444208
MMP-1, Proenzyme, Human Rheumatoid Synovial Fibroblast
Synonym(s):
Matrix Metalloproteinase 1, Human Interstitial Collagenase, Collagenase-1
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
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.
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
Takwi Nkyimbeng et al.
PloS one, 8(9), e73279-e73279 (2013-09-12)
Idiopathic pulmonary fibrosis (IPF) is a fatal disease characterized by excessive deposition of extracellular matrix (ECM). We investigated the regulation of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) in lung fibrosis. MMP and TIMP expression, collagenolytic activity and collagen content
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service