SLC3A2 Antibodies

Structure of SLC3A2

SLC3A2 protein is a type II transmembrane glycoprotein with a molecular weight of approximately 80 kDa. Its precise molecular weight varies slightly among different species due to differences in the degree of glycosylation.

This protein is composed of approximately 529 amino acids, and its structure includes a relatively short intracellular N-terminal, a hydrophobic transmembrane domain, and a large extracellular C-terminal domain. Its extracellular region covalently binds to the corresponding light chain proteins (such as SLC7A5) through disulfide bonds, forming a functional heterodimer transport complex. This structure determines that it does not directly transport substrates itself, but acts as a molecular chaperone and anchoring protein, responsible for accurately targeting and stabilizing light chains on the cell membrane, thereby achieving the coordinated transport of essential amino acids such as leucine and phenylalanine, which is crucial for cell growth, proliferation and metabolic regulation.

Fig. 1 Modeling the SLC3A2-P62 Complex Using AlphaFold2 and Molecular Docking.¹

Key structural properties of SLC3A2:

• Single-pass transmembrane topology
• Bulky glycosylated extracellular domains
• Heterodimers are formed with light chain proteins through disulfide bonds
• As chaperone subunit, it ensures the correct assembly of transport complex and membrane positioning

Functions of SLC3A2

The primary function of the SLC3A2 protein is to serve as a regulatory subunit of amino acid transporters, but it is also involved in a variety of key cellular physiological processes, including immune regulation, cell adhesion, and signal transduction.

Unlike classic transport proteins with a single function, SLC3A2 (CD98hc) exhibits a high degree of "platform" and "hub" characteristics. By combining different light chain partners, it endows cells with differentiated amino acid uptake capabilities, enabling their functions to be dynamically regulated according to cell types and physiological/pathological conditions. It integrates multiple aspects such as nutrient transport, cell signaling, and intercellular communication.

Applications of SLC3A2 and SLC3A2 Antibody in Literature

1. Zhang, Cunjie, et al. "SLC3A2 N-glycosylation and Golgi remodeling regulate SLC7A amino acid exchangers and stress mitigation." Journal of Biological Chemistry 299.12 (2023): 105416. https://doi.org/10.1016/j.jbc.2023.105416

The article indicates that the N-glycosylation sites (N365 and N381) of SLC3A2, after being modified by Golgi bodies, respectively regulate endocytosis and membrane surface retention, affecting the assembly of amino acid transport complexes and cellular metabolic balance, thereby playing different roles in growth and stress responses.

2. Nachef, Marianna, et al. "Targeting SLC1A5 and SLC3A2/SLC7A5 as a potential strategy to strengthen anti-tumor immunity in the tumor microenvironment." Frontiers in immunology 12 (2021): 624324. https://doi.org/10.3389/fimmu.2021.624324

The article indicates that the tumor microenvironment (TME) metabolism inhibits the function of immune cells. By up-regulating amino acid transporters such as SLC1A5, SLC7A5 and SLC3A2, the metabolic capacity and effector function of CAR-T/NK cells can be enhanced, and the mTORC1 pathway can be activated, thereby improving the efficacy of immunotherapy.

3. Xiang, Peng, et al. "Metabolite Neu5Ac triggers SLC3A2 degradation promoting vascular endothelial ferroptosis and aggravates atherosclerosis progression in ApoE-/-mice." Theranostics 13.14 (2023): 4993. https://doi.org/10.7150/thno.87968

Research has revealed that the metabolite Neu5Ac induces ferroptosis and inflammatory damage in vascular endothelial cells by mediating the ubiquitination and degradation of SLC3A2, thereby promoting the progression of atherosclerotic plaques and providing new targets and ideas for the prevention and treatment of cardiovascular diseases.

4. Ren, Yimin, et al. "SSRP1/SLC3A2 Axis in Arginine Transport: A New Target for Overcoming Immune Evasion and Tumor Progression in Peripheral T‐Cell Lymphoma." Advanced Science 12.21 (2025): 2415698. https://doi.org/10.1002/advs.202415698

Research has revealed that SLC3A2-mediated arginine uptake promotes the malignant progression and immune escape of peripheral T-cell lymphoma. Quinacillin inhibits SLC3A2 by targeting SSRP1, down-regulates arginine levels, and demonstrates significant anti-tumor potential in combination with HDAC inhibitors.

5. Chen, Lin-Yun, et al. "RNA-binding protein YBX3 promotes PPARγ-SLC3A2 mediated BCAA metabolism fueling brown adipogenesis and thermogenesis." Molecular Metabolism 90 (2024): 102053. https://doi.org/10.1016/j.molmet.2024.102053

Research has revealed that the RNA-binding protein YBX3 stabilizes the mRNA of SLC3A2 and Pparg, promoting the intake and decomposition of branched-chain amino acids by brown adipocytes and providing energy for mitochondrial heat production, thereby resisting obesity and related metabolic disorders.

Creative Biolabs: SLC3A2 Antibodies for Research

Creative Biolabs specializes in the production of high-quality SLC3A2 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom SLC3A2 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 SLC3A2 antibodies, custom preparations, or technical support, contact us at email.