YKT6 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O15498 |
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Clone Names | 80924293 |
Gene ID | 10652 |
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Other Names | Synaptobrevin homolog YKT6, 231-, YKT6 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6685b was selected from the C-term region of human YKT6. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
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. |
Name | YKT6 |
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Function | Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity. |
Cellular Location | Cytoplasm, cytosol. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side. Note=Probably cycles through vesicles between Golgi and endosomes |
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Provided below are standard protocols that you may find useful for product applications.
Background
YKT6 is one of the SNARE recognition molecules implicated in vesicular transport between secretory compartments. It is a membrane associated, isoprenylated protein that functions at the endoplasmic reticulum-Golgi transport step. This protein is highly conserved from yeast to human and can functionally complement the loss of the yeast homolog in the yeast secretory pathway.
References
Veit,M., Biochem. J. 384 (PT 2), 233-237 (2004)
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