MATK Antibodies

Structure of MATK

MATK is a tyrosine kinase with a molecular weight of approximately 56 kDa. Its molecular weight remains relatively stable across different species, with the main differences coming from minor variations in the regulatory domain.

MATK is composed of approximately 500 amino acids and has a typical kinase folding structure, including the N-terminal SH3 domain (mediating protein interactions), the central SH2 domain (binding phosphorylated tyrosine), and the C-terminal kinase domain (catalytic phosphorylation). Its activity is regulated by its own phosphorylation and plays a key role in the T-cell receptor signaling pathway. The crystal structure analysis of MATK reveals its self-inhibition mechanism, providing a structural basis for the design of targeted drugs.

Fig. 1 Nucleotide and deduced amino acid sequence of the human MATK gene.¹

Key structural properties of MATK:

• SH3-SH2- kinase domain modular architecture
• Self-inhibitory conformation
• Key phosphorylation sites (Tyr394/Tyr504)

Functions of MATK

The core function of the MATK gene is to regulate immune cell signal transduction and neural development processes, and it is also involved in multiple pathophysiological mechanisms.

The kinase activity of MATK exhibits typical substrate-specific phosphorylation characteristics. Compared with other tyrosine kinases (such as Lck and Fyn), its signal kinetics shows more precise threshold regulation characteristics, which makes it a precise regulator of immune synaptic signal transduction. The latest research has found that MATK forms signal micro-regions through a phase separation mechanism, further enhancing the specificity of its signal transduction.

Applications of MATK and MATK Antibody in Literature

1. Maybee, Deanna V., et al. "MMP-2 regulates Src activation via repression of the CHK/MATK tumor suppressor in osteosarcoma." Cancer Reports 7.2 (2024): e1946. https://doi.org/10.1002/cnr2.1946

This study reveals that MMP-2 regulates Src kinase activity and promotes osteosarcoma cell migration by inhibiting its endogenous inhibitor CHK/MATK. Experiments have shown that inhibiting MMP-2 or overexpressing CHK/MATK can reverse doxorubicin-induced migration, suggesting that targeting the MMP-2-CHK/MATK pathway can enhance the efficacy of doxorubicin and inhibit osteosarcoma metastasis.

2. Zhong, Cheng, et al. "Prognostic Function and Immunologic Landscape of a Predictive Model Based on Five Senescence-Related Genes in IPF Bronchoalveolar Lavage Fluid." Biomedicines 12.6 (2024): 1246. https://doi.org/10.3390/biomedicines12061246

This study constructed a prognostic model of idiopathic pulmonary fibrosis based on five aging-related genes (including megakaryocyte-associated tyrosine kinase MATK), verifying that the model can effectively predict the risk stratification of patients and revealing that the increased infiltration of neutrophils and other immune cells in the alveolar lavage fluid of high-risk group patients is associated with a poor prognosis.

3. Deng, Bijia, et al. "Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product." Journal of Biological Chemistry 270.4 (1995): 1833-1842. https://doi.org/10.1074/jbc.270.4.1833

In this study, human and murine MATK genes (megakaryocyte-associated tyrosine kinases) were successfully cloned and identified, revealing that they regulate the activity of Src family kinases through the SH3/SH2 domain and ATP binding sites. Experiments have confirmed that MATK can phosphorylate the C-terminal tyrosine of Src protein, and antisense oligonucleotide inhibition significantly reduces the proliferation of megakaryocyte progenitor cells, indicating that it plays a key regulatory role in the megakaryocyte growth and differentiation signaling pathway.

4. Advani, Gahana, et al. "Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine." Cell Communication and Signaling 15.1 (2017): 29. https://doi.org/10.1186/s12964-017-0186-x

This study reveals the dual mechanism differences in the inhibition of Src family kinases (SFKs) by Csk and Chk (MATK) : Csk mainly inhibits SFKs by catalyzing C-terminal tyrosine phosphorylation, while Chk (MATK) relies on high-affinity binding in the kinase domain to achieve non-catalytic inhibition. In colorectal cancer cells, the absence of Chk leads to the excessive activation of SFKs, confirming the key role of its non-catalytic inhibitory mechanism in regulating tumor growth.

5. Zrihan-Licht, Sheila, et al. "Association of csk-homologous kinase (CHK)(formerly MATK) with HER-2/ErbB-2 in breast cancer cells." Journal of Biological Chemistry 272.3 (1997): 1856-1863. https://doi.org/10.1074/jbc.272.3.1856

This study reveals that CHK (MATK) is a tyrosine kinase that is highly expressed in breast cancer tissues but not detected in normal tissues. Research has found that CHK specifically binds to Heregulin-activated ErbB-2 through its SH2 domain and may be involved in breast cancer signaling.

Creative Biolabs: MATK Antibodies for Research

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

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