Tensin 1: Proteins and Enzymes
Tensin 1 (TNS1, human Tensin 1 theoretical molecular weight 186kDa) belongs to a family of focal adhesion proteins which in mammals includes three other members: Tensin 2, Tensin 3, and C-terminal tensin-like (Cten or Tensin 4) (1, 2). Tensins localize to focal adhesion sites, which are functional domains of the cellular membrane that mediate interactions between the actin cytoskeleton and the extracellular matrix (1). Transmembrane integrin receptors (alpha-beta heterodimer) predominate within focal adhesions and serve to bridge the interactions between extracellular components and the cytoskeleton (3). Tensin 1 interacts with both actin filaments and beta-integrin receptors within focal adhesion sites to mediate cellular responses to extracellular signals (1, 4). Several common functional domains are shared between some tensin family members including: 1) amino terminal PTEN-related tyrosine phosphatase (PTP) domain, 2) amino terminal actin-binding (ABD-1) domain, 3) amino terminal focal adhesion binding (FAB-N) domain, 4) carboxy terminal Src homology 2 (SH2) domain, 5) carboxy terminal phosphotyrosine binding (PTB) domain, and 6) carboxy terminal focal adhesion binding (FAB-C) domain (4). The PTB domain allows tensins to interact with beta-integrin cytoplasmic tails, while their SH2 domain supports interaction with tyrosine-phosphorylated signaling proteins (1). The interactions of tensins with focal adhesion kinases and phosphatases support diverse cellular processes such as attachment, migration, and polarization. Loss of function studies have revealed that tensin 1 plays a critical role for normal kidney function, skeletal muscle regeneration and angiogenesis (1).
References
1. Lo, S. H. (2017). Tensins. Current Biology. https://doi.org/10.1016/j.cub.2017.02.041
2. Lo, S. H. (2014). C-terminal tensin-like (CTEN): A promising biomarker and target for cancer. International Journal of Biochemistry and Cell Biology. https://doi.org/10.1016/j.biocel.2014.04.003
3. Armitage, S. K., & Plotnikov, S. V. (2016). Bridging the gap: A new study reveals that a protein called talin forms a vital link between microtubules and focal adhesions at the surface of cells. ELife. https://doi.org/10.7554/eLife.19733
4. Lo, S. H. (2006). Focal adhesions: What's new inside. Developmental Biology. https://doi.org/10.1016/j.ydbio.2006.03.029
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References
1. Lo, S. H. (2017). Tensins. Current Biology. https://doi.org/10.1016/j.cub.2017.02.041
2. Lo, S. H. (2014). C-terminal tensin-like (CTEN): A promising biomarker and target for cancer. International Journal of Biochemistry and Cell Biology. https://doi.org/10.1016/j.biocel.2014.04.003
3. Armitage, S. K., & Plotnikov, S. V. (2016). Bridging the gap: A new study reveals that a protein called talin forms a vital link between microtubules and focal adhesions at the surface of cells. ELife. https://doi.org/10.7554/eLife.19733
4. Lo, S. H. (2006). Focal adhesions: What's new inside. Developmental Biology. https://doi.org/10.1016/j.ydbio.2006.03.029
3 results for "Tensin 1 Proteins and Enzymes" in Products
3 results for "Tensin 1 Proteins and Enzymes" in Products
Tensin 1: Proteins and Enzymes
Tensin 1 (TNS1, human Tensin 1 theoretical molecular weight 186kDa) belongs to a family of focal adhesion proteins which in mammals includes three other members: Tensin 2, Tensin 3, and C-terminal tensin-like (Cten or Tensin 4) (1, 2). Tensins localize to focal adhesion sites, which are functional domains of the cellular membrane that mediate interactions between the actin cytoskeleton and the extracellular matrix (1). Transmembrane integrin receptors (alpha-beta heterodimer) predominate within focal adhesions and serve to bridge the interactions between extracellular components and the cytoskeleton (3). Tensin 1 interacts with both actin filaments and beta-integrin receptors within focal adhesion sites to mediate cellular responses to extracellular signals (1, 4). Several common functional domains are shared between some tensin family members including: 1) amino terminal PTEN-related tyrosine phosphatase (PTP) domain, 2) amino terminal actin-binding (ABD-1) domain, 3) amino terminal focal adhesion binding (FAB-N) domain, 4) carboxy terminal Src homology 2 (SH2) domain, 5) carboxy terminal phosphotyrosine binding (PTB) domain, and 6) carboxy terminal focal adhesion binding (FAB-C) domain (4). The PTB domain allows tensins to interact with beta-integrin cytoplasmic tails, while their SH2 domain supports interaction with tyrosine-phosphorylated signaling proteins (1). The interactions of tensins with focal adhesion kinases and phosphatases support diverse cellular processes such as attachment, migration, and polarization. Loss of function studies have revealed that tensin 1 plays a critical role for normal kidney function, skeletal muscle regeneration and angiogenesis (1).
References
1. Lo, S. H. (2017). Tensins. Current Biology. https://doi.org/10.1016/j.cub.2017.02.041
2. Lo, S. H. (2014). C-terminal tensin-like (CTEN): A promising biomarker and target for cancer. International Journal of Biochemistry and Cell Biology. https://doi.org/10.1016/j.biocel.2014.04.003
3. Armitage, S. K., & Plotnikov, S. V. (2016). Bridging the gap: A new study reveals that a protein called talin forms a vital link between microtubules and focal adhesions at the surface of cells. ELife. https://doi.org/10.7554/eLife.19733
4. Lo, S. H. (2006). Focal adhesions: What's new inside. Developmental Biology. https://doi.org/10.1016/j.ydbio.2006.03.029
Show More
References
1. Lo, S. H. (2017). Tensins. Current Biology. https://doi.org/10.1016/j.cub.2017.02.041
2. Lo, S. H. (2014). C-terminal tensin-like (CTEN): A promising biomarker and target for cancer. International Journal of Biochemistry and Cell Biology. https://doi.org/10.1016/j.biocel.2014.04.003
3. Armitage, S. K., & Plotnikov, S. V. (2016). Bridging the gap: A new study reveals that a protein called talin forms a vital link between microtubules and focal adhesions at the surface of cells. ELife. https://doi.org/10.7554/eLife.19733
4. Lo, S. H. (2006). Focal adhesions: What's new inside. Developmental Biology. https://doi.org/10.1016/j.ydbio.2006.03.029
| Applications: | WB, ELISA, MA, AP, PAGE |
![SDS-PAGE: Recombinant Human Tensin 1 GST (N-Term) Protein [H00007145-P01]](https://resources.bio-techne.com/images/products/qc_test-H00007145-P01-1.jpg "SDS-PAGE: Recombinant Human Tensin 1 GST (N-Term) Protein [H00007145-P01]")
| Applications: | AC |
| Applications: | AC |