MT1-MMP (D1E4) Rabbit mAb

• 产品编号：CST-13130S      品牌：CST       原厂货号：13130S
• 产品分类：抗体 > 一抗 > 蛋白特异性一抗
• 应用分类：

描述：

MT1-MMP (D1E4) Rabbit mAb可以识别内源性总的MT1-MMP蛋白。单克隆抗体由合成肽段免疫动物产生，该肽段与人MT1-MMP蛋白Met293附近氨基酸序列一致。基质金属蛋白酶(MMP)家族是一组锌依赖酶能够靶向细胞外蛋白，包括生长因子，细胞表面受体，黏附分子和其他蛋白酶(1)。基质金属蛋白酶，可以根据功能和细胞定位划分，包括6个不同的膜型(MT)金属蛋白酶，它们有相同的跨膜结构域和短胞质尾巴(2)。膜型1金属蛋白酶(MT1-MMP, MMP14) 参与调节发育，血管生成，组织重构和进行性肿瘤(3-6)。MT1-MMP和其他金属蛋白酶通过积累在被称为invadopodia的特殊结构促进肿瘤细胞的侵袭，它重塑细胞外基质，并允许肿瘤细胞突破基底膜(7)。MT1-MMP在细胞表面的丰度和存在被靶细胞的内吞作用所控制，这可是通过调节MT1-MMP的胞质结构域所控制的(8)。MT1-MMP的蛋白酶活性可以通过同源二聚体形成，催化加工，结构域脱落和抑制蛋白的相互作用而得到进一步的规范。全长MT1-MMP 被furin在trans-Golgi网络裂解从而去除了抑制肽结构域而导致MT1-MMP酶原的激活(9)。细胞表面，MT1-MMP能在一个细胞复合物与可溶性金属蛋白酶MMP2和MMP抑制子TIMP2中找到。MT1-MMP介导了MMP2的裂解和激活生产活性MMP2胶原酶，它在ECM重构和肿瘤侵袭过程中发挥重要作用（10）。除了和MMP2外，MT1-MMP还可以和大量的底物结合，包括间质胶原，黏附糖蛋白 (如层粘连蛋白)和细胞表面受体(11)。

1. Kessenbrock, K. et al. (2010) Cell 141, 52-67.
2. Nagase, H. et al. (2006) Cardiovasc Res 69, 562-73.
3. Sounni, N.E. and Noel, A. (2008) Biochimie 87, 329-42.
4. van Hinsbergh, V.W. and Koolwijk, P. (2008) Cardiovasc Res 78, 203-12.
5. Rowe, R.G. and Weiss, S.J. (2008) Trends Cell Biol 18, 560-74.
6. Tang, Y. et al. (2013) Dev Cell 25, 402-16.
7. Poincloux, R. et al. (2009) J Cell Sci 122, 3015-24.
8. Gingras, D. and Béliveau, R. (2010) Biochim Biophys Acta 1803, 142-50.
9. Osenkowski, P. et al. (2004) J Cell Physiol 200, 2-10.
10. Sato, H. and Takino, T. (2010) Cancer Sci 101, 843-7.
11. Barbolina, M.V. and Stack, M.S. (2008) Semin Cell Dev Biol 19, 24-33.

原厂资料：

Specificity / Sensitivity

MT1-MMP (D1E4) Rabbit mAb recognizes endogenous levels of total MT1-MMP protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Met293 of human MT1-MMP protein.

Background

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, and other proteases (1). Matrix metalloproteinases can be broadly categorized based on function and cellular localization, and include six distinct membrane-type (MT) metalloproteinases that share a transmembrane domain and short cytoplasmic tail (2). Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP14) is involved in regulating development, angiogenesis, tissue remodeling, and tumor progression (3-6). MT1-MMP and other metalloproteinases promote tumor cell invasion by accumulating in specialized structures known as invadopodia, which remodel the ECM and allow tumor cells to breach the basement membrane (7). The abundance and presence of MT1-MMP at the cell surface is controlled by targeted endocytosis, which may be regulated by the MT1-MMP cytoplasmic domain (8). MT1-MMP protease activity can be further regulated through homodimer formation, autocatalytic processing, domain shedding and the interaction with inhibitory proteins. Activation of the MT1-MMP proenzyme results from cleavage of full-length MT1-MMP by furin in the trans-Golgi network, which removes the inhibitory propeptide domain (9). At the cell surface, MT1-MMP can be found in a protein complex with the soluble metalloproteinase MMP2 and the MMP inhibitor TIMP2. MT1-MMP mediated cleavage and activation of MMP2 generates the active MMP2 collagenase, which plays important roles in ECM remodeling and tumor invasion (10). MT1-MMP interacts with a large number of substrates in addition to MMP2, including interstitial collagens, adhesive glycoproteins (i.e. laminin), and cell surface receptors (11).

1. Kessenbrock, K. et al. (2010) Cell 141, 52-67.
2. Nagase, H. et al. (2006) Cardiovasc Res 69, 562-73.
3. Sounni, N.E. and Noel, A. (2008) Biochimie 87, 329-42.
4. van Hinsbergh, V.W. and Koolwijk, P. (2008) Cardiovasc Res 78, 203-12.
5. Rowe, R.G. and Weiss, S.J. (2008) Trends Cell Biol 18, 560-74.
6. Tang, Y. et al. (2013) Dev Cell 25, 402-16.
7. Poincloux, R. et al. (2009) J Cell Sci 122, 3015-24.
8. Gingras, D. and Béliveau, R. (2010) Biochim Biophys Acta 1803, 142-50.
9. Osenkowski, P. et al. (2004) J Cell Physiol 200, 2-10.
10. Sato, H. and Takino, T. (2010) Cancer Sci 101, 843-7.
11. Barbolina, M.V. and Stack, M.S. (2008) Semin Cell Dev Biol 19, 24-33.

注意事项：

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150
mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02%
sodium azide. Store at –20°C. Do not aliquot the antibody