Products

Biaffin

Newsletter

kinases protein kinase inhibitors signaling activators kinase substrates antibodies bioluminescence assays
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)

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

More details

MM9-H5221-050

Availability: within 7 days

420,00 €

Background
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]

Source
Recombinant human MMP9 Protein (rhMMP9), His Tag (MM9-H5221) is expressed from human 293 cells (HEK293). It contains AA Ala 20 - Pro 469 (Accession # AAH06093).
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.

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

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

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

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

Storage
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.

Bioactivity
Please refer to product data sheet.

Clinical and Translational Updates

(1) "GHRH expression plasmid improves osteoporosis and skin damage in aged mice"
Ye, Wang, Zeng et al
Growth Horm IGF Res (2021) 60-61, 101429
(2) "Arbutin protects brain against middle cerebral artery occlusion-reperfusion (MCAo/R) injury"
Kumar, Singh, Kushwah et al
Biochem Biophys Res Commun (2021) 577, 52-57
(3) "Two-year randomized clinical trial of different restorative techniques in non-carious cervical lesions and MMP activity in gingival crevicular fluid"
Gonçalves, Scaffa, Shinohara et al
Clin Oral Investig (2021)
Showing 1-3 of 32269 papers.
Please refer to product data sheet.