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Human MMP-1 (Catalytic Domain)

$595.00

Catalog Number: B2011328 (1 µg)
Human MMP-1 (Catalytic Domain) is a high quality sequence corresponding to the catalytic domain of human recombinant MMP-1 . This product has been used as molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

Live enquiry about this product via Text/SMS: 1-858-900-3210.

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SKU: B2011328 Categories: ,

Description

Human MMP-1 (Catalytic Domain)
Catalog number: B2011328
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 1 µg
Molecular Weight or Concentration: 17.5 kDa
Supplied as: Solution
Applications: molecular tool for various biochemical applications
Storage: -80 °C
Keywords: Human MMP-1 Catalytic Domain
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: Paladini RD, Wei G, Kundu A, Zhao Q, Bookbinder LH, Keller GA, Shepard HM, Frost GI. Mutations in the catalytic domain of human matrix metalloproteinase-1 (MMP-1) that allow for regulated activity through the use of Ca2+ J Biol Chem. 2013 Mar 1;288(9):6629-39.
2: Chapple SJ, Cheng X, Mann GE. Effects of 4-hydroxynonenal on vascular endothelial and smooth muscle cell redox signaling and function in health and disease Redox Biol. 2013 May 23;1(1):319-31.
3: Vallon R, Müller R, Moosmayer D, Gerlach E, Angel P. The catalytic domain of activated collagenase I (MMP-1) is absolutely required for interaction with its specific inhibitor, tissue inhibitor of metalloproteinases-1 (TIMP-1) Eur J Biochem. 1997 Feb 15;244(1):81-8.
4: Pardo A, Selman M. MMP-1: the elder of the family Int J Biochem Cell Biol. 2005 Feb;37(2):283-8.
5: Iyer S, Visse R, Nagase H, Acharya KR. Crystal structure of an active form of human MMP-1 J Mol Biol. 2006 Sep 8;362(1):78-88.
6: Iyer S, Wei S, Brew K, Acharya KR. Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1 J Biol Chem. 2007 Jan 5;282(1):364-71.
7: Bhaskaran R, Palmier MO, Lauer-Fields JL, Fields GB, Van Doren SR. MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity J Biol Chem. 2008 Aug 1;283(31):21779-88.
8: Karabencheva-Christova TG, Christov CZ, Fields GB. Conformational Dynamics of Matrix Metalloproteinase-1·Triple-Helical Peptide Complexes J Phys Chem B. 2018 May 31;122(21):5316-5326.
9: Fields GB. Biophysical studies of matrix metalloproteinase/triple-helix complexes Adv Protein Chem Struct Biol. 2014;97:37-48.
10: Lin J, Kakkar V, Lu X. Impact of matrix metalloproteinases on atherosclerosis Curr Drug Targets. 2014 Apr;15(4):442-53.

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