supplied as a 0.22 μm-filtered solution, containing 20 mM Trizma®, pH 7.5, containing 8 mM CaCl2, 119 mM NaCl, 20% glycerol, and 0.05% Brij® 35.

储存及稳定性

Store the product at –70 °C. The product retains its activity for at least 2 years as supplied. After initial thawing, it is recommended to store the protein in working aliquots at –70 °C.

其他说明

This product was pre-activated in vitro using 4-Aminophenylmercuric acetate (APMA). Thus, it is active and ready for use. In order to save our customers from handling hazardous materials, and for environmental saving, the highly toxic and fatal APMA was removed from the final preparation.

法律信息

Brij is a registered trademark of Croda International PLC
Trizma is a registered trademark of Merck KGaA, Darmstadt, Germany

免责声明

This product is for R&D use only. Not for drug, household, or other uses. Please consult the Safety Data Sheet for information regarding hazards and safe handling practices

储存分类代码

12 - Non Combustible Liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

没有发现合适的版本?

如果您需要特殊版本,可通过批号或批次号查找具体证书。

已有该产品?

在文件库中查找您最近购买产品的文档。

访问文档库

M-J Hannocks et al.
Matrix biology : journal of the International Society for Matrix Biology, 75-76, 102-113 (2017-11-22)
This review focuses on the complementary roles of MMP-2 and MMP-9 in leukocyte migration into the brain in neuroinflammation, studied mainly in a murine model of experimental autoimmune encephalomyelitis (EAE) that has similarity to the human disease multiple sclerosis. We
Andrea Page-McCaw et al.
Nature reviews. Molecular cell biology, 8(3), 221-233 (2007-02-24)
Matrix metalloproteinases (MMPs) were discovered because of their role in amphibian metamorphosis, yet they have attracted more attention because of their roles in disease. Despite intensive scrutiny in vitro, in cell culture and in animal models, the normal physiological roles
Rugmani Padmanabhan Iyer et al.
American journal of physiology. Heart and circulatory physiology, 311(1), H190-H198 (2016-05-22)
Following myocardial infarction (MI), the left ventricle (LV) undergoes a series of cardiac wound healing responses that involve both the stimulation of robust inflammation to clear necrotic myocytes and tissue debris and the induction of extracellular matrix (ECM) protein synthesis
Nayara I Medeiros et al.
Frontiers in immunology, 10, 800-800 (2019-05-07)
Background: Chagas cardiomyopathy is the main fibrosing myocarditis among known heart diseases. Development of cardiomyopathy has been related to extracellular matrix (ECM) remodeling, which are controlled by matrix metalloproteinases (MMPs) and cytokines, especially interleukin (IL)-1β. The convertion of 31KDa inactive
Maria Caroline Vos et al.
Reproductive biology and endocrinology : RB&E, 12, 12-12 (2014-02-04)
The aim of this study was to investigate the presence of MMP-14 and MMP-2 during human ovarian follicular development using immunohistochemistry, and the activity of MMP-2 in follicular fluid using zymography. Ovarian tissue collected from the archives of the Department

我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.

联系技术服务部门