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444208

Sigma-Aldrich

MMP-1, Proenzyme, Human Rheumatoid Synovial Fibroblast

Synonym(s):

Matrix Metalloproteinase 1, Human Interstitial Collagenase, Collagenase-1

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352202
NACRES:
NA.77

Assay

≥90% (SDS-PAGE)

Quality Level

form

liquid

specific activity

≥15 mU/mg protein

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

foreign activity

other MMP activity, none detected

shipped in

wet ice

storage temp.

−70°C

General description

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.

Packaging

Please refer to vial label for lot-specific concentration.

Warning

Toxicity: Standard Handling (A)

Unit Definition

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.

Physical form

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.

Preparation Note

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).

Other Notes

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.

Legal Information

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

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

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’.

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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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