KMT2A Antibodies

Structure of KMT2A

KMT2A is a nucleoprotein with an extremely high molecular weight. The molecular weight of its human isomer is approximately within the range of 430-550 kDa, with specific values varying depending on different splicing variants. This significant molecular weight difference mainly stems from the diversity of protein domain composition and transcript length.

This protein is composed of over 3,500 amino acid residues, and its primary structure contains multiple highly conserved functional modules. The core feature of the KMT2A protein structure is the presence of a catalytically active SET domain, which is responsible for catalyzing the methylation modification of lysine at the 4th position of histone H3. The C-terminal of a protein usually contains a FYRN domain related to transcriptional regulation, while the N-terminal contains multiple XX repeat sequences. These regions jointly mediate protein-protein and protein-DNA interactions. Its tertiary structure is maintained stable through multiple zinc finger molds, forming a functional scaffold capable of recruiting various transcriptional cofactors.

Fig. 1 Schematic representation of KTM2A gene structure and cofactors.¹

Key structural properties of KMT2A:

• Extended conformation composed of multiple domains
• SET domain structure constitute the catalytic activity center
• Multiple zinc finger modalities mediate nucleic acid interactions

Functions of KMT2A

The core function of the KMT2A protein is to regulate gene transcription as a histone methyltransferase. Its main physiological functions and pathological significance are as follows:

The methylation function of KMT2A depends on its specific binding to nucleosomes. This mode of action is independent of DNA sequence characteristics, reflecting the unique nature of epigenetic regulation and making it a key molecular hub connecting chromatin state and gene expression.

Applications of KMT2A and KMT2A Antibody in Literature

1. Guarnera, Luca, et al. "KMT2A rearrangements in leukemias: molecular aspects and therapeutic perspectives." International journal of molecular sciences 25.16 (2024): 9023. https://doi.org/10.3390/ijms25169023

The article indicates that KMT2A gene rearrangement is more common in childhood leukemia, which can easily lead to chemotherapy resistance and a high risk of recurrence, and the survival rate of patients is generally low. The current treatment strategies include intense chemotherapy, targeted therapy and hematopoietic stem cell transplantation. In particular, transplantation has shown remarkable effects on some children. This article reviews the variant types, clinical features and treatment progress of KMT2A.

2. Ogino, Jayme, and Yali Dou. "Histone methyltransferase KMT2A: Developmental regulation to oncogenic transformation." Journal of Biological Chemistry 300.10 (2024): 107791. https://doi.org/10.1016/j.jbc.2024.107791

The article indicates that KMT2A is an important histone methyltransferase, and its abnormal function is closely related to various diseases, especially leukemia. This article reviews the structure and function of KMT2A and its role in development and tumors, and explores the related targeted therapeutic strategies.

3. Yin, Lei, et al. "Recent Developments and Evolving Therapeutic Strategies in KMT2A‐Rearranged Acute Leukemia." Cancer Medicine 13.20 (2024): e70326. https://doi.org/10.1002/cam4.70326

The article indicates that KMT2A gene rearrangement is a common and high-risk variant in acute leukemia, closely related to strong invasiveness and poor prognosis. This review systematically explores the characteristics, mechanisms and clinical status of KMT2A rearrangement leukemia, and looks forward to new targeted and immunotherapy strategies based on its biological characteristics.

4. Cowell, Ian G., and Caroline A. Austin. "DNA fragility at the KMT2A/MLL locus: insights from old and new technologies." Open Biology 13.1 (2023): 220232. https://doi.org/10.1098/rsob.220232

The article indicates that the KMT2A gene is prone to rearrangement in specific regions, especially after treatment with topoisomerase inhibitors (such as etoposide). Although the drug can induce extensive DNA breaks in this area, the clinically observed hotspots of breaks are relatively concentrated, indicating that in addition to direct cleavage, other factors such as the secondary structure of DNA also jointly determine the selection of break sites.

5. Zhang, Changlin, et al. "KMT2A regulates cervical cancer cell growth through targeting VDAC1." Aging (Albany NY) 12.10 (2020): 9604. https://doi.org/10.18632/aging.103229

The article indicates that KMT2A promotes tumor growth in cervical cancer by regulating VDAC1 expression. Inhibiting KMT2A can impede the proliferation and migration of cancer cells and induce apoptosis. Clinical data also show that KMT2A and VDAC1 are co-highly expressed in cancer tissues. This signal axis provides a new target for the research on the mechanism and treatment of cervical cancer.

Creative Biolabs: KMT2A Antibodies for Research

Creative Biolabs specializes in the production of high-quality KMT2A antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom KMT2A 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 KMT2A antibodies, custom preparations, or technical support, contact us at email.