跳转至内容
Merck
CN

SAE0175

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 查看组织和合同定价。

选择尺寸


关于此项目

NACRES:
NA.32
UNSPSC Code:
12352202
技术服务
需要帮助?我们经验丰富的科学家团队随时乐意为您服务。
让我们为您提供帮助
技术服务
需要帮助?我们经验丰富的科学家团队随时乐意为您服务。
让我们为您提供帮助

产品名称

MMP-2 pre-activated human, recombinant, ≥1,000 pmol/min/μg, expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

specific activity

≥1000 pmol/min-μg

shipped in

dry ice

storage temp.

−70°C

Quality Level

Disclaimer

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

Features and Benefits

  • 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

General description

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.

Other Notes

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.

Physical form

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.

Preparation Note

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.

Legal Information

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

存储类别

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

常规特殊物品
此项目有

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
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
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
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
Ulrich Eckhard et al.
Matrix biology : journal of the International Society for Matrix Biology, 49, 37-60 (2015-09-27)
Secreted and membrane tethered matrix metalloproteinases (MMPs) are key homeostatic proteases regulating the extracellular signaling and structural matrix environment of cells and tissues. For drug targeting of proteases, selectivity for individual molecules is highly desired and can be met by

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.

联系客户支持