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SRP6271

Sigma-Aldrich

MMP-9 human

recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

Synonym(s):

CLG4B, GELB, MANDP2, MMP-9, Matrix Metalloproteinase-9

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

recombinant

expressed in HEK 293 cells

tag

6-His tagged (C-terminus)

Assay

≥95% (SDS-PAGE)

form

lyophilized powder

mol wt

calculated mol wt 50.8 kDa
observed mol wt 55-65 kDa (DTT-reduced. Protein migrates due to different glycosylation. Ala 20 is the predicted N-terminus.)

packaging

pkg of 10 and 50 μg

impurities

<1 EU/μg endotoxin (LAL test)

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... MMP-9(4318)

General description

Most MMPs (matrix metalloproteinases) are secreted as inactive pro-proteins which are activated when cleaved by extracellular proteinases. MMP-9, also known as 92kDa type IV collagenase, 92kDa gelatinase/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, MMP-9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline rich linker region, and a carboxyl terminal hemopexin like domain.

Application

MMP-9 human has been used as a standard in gelatin zymography.

Biochem/physiol Actions

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. Studies in rhesus monkeys suggest that MMP-9 is involved in IL-8 (interleukin-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 MMP-2 and -9, which are key effectors of ECM (extracellular matrrix) remodeling. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP-9 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. It is also associated with lumbar-disc herniation and metaphyseal anadysplasia.

Physical form

Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Thrombospondin-1 suppresses spontaneous tumor growth and inhibits activation of matrix metalloproteinase-9 and mobilization of vascular endothelial growth factor.
Rodriguez-Manzaneque JC, et al.
Proceedings of the National Academy of Sciences of the USA, 98, 12485-12490 (2001)
Prevention of interleukin-8-induced mobilization of hematopoietic progenitor cells in rhesus monkeys by inhibitory antibodies against the metalloproteinase gelatinase B (MMP-9).
Pruijt JF, et al.
Proceedings of the National Academy of Sciences of the USA, 96, 10863-10868 (1999)
Lin Liu et al.
Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie, 117, 109096-109096 (2019-06-16)
The distant metastasis in gastric has become an obstacle for treatment in clinic. However, the underlying mechanism is not well illustrated. Here, our aim is to reveal the mechanism and try to explore the potential strategy to overcome the distant
Elevated circulatory MMP-2 and MMP-9 levels and activities in patients with rheumatoid arthritis and systemic lupus erythematosus.
Chang YH, et al.
Clinical Biochemistry, 41, 955-959 (2008)
Orlando Maiorani et al.
Scientific reports, 7, 39974-39974 (2017-01-12)
The extracellular matrix glycoprotein EMILIN1 exerts a wide range of functions mainly associated with its gC1q domain. Besides providing functional significance for adhesion and migration, the direct interaction between α4β1 integrin and EMILIN1-gC1q regulates cell proliferation, transducing net anti-proliferative effects.

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