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SEC23A Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q15436 |
|---|---|
| Clone Names | 100528130 |
| Gene ID | 10484 |
|---|---|
| Other Names | Protein transport protein Sec23A, SEC23-related protein A, SEC23A |
| 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 | SEC23A (HGNC:10701) |
|---|---|
| Function | Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex. Required for the translocation of insulin-induced glucose transporter SLC2A4/GLUT4 to the cell membrane (By similarity). |
| Cellular Location | Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytosol. Note=Enriched at endoplasmic reticulum exit sites, also known as transitional endoplasmic reticulum (tER) |
| Tissue Location | Ubiquitously expressed. |
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene is a member of the SEC23subfamily of the SEC23/SEC24 family. It is part of a proteincomplex and found in the ribosome-free transitional face of theendoplasmic reticulum (ER) and associated vesicles. This proteinhas similarity to yeast Sec23p component of COPII. COPII is thecoat protein complex responsible for vesicle budding from the ER.The encoded protein is suggested to play a role in the ER-Golgiprotein trafficking.
References
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Townley, A.K., et al. J. Cell. Sci. 121 (PT 18), 3025-3034 (2008) :Stagg, S.M., et al. Cell 134(3):474-484(2008)Bi, X., et al. Dev. Cell 13(5):635-645(2007)Tu, L.C., et al. Mol. Cell Proteomics 6(4):575-588(2007)
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