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Merck

SRP6271

Sigma-Aldrich

MMP-9 human

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

Synonym(e):

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

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About This Item

UNSPSC-Code:
12352202
NACRES:
NA.32

Biologische Quelle

human

Rekombinant

expressed in HEK 293 cells

Markierung

6-His tagged (C-terminus)

Assay

≥95% (SDS-PAGE)

Form

lyophilized powder

Mol-Gew.

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.)

Verpackung

pkg of 10 and 50 μg

Verunreinigungen

<1 EU/μg endotoxin (LAL test)

UniProt-Hinterlegungsnummer

Versandbedingung

wet ice

Lagertemp.

−20°C

Angaben zum Gen

human ... MMP-9(4318)

Allgemeine Beschreibung

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.

Anwendung

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

Biochem./physiol. Wirkung

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.

Physikalische 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.

Rekonstituierung

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.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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Die Dokumentenbibliothek aufrufen

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)

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