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SAE0174

Sigma-Aldrich

MMP-2 human

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

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Synonym(s):
72 kDa gelatinase, Gelatinase A, MMP-2, Matrix metalloproteinase-2, TBE-1

recombinant

expressed in HEK 293 cells

Quality Level

specific activity

≥1000 pmol/min-μg

shipped in

dry ice

storage temp.

−70°C

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vibrant-m

SAE0174

MMP-2 human

vibrant-m

SAE0077

MMP-9 human

vibrant-m

SAE0175

MMP-2 pre-activated human

vibrant-m

SRP6270

MMP-2 human

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

wet ice

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

storage temp.

−70°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

-

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 is not pre-activated, and may be activated by APMA or otherwise

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.

Features and Benefits

  • Highly purified protein without artificial fusion tags
  • Expressed in human cells (HEK 293) for proper glycosylation
  • High substrate activity after activation with APMA or other methods

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.

Storage and Stability

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

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

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
Zhengyuan Cheng et al.
International journal of molecular sciences, 18(4) (2017-04-12)
Gelatinases are members of the matrix metalloproteinase (MMPs) family; they play an important role in the degradation of the extracellular matrix (ECM). This effect is also crucial in the development and progression of chronic kidney disease (CKD). Its expression, as
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
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
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

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