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Recombinant human MMP9 Protein, His tag (active enzyme), 50µg  

Recombinant human MMP9 Protein, His tag (active enzyme), 50µg

Recombinant human MMP9 Protein, Ala20-Pro469, expressed in HEK293 cells, His tag (active enzyme)

recombinant, human, protein, MMP9, CLG4B, GELB, MANDP2, MMP-9, Matrix metallopeptidase 9, matrix metalloproteinase, Gelatinase B

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Availability: within 7 days

420,00 €

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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. Thrombospondins, intervertebral disc proteins, regulate the effective levels of matrix metalloproteinases (MMPs) 2 and 9, which are key effectors of ECM remodeling.[1]
Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), CLG4B, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. . Structurally, MMP9 maybe be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.[2]

Recombinant Human MMP-9, His Tag (MM9-H5221) is expressed from human 293 cells (HEK293). It contains AA Ala 20 - Pro 469 (Accession # AAH06093). It needs to be activated by agents such as APMA in vitro to have hydrolytic activity.
Predicted N-terminus: Ala 20

Molecular Characterization
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 50.8 kDa. The protein migrates as 58-66 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Less than 1.0 EU per μg of the or rhMMP9 by the LAL method.

>90% purity as determined by SDS-PAGE of reduced rhMMP9.

Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.

See Certificate of Analysis for details of reconstitution instruction and specific concentration.

For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
-20°C to -70°C for 12 months in lyophilized state;
-70°C for 3 months under sterile conditions after reconstitution.

Please refer to product data sheet.

Clinical and Translational Updates

(1) "Laminar shear stress inhibits inflammation by activating autophagy in human aortic endothelial cells through HMGB1 nuclear translocation"
Meng, Pu, Qi et al
Commun Biol (2022) 5 (1), 425
(2) "Development of double strand RNA mPEI nanoparticles and application in treating invasive breast cancer"
Liu, Mu, Bai et al
RSC Adv (2019) 9 (23), 13186-13200
(3) "Modified Protocol for Establishment of Intracranial Arterial Dolichoectasia Model by Injection of Elastase Into Cerebellomedullary Cistern in Mice"
Liu, Niu, Zhang et al
Front Neurol (2022) 13, 860541
Showing 1-3 of 33404 papers.