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SRP6271

Sigma-Aldrich

MMP-9 human

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

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in HEK 293 cells

Étiquette/Marqueur

6-His tagged (C-terminus)

Pureté

≥95% (SDS-PAGE)

Forme

lyophilized powder

Poids mol.

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.)

Conditionnement

pkg of 10 and 50 μg

Impuretés

<1 EU/μg endotoxin (LAL test)

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

human ... MMP-9(4318)

Description générale

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.

Actions biochimiques/physiologiques

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.

Forme physique

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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Enhanced expression of MMP-7 and MMP-9 in demyelinating multiple sclerosis lesions.
Cossins JA, et al.
Acta Neuropathologica, 94, 590-598 (1997)
Shimin Zhang et al.
Theriogenology, 151, 144-150 (2020-04-29)
Successful implantation is closely linked to the expression of MMP-2 and MMP-9, which greatly influence the ability of an embryo to degrade the basement membrane of the uterine epithelium, mainly composed of type IV collagen, and invade the uterine stroma.
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)
Matrix metalloproteinases: fold and function of their catalytic domains.
Tallant C, et al.
Biochimica et Biophysica Acta, 1803, 20-28 (2010)
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

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