Technical Data
Synip (Syntaxin 4-Interacting protein)
Insulin binds to and activates its receptor and initiates a signaling cascade that eventually induces the translocation of the Glut4 glucose transporter from its intracellular locations to the plasma membrane. Initiating this pathway facilitates glucose uptake in fat and skeletal muscle cells (1). Synip and Syntaxin 4 are two proteins thought to be involved in the recruitment of Glut4-containing vesicles to plasma membrane (2,3). Synip associates with Syntaxin 4 when insulin is absent. Insulin signaling triggers the dissociation of the two proteins and allows Syntaxin 4 to complex with VAMP2, which is essential for Glut4 translocation to plasma membrane (24). Overexpression of a dominant-negative form of Synip prevents Glut4 from translocating to plasma membrane in response to insulin stimulation (3). Synip together with Syntaxin 4, therefore, regulates Glut4 transport to plasma membrane.

Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
100ul-20CBlue IceHumanRabbit
Not determined
Synthetic peptide (KLH-coupled) derived from the sequence of human Synip
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 100ug/ml BSA, 50% glycerol and less than 0.02% sodium azide.
Detects endogenous levels of total Synip protein.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
(1) Watson, R.T. and Pessin, J.E. (2006) Trends Biochem. Sci. 31, 215222.
(2) Min, J. et al. (1999) Mol. Cell 3, 751760.
(3) Yamada, E. et al. (2005) J. Cell Biol. 168, 921928.
(4) Foster, L.J. and Klip, A. (2000) Am. J. Physiol. Cell Physiol. 279, C877C890.