Flow cytometric analysis of serum starved U-2 OS cells, untreated (blue) or treated with TPA (200nM, 24 hours) using MMP-9 (D6O3H) XP Rabbit mAb (green). Anti-rabbit IgG (H+L), F(ab')2 Fragment (PE Conjugate) was used as a secondary antibody.
Immunoprecipitation of MMP-2 protein from U87 cell extracts. Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is MMP-2 (D2O4T) Rabbit mAb. Western blot analysis was performed using MMP-2 (D2O4T) Rabbit mAb.
Western blot analysis of extracts from HeLa, HT-1080, and NIH/3T3 cells using MT1-MMP (D1E4) Rabbit mAb.
Western blot analysis of extracts from various cell lines using MMP-3 (D7F5B) Rabbit mAb.
Western blot analysis of extracts from various cell lines using TIMP1 (D10E6) Rabbit mAb.
Western blot analysis of extracts from HT-1080, A172, and COS-7 cells using TIMP2 (D18B7) Rabbit mAb.
Western blot analysis of extracts from A-431, and NIH/3T3 cells, using TIMP3 (D74B10) Rabbit mAb.
Western blot analysis of extracts from concentrated culture medium of IGROV-1 and HT-29 cell lines using MMP-7 Antibody.
After the primary antibody is bound to the target protein, a complex with HRP-linked secondary antibody is formed. The LumiGLO® is added and emits light during enzyme catalyzed decomposition.
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using MMP-9 (D6O3H) XP® Rabbit mAb.
Western blot analysis of extracts from U87, 3T3-L1 and C2C12 cells using MMP-2 (D4O4T) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human lung carcinoma using MMP-9 (D6O3H) XP® Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded U-2 OS cell pellets, untreated (left) or treated with TPA #4174 (right), using MMP-9 (D6O3H) XP® Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human colon carcinoma using MMP-9 (D6O3H) XP® Rabbit mAb in the presence of control peptide (left) or antigen-specific peptide (right).
Western blot analysis of concentrated, serum-free cultured medium from U-2 OS cells, untreated (-) or treated with TPA #4174 (200 nM, 48 hr; +), using MMP-9 (D6O3H) XP® Rabbit mAb.
|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|
|MT1-MMP (D1E4) Rabbit mAb 13130||20 µl||
||H M||50, 62||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||
|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
The Matrix Remodeling Antibody Sampler Kit provides an economical means of detecting different MMPs and TIMPs using the specific corresponding antibodies. The kit contains enough antibody to perform at least two western blot experiments with each primary antibody.
Each antibody in the Matrix Remodeling Antibody Sampler Kit detects endogenous levels of its target protein.
Monoclonal antibodies are produced by immunizing rabbits with synthetic peptides corresponding to Pro117 of human MMP2, Ser417 of human MMP3, Phe542 of human MMP9, Met293 of MT1-MMP, Ala134 of human TIMP1, Thr135 of human TIMP2, and Lys53 of human TIMP3. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to Phe98 of human MMP-7. Antibodies are purified by protein A and peptide affinity chromatography.
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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