Mouse TIMP-2 DuoSet ELISA, 5 Plate

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

TIMPs-1 through -4 regulate the activity of zinc metalloproteases known as MMPs, ADAMs and ADAMTSs. Structurally, TIMPs contain two domains. The N-terminal domain binds to the active site of mature metalloproteases via a 1:1 non-covalent interaction, blocking access of substrates to the catalytic site. In addition, The C-terminal domain of TIMP-1 and TIMP-2 binds to the hemopexin- like domain of pro-MMP-9 and pro-MMP-2, respectively. The latter binding is essential for the cell surface activation of MMP-2 by MMP-14.

We have publications tested in 1 confirmed species: Mouse.

Showing Publications 1 - 3 of 3.

Publications using DY6304-05	Applications	Species
K Thomas, L Zondler, N Ludwig, M Kardell, C Lüneburg, K Henke, S Mersmann, A Margraf, T Spieker, T Tekath, A Velic, R Holtmeier, J Hermann, V Jankowski, M Meersch, D Vestweber, M Westphal, J Roth, MA Schäfers, JA Kellum, CA Lowell, J Rossaint, A Zarbock Glutamine prevents acute kidney injury by modulating oxidative stress and apoptosis in tubular epithelial cells JCI Insight, 2022-11-08;7(21):. 2022-11-08 [PMID: 36107633] (Mouse)		Mouse
J Rossaint, M Meersch, K Thomas, S Mersmann, M Lehmann, J Skupski, T Tekath, P Rosenberge, JA Kellum, H Pavenstädt, A Zarbock Remote ischemic preconditioning causes transient cell-cycle arrest and renal protection by a NF-kB-dependent Sema5B pathway JCI Insight, 2022-07-22;0(0):. 2022-07-22 [PMID: 35727636] (Mouse)		Mouse
J Vandooren, W Swinnen, E Ugarte-Ber, L Boon, D Dorst, E Martens, G Opdenakker Endotoxemia shifts neutrophils with TIMP-free gelatinase B/ MMP-9 from bone marrow to periphery and induces systematic upregulation of TIMP-1 Haematologica, 2017-08-03;0(0):. 2017-08-03 [PMID: 28775117] (Mouse)		Mouse

Array DY6304-05

• TIMP-2 Antibodies
• TIMP-2 ELISA Kits
• TIMP-2 Lysate
• TIMP-2 Proteins
• TIMP-2 Proteins and Enzymes
• TIMP-2 ELISAs