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MMP 8 Human

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MMP 8 Human


MMP 8 Human  的詳細(xì)介紹

Catalogue number

ENZ-301

Synonyms

EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL-CL, HNC, CLG1.

Introduction

Full-length recombinant human neutrophil MMP-8, latent form.
Matrix metalloproteinase 8 (MMP-8), degrades interstitial collagens, acting preferentially on collagen type I.
Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.

Description

Matrix Metalloproteinase-8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 75 kDa.
The MMP-8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered clear solution.

Formulation

The MMP-8 protein solution (100 units/ml) in 0.05M Tris-HCl buffer, pH 7.6, 0.2M NaCl, 5mM CaCl2, 0.0025% NaN3 and 0.1% BSA.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
Avoid multiple freeze-thaw cycles.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

100 units/ml after activation with APMA by solution assay method.
One unit of collagenolytic activity is defined as the cleavage of 1μg of collagen per minute by the solution method.

Applications

Used as a standard for analyzing mammalian colagenase activity.

Safety Data Sheet

SDS

Usage

Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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