Cat. # | Size | Qty. | Price |
---|---|---|---|
73959T | 1 Kit (8 x 20 microliters) |
|
Product Includes | Quantity | Applications | Reactivity | MW(kDa) | Isotype |
---|---|---|---|---|---|
MMP-9 (D6O3H) XP® Rabbit mAb 13667 | 20 µl |
|
H | 84, 92 | Rabbit IgG |
MMP-2 (D2O4T) Rabbit mAb 87809 | 20 µl |
|
H M | 64,72 | Rabbit IgG |
MMP-3 (D7F5B) Rabbit mAb 14351 | 20 µl |
|
H R | 60 | Rabbit IgG |
TIMP1 (D10E6) Rabbit mAb 8946 | 20 µl |
|
H Mk | 26 | Rabbit IgG |
TIMP2 (D18B7) Rabbit mAb 5738 | 20 µl |
|
H M Mk | 22 | Rabbit IgG |
TIMP3 (D74B10) Rabbit mAb 5673 | 20 µl |
|
H M R | 20, 25 | Rabbit IgG |
MMP-7 Antibody 71031 | 20 µl |
|
H | 28 | Rabbit |
MT1-MMP (E3S5S) Rabbit mAb 26424 | 20 µl |
|
H | 62 | Rabbit IgG |
Anti-rabbit IgG, HRP-linked Antibody 7074 | 100 µl |
|
Rab | Goat |
Product Information
Matrix remodeling is mainly controlled by MMPs and TIMPs. The matrix metalloproteinase (MMP) family of proteases are a group of zinc-dependent enzymes that target extracellular proteins, including growth factors, cell surface receptors, adhesion molecules, matrix structural proteins, and other proteases (1, 2). Among the family members, MMP-2, MMP-3, MMP-7, MMP-9, and MMP14 (MT1-MMP) have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (3). MMP activity is regulated by mechanisms of both transcriptional control and post translational protein processing. Once synthesized, MMPs exist as latent proenzymes. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full-length protein (4). MMP activity can be inhibited through its binding to endogenously expressed TIMPs. TIMPs are members of the family of tissue inhibitors of matrix metalloproteinases that include TIMP1, TIMP2, TIMP3, and TIMP4. The main function of TIMPs is their inhibitory effect on MMPs. TIMPs irreversibly inactivate MMPs by direct binding MMPs and chelating their zinc cofactor at the catalytic site to inhibit the proteinase function (5,6).
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