MAFA Antibodies

Background

MAFA is a transcription factor belonging to the basic leucine zipper (bZIP) family, mainly regulating the functions of macrophages and B cells, and participating in physiological processes such as immune responses, oxidative stress, and the cell cycle. This protein plays a dual role in inflammatory responses and tumorigenesis by binding to specific DNA sequences to activate or inhibit the expression of target genes. MAFA was initially identified as a key regulatory factor of pancreatic β cells in 2002. Subsequent studies have found that it is widely expressed in various tissues and is particularly crucial for maintaining immune homeostasis and metabolic balance. Its unique domain composition and dynamic dimerization characteristics make it an important model for studying transcriptional regulatory mechanisms, providing a new perspective for understanding the molecular basis of immune-related diseases and cancers.

Structure Function Application Advantage Our Products

Structure of MAFA

MAFA is a basic leucine zipper (bZIP) transcription factor with a molecular weight of approximately 18-20 kDa. Its precise molecular weight varies slightly among different subtypes (such as MAFA, MAFB) and post-translational modifications (such as phosphorylation).

Species	Human	Mice	Rats
Molecular Weight (kDa)	~18-20	~18-20	~18-20
Primary Structural Differences	Contains a conserved DNA binding domain and a leucine zipper dimerization domain	Highly homologous and functionally similar	Highly similar to the human MAFA structure

MAFA is composed of approximately 300 amino acids, and its structure includes the N-terminal transcriptional activation domain, the central DNA binding domain, and the C-terminal leucine zipper dimerization domain. This protein forms homologous or heterodimers through leucine zippers (such as binding to MAFB), and then recognizes and binds to specific DNA sequences (such as MARE elements) to regulate the expression of target genes. The DNA binding ability of MAFA is influenced by its phosphorylation state, while the C-terminal domain determines its interaction ability with different protein chaperone. This transcription factor plays a key regulatory role in various tissues such as pancreatic islet β cells and immune cells.

Fig. 1:Changes in the structure of MAFA. (OA Literature) Fig. 1 Pathogenic mechanisms of defective MAFA phosphorylation: Thr57Arg variants cause β-cell dysfunction and familial insulinoma.¹

Key structural properties of MAFA:

Alkaline leucine zipper (bZIP) structure
Conserved DNA binding motifs
Phosphorylation regulatory site
N-terminal transcriptional activation domain
C-end dimerization interface

Functions of MAFA

The core function of MAFA is to regulate gene expression, especially playing a key role in pancreatic beta cells and the immune system. In addition, it is also involved in a variety of physiological processes such as cell differentiation, metabolic balance and oxidative stress response.

Function	Description
Regulation of pancreatic beta cells	Activate the expression of insulin genes (such as INS) and other genes related to β -cell function to maintain glucose homeostasis.
Immune regulation	In macrophages and the regulation of inflammatory factor expression in B cell, affect the congenital and adaptive immune responses.
Cell cycle regulation	Through promoting the proliferation inhibition gene (such as CCND1) or activation of suppressor, involved in cell growth and differentiation.
Oxidative stress response	Regulate the expression of antioxidant enzymes (such as SOD and CAT) to help cells cope with reactive oxygen species (ROS) damage.
Metabolic balance	Genes related to lipid and glucose metabolism are closely associated with metabolic diseases such as diabetes and obesity.

The oxygen dissociation curve of myoglobin is hyperbolic in contrast to hemoglobin’s sigmoidal curve, indicating its higher oxygen affinity and role as a short-term oxygen reservoir.

Applications of MAFA and MAFA Antibody in Literature

1. Liang, Jiani, et al. "MafA regulation in β-cells: from transcriptional to post-translational mechanisms." Biomolecules 12.4 (2022): 535. https://doi.org/10.3390/biom12040535

This article reviews the key role of the transcription factor MafA in pancreatic islet β cells, with a focus on exploring its molecular mechanisms in insulin secretion and blood glucose regulation. The article analyzed the relationship between the expression regulation of MafA (including transcriptional and post-translational modifications) and β -cell dysfunction in type 2 diabetes, providing a theoretical basis for the search of therapeutic targets for diabetes.

2. Nishimura, Wataru, Hiroaki Iwasa, and Munkhtuya Tumurkhuu. "Role of the Transcription Factor MAFA in the Maintenance of Pancreatic β-Cells." International journal of molecular sciences 23.9 (2022): 4478.https://doi.org/10.3390/ijms23094478

This article focuses on the core role of the transcription factor MAFA in maintaining the function of pancreatic islet β cells. MAFA is closely related to insulin expression and the β -cell maturation phenotype. Its down-regulation can lead to β -cell dedifferentiation and cause type 2 diabetes. Studying the regulatory mechanism of MAFA is of great significance for the treatment of diabetes and the protection of β -cell function.

3. Kaneto, Hideaki, et al. "A Crucial Role of MafA as a Novel Therapeutic Target for Diabetes." Journal of Biological Chemistry 280.15 (2005): 15047-15052.https://www.jbc.org/article/S0021-9258(20)66031-8/fulltext

Studies have shown that the β -cell-specific transcription factor MafA, in synergy with PDX-1 and NeuroD, can significantly activate the expression of insulin genes in the liver. In diabetes models, the combined treatment of three factors can effectively improve glucose tolerance, suggesting that MafA antibody detection may become a research tool for new targets in diabetes treatment.

4. Lecoin, Laure, et al. "Mafa-dependent GABAergic activity promotes mouse neonatal apneas." Nature Communications 13.1 (2022): 3284. https://doi.org/10.1038/s41467-022-30825-3

Research has found that the phosphorylated deletion mutant of Mafa protein (Mafa4A) causes neonatal apnea by enhancing the activity of GABAergic neurons. Mafa antibody detection confirmed that this transcription factor regulates the activity of the Gad2 promoter. Its abnormal expression may cause asphyxia by affecting the inhibitory neurons around the nucleus of the sublingual movement, leading to dysregulation of the upper respiratory tract muscle groups.

5. Zhu, Yaxi, et al. "PDX1, Neurogenin-3, and MAFA: critical transcription regulators for beta cell development and regeneration." Stem cell research & therapy 8.1 (2017): 240. https://doi.org/10.1186/s13287-017-0694-z

The article indicates that PDX1, NEUROG3 and MAFA are key transcription factors regulating β -cell development and insulin expression. Studies have shown that the detection of MAFA antibodies can verify its binding characteristics to insulin gene enhancers, which provides an important molecular target for β -cell regeneration therapy.

Creative Biolabs: MAFA Antibodies for Research

Creative Biolabs specializes in the production of high-quality MAFA antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom MAFA Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our MAFA antibodies, custom preparations, or technical support, contact us at email.

Reference

Fottner, Christian, et al. "Second MAFA variant causing a phosphorylation defect in the transactivation domain and familial insulinomatosis." Cancers 14.7 (2022): 1798. https://doi.org/10.3390/cancers14071798