MMP-9, Proenzyme, Human, Recombinant, CHO Cells

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MMP-9, Proenzyme, Human, Recombinant, CHO Cells

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货号：PF038-10UG

品牌：Millipore 密理博

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Replacement Information

重要规格表

Description
Overview	Recombinant, human pro-MMP-9 expressed in CHO cells. A portion (less than 10%) of the enzyme may be seen as a naturally-occurring dimer. Dimerization does not interfere with activation. May contain up to 10% TIMP proteins. During storage, a small portion (less than 10%) of the enzyme may also become activated. Requires activation prior to use. A simple activation protocol is included.
Catalogue Number	PF038
Brand Family	Calbiochem®
Synonyms	92 kDa Gelatinase, Matrix Metalloproteinase 9, Gelatinase B, Type IV Collagenase

References
References	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. 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.: 462-465. Zempo, N., et al. 1994. J. Vasc. Surg. 20, 209. Birkedal-Hansen, H. 1993. J. Periodontol. 64, 474. 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 & C.V. Gay, Eds.: 290-314. Jeffrey, J.J. 1992. in Wound Healing: Biochemical and Clinical Aspects. R.F. Diegelmann and W.J. Lindblad, Eds.: 177-194. 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

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.
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.: 462-465.
Zempo, N., et al. 1994. J. Vasc. Surg. 20, 209.
Birkedal-Hansen, H. 1993. J. Periodontol. 64, 474.
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 & C.V. Gay, Eds.: 290-314.
Jeffrey, J.J. 1992. in Wound Healing: Biochemical and Clinical Aspects. R.F. Diegelmann and W.J. Lindblad, Eds.: 177-194.
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	>1,300 pmoles/min/µg
Unit of Definition	Specific activity is determined using 10 μM (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-(3-[2, 4-dinitrophenyl]-L-2, 3-diaminopropionyl)-Ala-Arg-NH₂ (excitation 320 nm, emission 405 nm), and 20 ng enzyme in 100 μl of 50 mM Tris-HCl, pH 7.5, 10 mM CaCl₂, 150 mM NaCl, and 0.05% BRIJ<sup>®</sup>-35 Detergent at room temperature.
EC number	3.4.24.35
Form	Liquid
Formulation	In 150 mM NaCl, 50 mM Tris-HCl, 10 mM CaCl₂, 0.05% BRIJ^®-35 Detergent, pH 7.5.
Preservative	None

Applications
Application References	Zymography Xia, T., et al. 1996. Biochim. Biophys. Acta. 1293, 259. Kleiner, D.E. and Stetler-Stevenson W.G. 1994. Anal. Biochem. 218, 325. Heussen, C. and Dowdle, E.B. 1980. Anal. Biochem. 102, 196. Substrate Cleavage Assay Xia, T., et al. 1996. Biochim. Biophys. Acta. 1293, 259.
Key Applications	Immunoblotting (Western Blotting) Substrate Cleavage Assay Zymography
Application Notes	Immunoblotting (1 µg protein/lane) Substrate Cleavage Assay (1 µg protein/lane, see application references) Zymography (1 µg protein/lane, see application references)
Application Comments	MMP-9 Proenzyme can be measured by its ability to degrade gelatin in a zymogram. 0.5 ng of enzyme is sufficient to visualize degraded gelatin with coomassie blue stain. The specific activity as measured with 10 µM (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-(3-[2, 4-dinitrophenyl]-L-2, 3-diaminopropionyl)-Ala-Arg-NH₂ (excitation 320 nm, emission 405 nm), and 20 ng enzyme in 100 µl of 50 mM Tris-HCl, pH 7.5, 10 mM CaCl₂, 150 mM NaCl, and 0.05% Brij-35 at room temperature, is >1,300 pmoles/min/µg. To activate MMP-9 proenzyme, prepare p-aminophenylmercuric acetate (APMA) concentrate in dimethylsulfoxide (DMSO). Add APMA to MMP-9 proenzyme to give a final APMA concentration of 1 mM. Incubate at 37°C for 16 to 24 h.

Biological Information
Purity	>90% by SDS-PAGE
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 thaw, aliquot and freeze (-70°C).