MAFF Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9ULX9 |
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Clone Names | 81202098 |
Gene ID | 23764 |
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Other Names | Transcription factor MafF, U-Maf, V-maf musculoaponeurotic fibrosarcoma oncogene homolog F, MAFF |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6837c was selected from the Center region of human MAFF. 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 | MAFF |
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Function | Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (PubMed:8932385). However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2L1/NRF1, and recruiting them to specific DNA-binding sites. Interacts with the upstream promoter region of the oxytocin receptor gene (PubMed:8932385, PubMed:16549056). May be a transcriptional enhancer in the up-regulation of the oxytocin receptor gene at parturition (PubMed:10527846). |
Cellular Location | Nucleus. |
Tissue Location | Expressed in the term myometrium and kidney. |
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Provided below are standard protocols that you may find useful for product applications.
Background
MAFF is a basic leucine zipper (bZIP) transcription factor that lacks a transactivation domain. It is known to bind the US-2 DNA element in the promoter of the oxytocin receptor (OTR) gene and most likely heterodimerizes with other leucine zipper-containing proteins to enhance expression of the OTR gene during term pregnancy. This protein can also form homodimers, and since it lacks a transactivation domain, the homodimer may act as a repressor of transcription.
References
Kataoka,K., et.al., J. Biol. Chem. 276 (1), 819-826 (2001)
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