Western blot of rat cortex lysate showing specific immunolabeling of the ~65 kDa Munc-18 protein phosphorylated at Ser515. Immunolabeling is blocked by the phosphopeptide (peptide) used as the antigen but not by the corresponding dephosphopeptide (not shown). .
|Tested species reactivity||Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser515 of rat STXBP2 conjugated to KLH|
|Storage buffer||0.01M HEPES, pH 7.5, with 0.15M NaCl, 100µg/ml BSA, 50% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1/1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
This antibody is predicted to react with bovine, canine, chicken, human, mouse, non-human primate and Xenopus based on 100% sequence homology.
In Western blot, this antibody is specific for the ~65 kDa Munc-18 protein phosphorylated at Ser515. Immunolabeling is blocked by the phosphopeptide used as the antigen but not by the corresponding dephosphopeptide.
Munc-18 ( mammalian homologue of Unc-18) is a protein that is thought to be involved in regulating exocytosis due, at least in part, to it ability to bind syntaxin (Ciufo et al., 2005). Munc18-1 is a neuron-specific member of the Sec1/Munc18 protein family that binds to syntaxin1A and is thought to stabilize the complex (Liu et al., 2004). The function of Munc-18 is thought to be regulated by PKC phosphorylation of Ser515 on the Munc-18 protein (Sassa et al., 1996).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.