SLAMF7 Antibodies

Structure of SLAMF7

SLAMF7 is an immune regulatory receptor protein. Its molecular weight varies depending on the degree of glycosylation. The molecular weight of the transmembrane form is approximately 37-42 kDa, while that of the soluble form is approximately 33 kDa. There are certain differences in its molecular weight among different species.

The SLAMF7 protein is composed of 331 amino acids and has a typical type I transmembrane protein structure. Its extracellular region contains an N-terminal IgV-like domain and a C-terminal IgC2-like domain, which are responsible for binding to homologous receptors or other ligands. The intracellular region contains an immunoreceptor tyrosine-based switch motif (ITSM), which can recruit adaptor proteins such as SAP or EAT-2, thereby transducing activating or inhibitory signals. This protein is expressed on the surface of natural killer (NK) cells and cytotoxic T lymphocytes, and plays a core role in tumor immune surveillance by regulating the formation and stability of immune synapses.

Fig. 1 Expression and engagement of SLAMF7 on human CD8+ T cells.¹

Key structural properties of SLAMF7:

• Extracellular immunoglobulin-like domain
• Single transmembrane α-helical structure
• Intracellular immune receptor tyrosine motif
• Dependence on glycosylation for functional regulation

Functions of SLAMF7

The main function of SLAMF7 (also known as CRACC or CS1) is to regulate the activation and inhibition of immune cells, playing a central role in cell-mediated cytotoxicity. It is also involved in maintaining immune homeostasis and tumor immune surveillance.

Similar to many immune receptors, the function of SLAMF7 is background-dependent: its signal output depends on the cell type, the microenvironment of ligand interactions, and the available intracellular signaling molecules. This characteristic enables it to flexibly regulate the intensity and direction of the immune response.

Applications of SLAMF7 and SLAMF7 Antibody in Literature

1. Wu, Yongjian, et al. "SLAMF7 regulates the inflammatory response in macrophages during polymicrobial sepsis." The Journal of Clinical Investigation 133.6 (2023). https://doi.org/10.1172/JCI150224

The study found that SLAMF7, in sepsis, inhibits the ubiquitination of TRAF6 by binding to SHIP1, thereby negatively regulating the excessive inflammatory response of macrophages mediated by TLRs and reducing organ damage. This provides a new perspective for the treatment of sepsis.

2. Chu, Emily, et al. "SLAMF7 as a promising immunotherapeutic target in multiple myeloma treatments." Current Oncology 30.9 (2023): 7891-7903. https://doi.org/10.3390/curroncol30090573

Research has revealed that SLAMF7 is an important therapeutic target for multiple myeloma. Monoclonal antibodies targeting this protein have shown efficacy in clinical trials. This article reviews its structure, function, latest clinical progress, and combined treatment strategies, aiming to provide new strategies for improving the prognosis of multiple myeloma.

3. Zhou, Dianrong, et al. "SLAMF7 regulates goblet cell mucus production and negatively impacts gut homeostasis and commensalism." Gut Microbes 17.1 (2025): 2527857. https://doi.org/10.1080/19490976.2025.2527857

This study reveals the regulatory role of SLAMF7 in intestinal inflammation. The absence of SLAMF7 activates C1q+ M2-type macrophages through the STAT6-MafB pathway, promoting goblet cell formation and thickening of the mucus barrier, thereby alleviating intestinal inflammation and regulating the stability of the microbiota.

4. Stewart, Georgia, et al. "An oncolytic adenovirus targeting SLAMF7 demonstrates anti-myeloma efficacy." Leukemia (2025): 1-15. https://doi.org/10.1038/s41375-025-02617-3

This study developed a oncolytic adenovirus Ad[CE1A] targeting the SLAMF7 promoter. This virus can specifically infect and replicate in multiple myeloma cells, killing the tumor by inducing immunogenic cell death and other methods. It has shown significant efficacy both in vitro and in vivo.

5. Pellegrini, Joaquín Miguel, et al. "SLAMF7 and SLAMF8 receptors shape human plasmacytoid dendritic cell responses to intracellular bacteria." The Journal of Clinical Investigation 135.8 (2025). https://doi.org/10.1172/JCI182467

The research has found that SLAMF7/8 plays a crucial role in the ability of human plasmacytoid dendritic cells (pDCs) to resist bacterial infections such as those caused by Salmonella. They regulate the levels of reactive oxygen species in mitochondria and activate pathways such as NF-κB to enhance the function of pDCs and finely modulate the immune response, thereby influencing the course of the infection.

Creative Biolabs: SLAMF7 Antibodies for Research

Creative Biolabs specializes in the production of high-quality SLAMF7 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom SLAMF7 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 SLAMF7 antibodies, custom preparations, or technical support, contact us at email.