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RFX5 Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P48382 |
|---|---|
| Clone Names | 100427305 |
| Gene ID | 5993 |
|---|---|
| Other Names | DNA-binding protein RFX5, Regulatory factor X 5, RFX5 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP14004c was selected from the Center region of RFX5. 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 | RFX5 |
|---|---|
| Function | Activates transcription from class II MHC promoters. Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y. RFX binds the X1 box of MHC-II promoters. |
| Cellular Location | Nucleus. |
| Tissue Location | Ubiquitous. |
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Provided below are standard protocols that you may find useful for product applications.
Background
A lack of MHC-II expression results in a severeimmunodeficiency syndrome called MHC-II deficiency, or the barelymphocyte syndrome (BLS; MIM 209920). At least 4 complementationgroups have been identified in B-cell lines established frompatients with BLS. The molecular defects in complementation groupsB, C, and D all lead to a deficiency in RFX, a nuclear proteincomplex that binds to the X box of MHC-II promoters. The lack ofRFX binding activity in complementation group C results frommutations in the RFX5 gene encoding the 75-kD subunit of RFX(Steimle et al., 1995). RFX5 is the fifth member of the growingfamily of DNA-binding proteins sharing a novel and highlycharacteristic DNA-binding domain called the RFX motif. Multiplealternatively spliced transcript variants have been found but thefull-length natures of only two have been determined. [provided byRefSeq].
References
Laird, K.M., et al. J. Mol. Biol. 403(1):40-51(2010)Kong, X., et al. J. Mol. Cell. Cardiol. 46(3):292-299(2009)Garvie, C.W., et al. Biochim. Biophys. Acta 1779(12):797-804(2008)Ennis, S., et al. Lancet 372(9652):1828-1834(2008)Xu, Y., et al. J. Biol. Chem. 282(36):26046-26056(2007)
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