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Matrix Metalloproteinase (MMP)

Custom & Catalog Recombinant Proteins

Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components (1,2).

DescriptionSize Reference USD Qty  
Human MMP-1 - 100 µL100 µl AS-72004 98.00Order Form
Human MMP-10 - 100 µl100 µl AS-72067 98.00Order Form
Human MMP-13 - 100 µL100 µl AS-72011 98.00Order Form
Human MMP-14 - 100 µl100 µl AS-72068 98.00Order Form
Human MMP-2 - 100 µL100 µl AS-72005 98.00Order Form
Human MMP-3 - 100 µL100 µl AS-72006 98.00Order Form
Human MMP-7 - 100 µL100 µl AS-72007 98.00Order Form
MMP-1 (Catalytic Domain), human recombinant - 1 µg1 µg AS-55575-1 93.00Order Form
MMP-1 (Catalytic Domain), human recombinant - 10 µg10 µg AS-55575-10 297.00Order Form
MMP-12 (Catalytic Domain), human recombinant - 1 µg1 µg AS-55525-1 93.00Order Form
MMP-12 (Catalytic Domain), human recombinant - 10 µg10 µg AS-55525-10- 297.00Order Form
MMP-12 (Catalytic Domain), human recombinant - 50 µg50 µg AS-55525-50 990.00Order Form
MMP-9 (Catalytic Domain), human recombinant - 1 µg1 µg AS-55576-1 93.00Order Form
MMP-9 (Catalytic Domain), human recombinant - 10 µg10 µg AS-55576-10 297.00Order Form
MMP-9 (Catalytic Domain), human recombinant - 50 µg50 µg AS-55576-50 990.00Order Form
MMP-9 (Catalytic Domain), mouse recombinant - 1 µg1 µg AS-55884-1 93.00Order Form
MMP-9 (Catalytic Domain), mouse recombinant - 10 µg10 µg AS-55884-10 297.00Order Form
MMP-9 (Catalytic Domain), mouse recombinant - 50 µg50 µg AS-55884-50 990.00Order Form


Size:

  1 µg,, 10 µg or 50 µg

Storage:

  Please store at –80°C, Avoid repeated freeze-thaw cycles.

Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components (1,2).

AS-72004 Human MMP-1
MMP-1 (collagenase-1) is involved in tumor development and metastasis (3;4) and rheumatoid arthritis (5). It is proposed as a therapeutic target for these diseases. Native pro-MMP-1 is prepared from culture medium of human rheumatoid synovial fibroblasts. MMP-1 is secreted as pro-enzyme, which consists of a  propeptide of 80 amino acids, a catalytic domain of 162 amino acids, a 16-residue linker region, and a hemopexin domain of 189 amino acids(6). The native pro-MMP-1 has a major Mr 52-kDa unglycosylated and a minor Mr 57-kDa glycosylated form. The proteolytic activation of the 57/52-kDa species will form 47/42-kDa active collagenase6, and a 22-kDa Cterminal fragment (7).

AS-72005 Human MMP-2
MMP-2 (72-kDa gelatinase-A) is involved in tumor development and metastasis (8-10). It is proposed as a therapeutic target for cancer.
Recombinant human MMP-2 was expressed as a pro-enzyme from its DNA sequence, transfected into CHO cells.

AS-72006 Human MMP-3
MMP-3 (stromelysin-1, transin-1) has been shown to involved in tumor metastasis3 and rheumatoid arthritis (11,12). Therefore it is proposed as a therapeutic target for these diseases. The native pro-MMP-3 is Mr 59/57-kDa doublet, which can be autocatalyzed to an active form of 45-kDa, and is then processed partially to a second active form of 28-kDa.(13)
Human MMP-3 catalytic domain was expressed as 253 amino acid sequence (Pro19-Glu271) in E. coli. The molecular mass is approximately 28/29 kDa on SDS-PAGE.
Recombinant human MMP-3 enzyme has catalytic domain only and doesn’t need APMA activation before enzyme assay.

AS-72007 Human MMP-7
Recombinant human MMP-7 was expressed in E.coli. The molecular mass of zymogen is approximately 28-kDa on SDS-PAGE and the active form is 19-kDa.

As-72008 Human MMP-8
MMP-8 (neutrophil collagenase) is synthesized by neutrophils and stored in the specific granules until it is secreted.(14) Human MMP-8 is a full length pro-enzyme isolated from stimulated human neutrophil
granulocytes.

AS-72067 Human MMP-10
MMP-10 (stromelysin 2) is involved in several pathological conditions, such as cancer, arthritis and wound healing.(18-21) MMP-10 is secreted as zymogen with a prodomain, a catalytic domain, a hinge region, and a hemopexin-like domain. It can activate other MMPs such as MMP-1, MMP-8 and degrade a variety of substrates, including gelatin, collagens III, IV and V, fibronectin, aggrecan.
This recombinant human MMP-10 was expressed as a pro-enzyme enzyme from its DNA sequence (22) transfected into a mouse myeloma cell line, NS0. The apparent Mr on SDS-PAGE is 58-kDa.

AS-72011 Human MMP-13
MMP-13 (collagenase-3),1 is a member of the MMP family of extracellular proteases. Targets of MMP-13 include collagen, gelatin, aggracan, plasminogen and CXCL12. The native MMP-13 is secreted as a 60-kDa proenzyme, and activated by cleavage to a mature 48-kDa MMP-13.
Recombinant human MMP-13 was expressed as a pro-enzyme from its DNA sequence (23) transfected into CHO cells. The predicted Mr is 52-kDa.

AS-72068 Human MMP-14
MMP-14 (MT1-MMP), membrane-type MMP, plays an important role in tumor invasion. MMP-14 is expressed on the surface of invasive tumor cells,(24) in stromal cells of human colon, breast, and head and neck carcinomas.(25) MMP-14 is secreted as zymogen with a prodomain, a catalytic domain, a hinge region, a hemopexin-like domain, and a transmembrane domain. It can activate pro-MMP-2 and degrade a variety of substrates, including fibrillar collagens I, II, III, fibronectin, vitronectin and laminin-1 (26,27). A truncated human MMP-14 with His-tag was expressed in E. coli. The Mr on SDS-PAGE is 31kDa.

AS-55575 Human MMP-1 (Catalytic Domain)
The sequence (Accession # NP_002412) corresponding to the catalytic domain (aa 106-261) of Human MMP-1 was expressed in E. coli. The recombinant human MMP-1 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-1 Catalytic Domain is ~17.5 kDa.

AS-55576 Human MMP-9 (Catalytic Domain)
The sequence (Accession # NP_004985.2) corresponding to the catalytic domain (aa 112-445) of Human MMP-9 was expressed in E. coli. The recombinant human MMP-9 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-9 Catalytic Domain is ~40 kDa.

AS-55884 Mouse MMP-9 (Catalytic Domain)
The sequence (Accession # NP_038627) corresponding to the catalytic domain (aa 112-445) of Mouse MMP-9 was expressed in E. coli. The recombinant mouse MMP-9 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Mouse MMP-9 Catalytic Domain is ~38 kDa.

AS-55525 Human MMP-12 (Catalytic Domain)
The sequence (Accession # NP_002417) corresponding to the catalytic domain (aa 106-267) of Human MMP-12 was expressed in E. coli. The recombinant human MMP-12 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-12 Catalytic Domain is 18 kDa.

References:


1. J. F. Woessner, Jr. and C. J. Taplin, J.Biol.Chem. 263, 16918-16925 (1988).
2. J. F. Woessner, Jr., FASEB J. 5, 2145-2154 (1991).
3. G. I. Goldberg et al., Ann.N.Y.Acad.Sci. 580, 375-384 (1990).
4. W. G. Stetler-Stevenson, S. Aznavoorian, L. A. Liotta, Annu.Rev.Cell Biol. 9, 541-573 (1993).
5. E. M. Gravallese, J. M. Darling, A. L. Ladd, J. N. Katz, L. H. Glimcher, Arthritis Rheum. 34, 1076- 1084 (1991).
6. G. I. Goldberg et al., J.Biol.Chem 261, 6600-6605 (1986).
7. B. Birkedal-Hansen, W. G. Moore, R. E. Taylor, A. S. Bhown, H. Birkedal-Hansen, Biochemistry 27, 6751-6758 (1988).
8. Collier, I. et al. J. Biol. Chem. 263, 6579 (1988).
9. Salo, T. et al. J.Biol.Chem. 258, 3058 (1983).
10. Salo, T. et al. J.Biol.Chem. 260, 8526 (1985).
11. Chin, J. et al. J. Biol. Chem. 260, 12367 (1985).
12. Okada, Y. et al. J Biol. Chem. 261, 14245 (1986).
13. Okada, Y. et al. J. Biol. Chem. 261, 14245 (1986).
14. Bainton, D. et al. J. Exp. Med. 134, 907 (1971).
15. Wilhelm, SM. et al., J. Biol. Chem. 264, 17213 (1989).
16. Fosang, AJ. et al., Biochem. J. 295, 273 (1993).
17. Reponen, P. et al., J. Cell Biol. 124, 1091 (1994).
18. Gill, JH. et al. Neoplasia. 6, 777 (2004).
19. Ramos, MC. et al. Biol. Chem. 385, 75 (2004).
20. Salmela, MT.et al. Scand. J. Gastroenterol. 39, 1095 (2004).
21. Krampert, M. et al. Mol. Biol. Cell 15, 5242 (2004).
22. Muller, D. et al. Biochem. J. 253, 187 (1988)
23. Freije, J. et al. J. Biol .Chem. 269, 16766 (1994).
24. Sato, H. et al. Nature 370, 61 (1994).
25. A. Okada, A. et al., PNAS 92, 2730 (1995).
26. Pei, D. and SJ. Weiss J. Biol. Chem. 271, 9135 (1996).
27. Knight, CG. et al. FEBS Lett. 296, 263 (1992).
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