MafA Antibody [N21K22] | Primary Antibodies

Application: Reactivity: Mouse, Human

Usage Information

Dilution
WB1:1000 IHC1:100-1:500 IF1:100-1:500

Application
WB, IHC, IF

Reactivity
Mouse, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
36 kDa

Datasheet & SDS

Biological Description

Specificity
MafA Antibody [N21K22] detects endogenous levels of total MafA protein.

Clone
N21K22

Synonym(s)
Transcription factor MafA, Pancreatic beta-cell-specific transcriptional activator, RIPE3b1 factor, V-maf musculoaponeurotic fibrosarcoma oncogene homolog A, MAFA

Background
MafA is a β‑cell–enriched basic leucine zipper transcription factor of the large Maf family that binds the C1/RIPE3b1 element of the insulin promoter and functions as a key activator of glucose‑responsive insulin gene expression and β‑cell functional maturation. The protein contains an N‑terminal transactivation region and a C‑terminal basic region–leucine zipper domain that mediates dimerization and high‑affinity DNA binding; MafA forms homo‑ and heterodimers with other Maf family members and cooperates on chromatin with PDX1 and NEUROD1 to drive robust transcription of insulin and additional β‑cell identity genes. MafA occupancy at insulin promoters is required for full glucose‑stimulated insulin transcription, and MafA‑dependent activation selectively accounts for β‑cell–specific expression of insulin, distinguishing MafA from more broadly expressed islet transcription factors. Transcriptomic and functional analyses show that MafA and MafB coordinately regulate genes involved in stimulus–secretion coupling, ion handling, and oxidative stress defense, and in human and rodent islets MafA controls expression of exocytosis‑related components such as STX1A, STXBP1, SYT7, VAMP2, NSF, and RAB3A, thereby linking MafA activity not only to insulin biosynthesis but also to vesicle docking, priming, and fusion at the β‑cell membrane. MafA expression is low during early pancreas development and increases during late β‑cell differentiation, marking the acquisition of mature, glucose‑responsive β‑cell function, and its abundance is regulated at transcriptional and post‑translational levels by glucose, oxidative stress, and kinase pathways including GSK3‑mediated phosphorylation that affects MafA stability and activity. In adult β‑cells, MafA maintains basal and glucose‑induced expression of insulin and multiple secretory and metabolic genes, contributing to sustained insulin output and β‑cell survival under physiological conditions. In type 2 diabetes and other β‑cell dysfunction states, MafA protein levels and nuclear localization are reduced, and MafA target genes involved in exocytosis and metabolism are downregulated, correlating with impaired insulin secretion and defective stimulus–secretion coupling in human islets. Germline MAFA mutations in humans associate with familial diabetes and insulinomatosis, and these variants affect MafA phosphorylation or DNA‑binding properties, underscoring the importance of precise MafA regulation for β‑cell stability and glucose homeostasis. Across these contexts, MafA functions as a β‑cell–selective bZIP transcription factor whose domain structure, cooperative binding with PDX1 and NEUROD1, and control of insulin and exocytosis gene networks make it a central determinant of mature β‑cell identity, glucose‑responsive insulin secretion, and diabetes‑relevant β‑cell vulnerability.

Background

MafA is a β‑cell–enriched basic leucine zipper transcription factor of the large Maf family that binds the C1/RIPE3b1 element of the insulin promoter and functions as a key activator of glucose‑responsive insulin gene expression and β‑cell functional maturation. The protein contains an N‑terminal transactivation region and a C‑terminal basic region–leucine zipper domain that mediates dimerization and high‑affinity DNA binding; MafA forms homo‑ and heterodimers with other Maf family members and cooperates on chromatin with PDX1 and NEUROD1 to drive robust transcription of insulin and additional β‑cell identity genes. MafA occupancy at insulin promoters is required for full glucose‑stimulated insulin transcription, and MafA‑dependent activation selectively accounts for β‑cell–specific expression of insulin, distinguishing MafA from more broadly expressed islet transcription factors. Transcriptomic and functional analyses show that MafA and MafB coordinately regulate genes involved in stimulus–secretion coupling, ion handling, and oxidative stress defense, and in human and rodent islets MafA controls expression of exocytosis‑related components such as STX1A, STXBP1, SYT7, VAMP2, NSF, and RAB3A, thereby linking MafA activity not only to insulin biosynthesis but also to vesicle docking, priming, and fusion at the β‑cell membrane. MafA expression is low during early pancreas development and increases during late β‑cell differentiation, marking the acquisition of mature, glucose‑responsive β‑cell function, and its abundance is regulated at transcriptional and post‑translational levels by glucose, oxidative stress, and kinase pathways including GSK3‑mediated phosphorylation that affects MafA stability and activity. In adult β‑cells, MafA maintains basal and glucose‑induced expression of insulin and multiple secretory and metabolic genes, contributing to sustained insulin output and β‑cell survival under physiological conditions. In type 2 diabetes and other β‑cell dysfunction states, MafA protein levels and nuclear localization are reduced, and MafA target genes involved in exocytosis and metabolism are downregulated, correlating with impaired insulin secretion and defective stimulus–secretion coupling in human islets. Germline MAFA mutations in humans associate with familial diabetes and insulinomatosis, and these variants affect MafA phosphorylation or DNA‑binding properties, underscoring the importance of precise MafA regulation for β‑cell stability and glucose homeostasis. Across these contexts, MafA functions as a β‑cell–selective bZIP transcription factor whose domain structure, cooperative binding with PDX1 and NEUROD1, and control of insulin and exocytosis gene networks make it a central determinant of mature β‑cell identity, glucose‑responsive insulin secretion, and diabetes‑relevant β‑cell vulnerability.

References
https://pubmed.ncbi.nlm.nih.gov/35454124/ https://pubmed.ncbi.nlm.nih.gov/14973194/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%