|Other Names||Synaptosomal-associated protein 29, SNAP-29, Soluble 29 kDa NSF attachment protein, Vesicle-membrane fusion protein SNAP-29, SNAP29|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6972c was selected from the Center region of human SNAP29. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||SNAREs, Soluble N-ethylmaleimide-sensitive factor- attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Probably involved in multiple membrane trafficking steps.|
|Cellular Location||Cytoplasm. Membrane; Peripheral membrane protein. Cell junction, synapse, synaptosome. Note=Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic|
|Tissue Location||Found in brain, heart, kidney, liver, lung, placenta, skeletal muscle, spleen and pancreas|
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Provided below are standard protocols that you may find useful for product applications.
SNAP29 is a protein involved in multiple membrane trafficking steps. This protein binds tightly to multiple syntaxins and is localized to intracellular membrane structures rather than to the plasma membrane. While the protein is mostly membrane-bound, a significant fraction of it is found free in the cytoplasm.
Collins,J.E., et.al., Genome Biol. 5 (10), R84 (2004)Rotem-Yehudar,R., et.al., J. Biol. Chem. 276 (35), 33054-33060 (2001)
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