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FXYD5 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q96DB9 |
|---|---|
| Clone Names | 100528091 |
| Gene ID | 53827 |
|---|---|
| Other Names | FXYD domain-containing ion transport regulator 5, Dysadherin, FXYD5, DYSAD, IWU1 |
| 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 | FXYD5 |
|---|---|
| Synonyms | DYSAD, IWU1 |
| Function | Involved in down-regulation of E-cadherin which results in reduced cell adhesion. Promotes metastasis. |
| Cellular Location | Membrane; Single-pass type I membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of a family of small membraneproteins that share a 35-amino acid signature sequence domain,beginning with the sequence PFXYD and containing 7 invariant and 6highly conserved amino acids. The approved human gene nomenclaturefor the family is FXYD-domain containing ion transport regulator.Mouse FXYD5 has been termed RIC (Related to Ion Channel). FXYD2,also known as the gamma subunit of the Na,K-ATPase, regulates theproperties of that enzyme. FXYD1 (phospholemman), FXYD2 (gamma),FXYD3 (MAT-8), FXYD4 (CHIF), and FXYD5 (RIC) have been shown toinduce channel activity in experimental expression systems.Transmembrane topology has been established for two family members(FXYD1 and FXYD2), with the N-terminus extracellular and theC-terminus on the cytoplasmic side of the membrane. This geneproduct, FXYD5, is a glycoprotein that functions in theup-regulation of chemokine production, and it is involved in thereduction of cell adhesion via its ability to down-regulateE-cadherin. It also promotes metastasis, and has been linked to avariety of cancers. Alternative splicing results in multipletranscript variants. [RefSeq curation by Kathleen J. Sweadner,Ph.D., sweadner@helix.mgh.harvard.edu.].
References
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Ono, K., et al. Anticancer Res. 30(9):3273-3278(2010)Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)Liang, J.F., et al. Pathol. Res. Pract. 205(7):445-450(2009)Batistatou, A., et al. Endocr. Pathol. 19(3):197-202(2008)
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