Recombinant Human Tensin 1 GST (N-Term) Protein Summary
Description |
A recombinant protein with GST tag at N-terminal corresponding to the amino acids 1-385 of Human TNS1 Source: Wheat Germ (in vitro) Amino Acid Sequence: MSVSRTMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNIPGDSQTSVCITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKDDRFPEYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHRDDGMEDGNKQNTNSQSIGSISGGLEDQYTWPDTHWPSQS |
Preparation Method |
in vitro wheat germ expression system |
Details of Functionality |
This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated. |
Source |
Wheat germ |
Protein/Peptide Type |
Recombinant Protein |
Gene |
TNS1 |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- ELISA
- Immunoaffinity Purification
- Protein Array
- SDS-Page
- Western Blot
|
Theoretical MW |
70.1 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at -80C. Avoid freeze-thaw cycles. |
Buffer |
50 mM Tris-HCl, 10 mM reduced Glutathione, pH 8.0 in the elution buffer. |
Preservative |
No Preservative |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Notes
This product is produced by and distributed for Abnova, a company based in Taiwan.
Alternate Names for Recombinant Human Tensin 1 GST (N-Term) Protein
Background
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
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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