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RFX2 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P48378 |
|---|---|
| Clone Names | 100324254 |
| Gene ID | 5990 |
|---|---|
| Other Names | DNA-binding protein RFX2, Regulatory factor X 2, RFX2 |
| 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 | RFX2 |
|---|---|
| Function | Transcription factor that acts as a key regulator of spermatogenesis. Acts by regulating expression of genes required for the haploid phase during spermiogenesis, such as genes required for cilium assembly and function (By similarity). Recognizes and binds the X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3' present on promoters (PubMed:10330134). Probably activates transcription of the testis-specific histone gene H1-6 (By similarity). |
| Cellular Location | Nucleus {ECO:0000250|UniProtKB:B2GV50, ECO:0000255|PROSITE-ProRule:PRU00858}. Cytoplasm {ECO:0000250|UniProtKB:B2GV50}. Note=Mainly expressed in the nucleus and at lower level in cytoplasm. {ECO:0000250|UniProtKB:B2GV50} |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene is a member of the regulatory factor X genefamily, which encodes transcription factors that contain ahighly-conserved winged helix DNA binding domain. The proteinencoded by this gene is structurally related to regulatory factorsX1, X3, X4, and X5. It is a transcriptional activator that can bindDNA as a monomer or as a heterodimer with other RFX family members.This protein can bind to cis elements in the promoter of the IL-5receptor alpha gene. Two transcript variants encoding differentisoforms have been described for this gene, and both variantsutilize alternative polyadenylation sites.
References
Purvis, T.L., et al. Gene 460 (1-2), 20-29 (2010) :Bailey, S.D., et al. Diabetes Care (2010) In press :Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)Horvath, G.C., et al. Biol. Reprod. 71(5):1551-1559(2004)Maijgren, S., et al. Arch. Dermatol. Res. 295(11):482-489(2004)
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