Skip to Content
Merck
All Photos(1)

Key Documents

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

Sign Into View Organizational & Contract Pricing


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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Customers Also Viewed

Immunohistochemical expression of MMP-14 and MMP-2, and MMP-2 activity during human ovarian follicular development.
Vos MC, et al.
Reproductive Biology and Endocrinology, 12, 12-12 (2014)
Andrea Tham et al.
Inhalation toxicology, 29(3), 96-105 (2017-04-18)
Epidemiologic studies have linked inhalation of air pollutants such as ozone to cardiovascular mortality. Human exposure studies have shown that inhalation of ambient levels of ozone causes airway and systemic inflammation and an imbalance in sympathetic/parasympathetic tone. To explore molecular
Matrix metalloproteinases: fold and function of their catalytic domains.
Tallant C, et al.
Biochimica et Biophysica Acta, 1803, 20-28 (2010)
Matrix metalloproteinases: old dogs with new tricks.
Somerville RP, et al.
Genome Biology, 4, 216-216 (2003)
Enhanced expression of MMP-7 and MMP-9 in demyelinating multiple sclerosis lesions.
Cossins JA, et al.
Acta Neuropathologica, 94, 590-598 (1997)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service