Description_x000D_ General description_x000D_ Tensin 2 belongs to the tensin family. Tensins are multidomain proteins that are characterized with homologous C1, protein phosphatases (PTPases), C2, Src homology 2 (SH2) domains and pTyr-binding (PTB) domains. Tensin 2 mRNA is highly expressed in heart, kidney, skeletal muscle and liver._x000D_ Immunogen_x000D_ synthetic peptide located near the N-terminus human tensin 2, conjugated to KLH. The corresponding sequence is identical in human tensin 2 isoforms 2 and 3, and in rat and mouse tensin 2._x000D_ Application_x000D_ Anti-Tensin 2 (N-terminal) antibody produced in rabbit has been used in various immunochemical techniques including immunoblotting and immunofluorescence._x000D_ Physical form_x000D_ solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ Tensins are a family of focal adhesion proteins that link between the extracellular matrix (ECM) and the cytoskeleton via integrins, and therefore they might play a role in regulating cell shape and motility. Tensin 2 has been shown to be largely absent in a panel of human cancer cell lines and is down-regulated in human kidney cancer. Tensin 2 variant 3 also contributes to the aggressive tumor behavior in human hepatocellular carcinoma (HCC). The protein through its binding domains interacts with several binding partners and with the tumor suppressor gene deleted in liver cancer 1 (DLC1) to regulate DLC1 tumor suppressor activity. In addition, tensin 2 also stops Akt signaling and cell survival. It reduces intracellular PtdIns-3-4-5-P3 levels at the plasma membrane, indicating that in addition to regulating cytoskeletal dynamics, it influences phosphoinositide-Akt signaling via protein phosphatases (PTPases)domain.