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Key Documents

444208

Sigma-Aldrich

MMP-1, Proenzyme, Human Rheumatoid Synovial Fibroblast

Synonyme(s) :

Matrix Metalloproteinase 1, Human Interstitial Collagenase, Collagenase-1

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About This Item

Numéro de classification (Commission des enzymes):
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

Pureté

≥90% (SDS-PAGE)

Niveau de qualité

Forme

liquid

Activité spécifique

≥15 mU/mg protein

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze
avoid repeated freeze/thaw cycles

Activité étrangère

other MMP activity, none detected

Conditions d'expédition

wet ice

Température de stockage

−70°C

Description générale

M.W. 56,000/52,000. Note: 1 mU = 1 milliunit.
Native proMMP-1 from cultured, human rheumatoid synovial fibroblast. Corresponds to the 56 kDa/52 kDa enzyme. May contain some activated enzyme but requires APMA (Cat. No. 164610; 30-60 minutes at 37°C, just prior to use) to obtain fully activated enzyme (46 kDa/42 kDa). May also undergo autocatalysis to yield a 27 kDa/22 kDa active enzyme. Expressed by a large number of cell types. Cleaves fibrillar Type I collagen. Must be activated just prior to use.
Native proMMP-1 from cultured, human rheumatoid synovial fibroblast. Corresponds to the 56 kDa/52 kDa enzyme. May contain some activated enzyme but requires activation by APMA (Cat. No. 164610) for 30 - 60 min. at 30°C just prior to use to obtain fully activated enzyme (46 kDa/42 kDa). May also undergo autocatalysis to yield a 27 kDa/22 kDa active enzyme. Expressed by a large number of cell types. Cleaves fibrillar type I collagen.

Conditionnement

Please refer to vial label for lot-specific concentration.

Avertissement

Toxicity: Standard Handling (A)

Définition de l'unité

One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol 2,4-DNP-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min at 37°C pH 7.0.

Forme physique

In 300 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, 1 µM ZnCl₂, 0.05% BRIJ® 35 Detergent, 0.05% NaN₃, pH 7.0.

Notes préparatoires

Prepared from culture medium of human rheumatoid synovial fibroblasts that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Reconstitution

Following initial thaw, aliquot and freeze (-70°C).

Autres remarques

Liepinsh, E., et al. 2003. J. Biol. Chem.278, 25982.
Pilcher, B.K., et al. 1997. J. Cell Biol. 137, 1445.
Vallon, R., et al. 1997. Eur. J. Biochem. 244, 81.
Marcy, A.I., et al. 1991. Biochemistry30, 6476.
Stricklin, et al. 1983. Biochemistry22, 61.

Informations légales

Brij is a registered trademark of Croda International PLC
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Tatiana N Demidova-Rice et al.
Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society, 19(1), 59-70 (2010-12-08)
Studies in our laboratory indicate that collagenase from Clostridium histolyticum promotes endothelial cell and keratinocyte responses to injury in vitro and wound healing in vivo. We postulate that matrix degradation by Clostridial collagenase creates bioactive fragments that can stimulate cellular
Yejiao Shi et al.
Biomaterials science, 7(12), 5132-5142 (2019-10-03)
Matrix metalloproteinases (MMPs) are a family of endopeptidases capable of degrading extracellular matrix (ECM) components. They are known to play crucial roles during the ECM turnover in both physiological and pathological processes. As such, their activities are utilized as biological

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