MMP-2, Active, Human, Recombinant, CHO Cells

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MMP-2, Active, Human, Recombinant, CHO Cells

市场价：: 0.00

促销价：: ¥0.00

货号：PF023-5UG

品牌：Millipore 密理博

配送至：

北京朝阳

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数量：

EA (预计3-5工作日到货)

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Replacement Information

重要规格表

Description
Overview	Full-length, recombinant, human pro-MMP-2 expressed in mouse cells that is subsequently activated by APMA. APMA is removed through a desalting column. The substrate specificity for MMP-2 includes collagen (types IV, V, VII, and X), elastin, and gelatin (type I). The presence of TIMP-2 inhibitor prevents degradation of the MMP-2 C-terminal regulatory domain. TIMP-2 is also an inhibitor of proteolysis and will inhibit the activity of the enzyme. Useful for immunoblotting, substrate cleavage assay and zymography.
Catalogue Number	PF023
Brand Family	Calbiochem®
Synonyms	Active Matrix Metalloproteinase 2, Gelatinase A

References
References	Liepnisch, E., et al. 2003. J. Biol. Chem. 278, 25982. Parsons, S.L., et al. 1997. Br. J. Surg. 84, 160. Backstrom, J.R., et al. 1996. J. Neuro. 16, 7910. Lim, G.P., et al. 1996. J. Neurochem. 67, 251. Xia, T., et al. 1996. Biochim. Biophys. Acta 1293, 259. Chandler, S., et al. 1995 Neuroscience Letters 201, 226. Sang, Q.X., et al. 1995. Biochim. Biophys. Acta 1251, 99. Kenagy, R.D. and Clowes, A.W. 1994. In Inhibition of Matrix Metalloproteinases: Therapeutic Potential. Greenwald, R.A. and Golub L.M., Eds, 465. Zempo, N., et al. 1994. J. Vasc. Surg. 20, 217. Birkedal-Hansen, H. 1993. J. Periodontol. 64, 484. Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434. Delaisse, J-M. and Vaes, G. 1992. In Biology and Physiology of the Osteoclast. B.R. Rifkin and C.V. Gay, Eds., 290. Jeffrey, J.J. 1992. In Wound Healing: Biochemical and Clinical Aspects. R.F. Diegelmann and W.J. Lindblad, Eds., 194. Jeffrey, J.J. 1991. Semin. Perinatol. 15, 118. Liotta, L.A., et al. 1991. Cell 64, 327. Harris, E. 1990. N. Engl. J. Med. 322, 1277.

References

Liepnisch, E., et al. 2003. J. Biol. Chem. 278, 25982.
Parsons, S.L., et al. 1997. Br. J. Surg. 84, 160.
Backstrom, J.R., et al. 1996. J. Neuro. 16, 7910.
Lim, G.P., et al. 1996. J. Neurochem. 67, 251.
Xia, T., et al. 1996. Biochim. Biophys. Acta 1293, 259.
Chandler, S., et al. 1995 Neuroscience Letters 201, 226.
Sang, Q.X., et al. 1995. Biochim. Biophys. Acta 1251, 99.
Kenagy, R.D. and Clowes, A.W. 1994. In Inhibition of Matrix Metalloproteinases: Therapeutic Potential. Greenwald, R.A. and Golub L.M., Eds, 465.
Zempo, N., et al. 1994. J. Vasc. Surg. 20, 217.
Birkedal-Hansen, H. 1993. J. Periodontol. 64, 484.
Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434.
Delaisse, J-M. and Vaes, G. 1992. In Biology and Physiology of the Osteoclast. B.R. Rifkin and C.V. Gay, Eds., 290.
Jeffrey, J.J. 1992. In Wound Healing: Biochemical and Clinical Aspects. R.F. Diegelmann and W.J. Lindblad, Eds., 194.
Jeffrey, J.J. 1991. Semin. Perinatol. 15, 118.
Liotta, L.A., et al. 1991. Cell 64, 327.
Harris, E. 1990. N. Engl. J. Med. 322, 1277.

Product Information
Activity	ΔΑ₄₀₅/hour/µg protein: ≥ 7.0 in standard thiopeptolide hydrolysis assays.
EC number	3.4.24.24
Form	Liquid
Formulation	In 50 mM HEPES, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ^®-35 Detergent, pH 7.5.
Preservative	None

Applications

Biological Information
Purity	≥90% by SDS-PAGE; contains 9% TIMP-2
Concentration Label	Please refer to vial label for lot-specific concentration

Physicochemical Information

Dimensions

Materials Information

Toxicological Information

Safety Information according to GHS

Safety Information

Product Usage Statements

Storage and Shipping Information
Ship Code	Dry Ice Only
Toxicity	Standard Handling
Storage	≤ -70°C
Avoid freeze/thaw	Avoid freeze/thaw
Do not freeze	Ok to freeze
Special Instructions	Following initial use, aliquot into siliconized vials and freeze (-70°C).