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  MMP-1, Proenzyme, Human Rheumatoid Synovial Fibroblast
Cat. No. 444208  
All Categories » Calbiochem » Proteins and Enzymes » Proteases » Matrix Metalloproteinases (MMP)

Collagenase-1
Human Interstitial Collagenase
Matrix Metalloproteinase 1

Liquid. 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. AVOID FREEZE/THAW CYCLES. 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. Specific activity: ≥15 mU/mg protein. 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. Purity: ≥90% by SDS-PAGE. Contaminants: no other MMP activity detectable. 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. EC 3.4.24.7. M.W. 56,000/52,000. Note: 1 mU = 1 milliunit.

Ref.: 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. Biochemistry 30, 6476. Stricklin, et al. 1983. Biochemistry 22, 61.

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444208: MMP-1, Proenzyme, Human Rheumatoid Synovial Fibroblast - English
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All Categories » Calbiochem » Proteins and Enzymes » Proteases » Matrix Metalloproteinases (MMP)