Technical Data
Syntaxin 2 (Epimorphin)
Syntaxin 2, also known as epimorphin, is a 35kD type II integral membrane that belongs to the t-SNARE family, a group of proteins involved in protein transport (2). Syntaxin 2 was first identified as a factor that promotes branching morphogenesis in mammary epithelial cells (3). Studies using pancreatic exocrine acinar cells, in which the exocytic pathways are well defined, show primary localization of syntaxin 2 to the apical plasma membrane (4). Homologs of syntaxin 2 have been identified in various eukaryotes ranging from yeast to human (5, 6). Neuronal syntaxin is a component of a 20S complex implicated in vesicle docking and fusion, which involves its interaction with syntaxin through a ATP-dependent reaction modulated by synaptotagmin, SNAP-25, alpha-SNAP, and NSF (7).

Suitable for use in Western Blot, Immunohistochemistry and Immunoprecipitation. Other applications not tested.

Recommended Dilutions:
Optimal dilutions to be determined by the researcher.

Positive Controls:
Jurkat Cell Lysate
HeLa Cell Lysate
Rat Brain Tissue Extract
Mouse Brain Tissue Extract

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
100ug-20CBlue IceRatRabbit
Synthetic peptide corresponding to the sequence near the N-terminus of rat Syntaxin 2.
Purified by immunoaffinity chromatography.
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide, 50% glycerol.
Recognizes rat Syntaxin 2 at ~35kD. Species Crossreactivity: human, mouse, bovine, canine, chicken, Drosophila, hamster, monkey, porcine, rabbit, sheep and Xenopus.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. GenBank Accession Number L20823. 2. Bennett, M., Garcia-Arraras, J.E., Elferink, L.A., Peterson, K., Fleming, A.M., Hazuka, C.D. and Scheller, R.H. (1993) Cell 74: 863-873. 3. Hirai, Y., Lochter, A., Galosy, S., Koshida, S., Niwa, S. and Bissell, M.J. (1998) J. Biol. Chem. 140: 159-169. 4. Gaisano, H.Y., Ghai, M., Malkus, P.N., Sheu, L., Bouquillon, A., Bennett, M.K. and Trimble, W.S. (1996) Mol. Biol. Cell 12: 2019-2027. 5. Sollner, T., Whiteheart, S.W., Brunner, M., Erdjument-Bromage, H., Geromanos, S., Tempst, P. and Rothman, J.E. (1993) Nature 362: 318-324. 6. Calakos, N., and Scheller, R. (1996) Physiological Reviews 76: 1-29. 7. Sollner, T., Bennett, M.K., Whiteheart, S.W., Scheller, R.H., & J.E. Rothman (1993) Cell 75: 409-418. 8. Karim, S., Essenberg, R.C., Dillwith, J.W., Tucker, J.S., Bowman, A.S., Sauer, J.R. (2002) Insect Biochem Mol Biol 32(12): 1711-1721.