Mouse Anti-MAF1 Recombinant Antibody (CBFYM-1276) (CBMAB-M1435-FY)

Name: Mouse Anti-MAF1 Recombinant Antibody (CBFYM-1276)
SKU: CBMAB-M1435-FY
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBFYM-1276

Application

WB, IP, IF, IHC-P, ELISA

Specificity

Mouse, Rat, Human

Clonality

Monoclonal

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

MAF1 homolog (S. cerevisiae)

Introduction

This gene encodes a protein that is similar to Maf1, a Saccharomyces cerevisiae protein highly conserved in eukaryotic cells. Yeast Maf1 is a negative effector of RNA polymerase III. It responds to changes in the cellular environment and represses pol III transcription. Biochemical studies identified the initiation factor TFIIIB as a target for Maf1-dependent repression.

Entrez Gene ID

Human	84232
Mouse	68877
Rat	315093

UniProt ID

Human	Q9H063
Mouse	Q9D0U6
Rat	Q5XIH0

Alternative Names

MAF1 Homolog, Negative Regulator Of RNA Polymerase III; MAF1 Homolog (S. Cerevisiae)

Function

Plays a role in the repression of RNA polymerase III-mediated transcription in response to changing nutritional, environmental and cellular stress conditions to balance the production of highly abundant tRNAs, 5S rRNA, and other small non-coding RNAs with cell growth and maintenance (PubMed:18377933, PubMed:20233713, PubMed:20516213, PubMed:20543138).
Plays also a key role in cell fate determination by promoting mesorderm induction and adipocyte differentiation (By similarity).
Mechanistically, associates with the RNA polymerase III clamp and thereby impairs its recruitment to the complex made of the promoter DNA, TBP and the initiation factor TFIIIB (PubMed:20887893, PubMed:17505538).
When nutrients are available and mTOR kinase is active, MAF1 is hyperphosphorylated and RNA polymerase III is engaged in transcription. Stress-induced MAF1 dephosphorylation results in nuclear localization, increased targeting of gene-bound RNA polymerase III and a decrease in the transcriptional readout (PubMed:26941251).
Additionally, may also regulate RNA polymerase I and RNA polymerase II-dependent transcription through its ability to regulate expression of the central initiation factor TBP (PubMed:17499043).

Biological Process

Negative regulation of transcription by RNA polymerase IManual Assertion Based On ExperimentIDA:CACAO
Negative regulation of transcription by RNA polymerase IIIManual Assertion Based On ExperimentIDA:UniProtKB

Cellular Location

Nucleus
Cytoplasm

PTM

Phosphorylated at Ser-60, Ser-68 and Ser-75; the major sites of phosphorylation. Nuclear accumulation correlates with a concomitant dephosphorylation. Phosphorylation may attenuate its RNA polymerase III-repressive function.
Sumoylated with SUMO1 and SUMO2, mainly on Lys-35. Desumoylated by SENP1. SUMOylation promotes the ability of MAF1 to repress transcription and suppress colony formation.

Li, Y., Xiao, D., Chen, H., Zheng, X. S., & Xiang, M. (2023). Maf1 controls retinal neuron number by both RNA Pol III-and Pol II-dependent mechanisms. Iscience, 26(12), 108544.

Willemin, G., Mange, F., Praz, V., Lorrain, S., Cousin, P., Roger, C., ... & Hernandez, N. (2023). Contrasting effects of whole-body and hepatocyte-specific deletion of the RNA polymerase III repressor Maf1 in the mouse. Frontiers in Molecular Biosciences, 10.

Phillips, E., Ahmad, N., Sun, L., Iben, J., Walkey, C. J., Rusin, A., ... & Johnson, D. L. (2022). MAF1, a repressor of RNA polymerase III-dependent transcription, regulates bone mass. Elife, 11, e74740.

Li, L., Yu, Z., Zhao, D., Ren, Y., Hou, H., & Xu, Y. (2021). Structure of human RNA polymerase III elongation complex. Cell research, 31(7), 791-800.

Kulaberoglu, Y., Malik, Y., Borland, G., Selman, C., Alic, N., & Tullet, J. M. (2021). Rna polymerase III, ageing and longevity. Frontiers in Genetics, 12, 705122.

Noguchi, C., Wang, L., Shetty, M., Mell, J. C., Sell, C., & Noguchi, E. (2021). Maf1 limits RNA polymerase III-directed transcription to preserve genomic integrity and extend lifespan. Cell Cycle, 20(3), 247-255.

Oliveira Andrade, M., Sforça, M. L., Batista, F. A. H., Figueira, A. C. M., & Benedetti, C. E. (2020). The MAF1 phosphoregulatory region controls MAF1 interaction with the RNA polymerase III C34 subunit and transcriptional repression in plants. Plant Cell, 32(9), 3019-3035.

Wang, X., Rusin, A., Walkey, C. J., Lin, J. J., & Johnson, D. L. (2019). The RNA polymerase III repressor MAF1 is regulated by ubiquitin-dependent proteasome degradation and modulates cancer drug resistance and apoptosis. Journal of Biological Chemistry, 294(50), 19255-19268.

Szatkowska, R., Garcia-Albornoz, M., Roszkowska, K., Holman, S. W., Furmanek, E., Hubbard, S. J., ... & Adamczyk, M. (2019). Glycolytic flux in Saccharomyces cerevisiae is dependent on RNA polymerase III and its negative regulator Maf1. Biochemical Journal, 476(7), 1053-1082.

Hokonohara, K., Nishida, N., Miyoshi, N., Takahashi, H., Haraguchi, N., Hata, T., ... & Mori, M. (2019). Involvement of MAF1 homolog, negative regulator of RNA polymerase III in colorectal cancer progression. International journal of oncology, 54(3), 1001-1009.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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For research use only. Not intended for any clinical use.

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