Technical Data
Hrs-2 (HGS, Hepatocyte Growth Factor-regulated tyrosine kinase substrate2, Hrs2, SNAP-25 Interacting Protein Hrs-2)
Hrs/Hgs (hepatocyte growth factor-regulated tyrosine kinase substrate) is a tyrosine-phosphorylated member of a protein family characterized by a conserved 3-phosphoinositide- interacting RING zinc finger domain, the so called FYVE finger. A variant of Hrs, Hrs-2 is an ATPase that has been shown to play a regulatory role in the docking and/or fusion of synaptic vesicles to plasma membranes through a calcium-regulated interaction with SNAP-25. Hrs-2 physically interacts with Eps15, a protein required for receptor-mediated endocytosis. The Hrs-2/Eps15 interaction is calcium dependent, inhibited by SNAP-25 and alpha-adaptin, and results in the inhibition of receptor-mediated endocytosis. Immunoelectron microscopy reveals Hrs-2 localization on the limiting membrane of multivesicular bodies, organelles in the endosomal pathway. Recent data suggest that Hrs-2 acts to provide communication between endo- and exocytic processes.

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

Recommended Dilutions:
Immunohistochemistry: 1:100-1:1000
Immunoprecipitation: 2ug/ml
Western Blot: 1:2000-1:3000
Optimal dilutions to be determined by the researcher.

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 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
MabIgG2a6D466Affinity Purified
50ug-20CBlue IceRatMouse
Recombinant full length rat Hrs-2.
Purified by affinity chromatography.
Supplied as a liquid in PBS, pH 7.2, 50% glycerol.
Recognizes rat Hrs-2. Crossreactivity: Hrs (HGS). Species Crossreactivity: mouse, monkey and human.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. G. Jacobsson, et al.; Neuroendocrinology 70, 392 (1999). 2. S. Tsujimoto, et al.; Eur. J. Neurosci. 11, 3047 (1999). 3. A.J. Bean, et al.; J. Biol. Chem. 275, 15271 (2000). 4. S. Tsujimoto & A.J. Bean; J. Biol. Chem. 275, 2938 (2000). 5. A. Shukla, et al. Am. J. Phyiol. Renal. Physiol. 281, F546 (2005). 6. Q. Yan, et al. Mol. Biol. Cell 16, 2470 (2005). 7. S.K. Rayala, et al. J. Biol. Chem. 281, 4395 (2006).