CEACAM5 Antibodies

Structure of CEACAM5

CEACAM5 is a cell surface glycoprotein with a molecular weight of approximately 180-200 kDa. This difference mainly stems from the varying degrees of glycosylation modification.

This protein is composed of 702 amino acids, and its extracellular region contains 7 immunoglobulin-like domains (N-A1-A2-B1-B2-C-Y). The third domain (A2) mediates homodimerization, while the N-terminal domain is responsible for ligand recognition. The characteristic structure of CEACAM5 is its GPI anchoring region, which enables the protein to anchor on the cell membrane. The antigenic epitopes of this protein are mainly located in its glycosylated modification region, which is also the molecular basis for its use as a tumor marker.

Fig. 1 Molecular docking confirmed the interaction between CEACAM5 (green) and Galectin-9 (blue).¹

Key structural properties of CEACAM5:

• Extracellular region contains seven immunoglobulin domain sample structure
• The third immunoglobulin domain (A2) mediates homodimerization
• The N-terminal domain is responsible for specific ligand recognition and binding
• GPI anchor module will protein C end is fixed on the membrane surface
• Highly glycosylation antigen epitope area to form the immune detection basis

Functions of CEACAM5

The main function of CEACAM5 is to mediate intercellular recognition and adhesion, and it plays a significant role in tumor development.

The adhesion function of CEACAM5 depends on the specific interaction of its extracellular immunoglobulin-like domain, a characteristic that enables it to play a dual role in cell communication and tumor biology.

Applications of CEACAM5 and CEACAM5 Antibody in Literature

. Ajkunic, Azra, et al. "Assessment of TROP2, CEACAM5 and DLL3 in metastatic prostate cancer: Expression landscape and molecular correlates." npj Precision Oncology 8.1 (2024): 104. https://doi.org/10.1038/s41698-024-00599-6

Studies have shown that in castration-resistant prostate cancer (CRPC), CEACAM5 is most expressed in the neuroendocrine subtype (NEPC), and its expression level is regulated by epigenetic states (such as H3K27me3 modification). This discovery provides a new direction for the development of targeted therapies against CEACAM5.

. Bechmann, Marc B., et al. "Heterogeneity of CEACAM5 in breast cancer." Oncotarget 11.43 (2020): 3886. https://doi.org/10.18632/oncotarget.27778

Studies have shown that in breast cancer, CEACAM5 is overexpressed in most ER-positive and HER2-overexpressed subtypes, but it is mostly negative in triple-negative breast cancer. Research has found that cancer cells expressing CEACAM5 have relatively low invasiveness, but they show heterogeneous expression in both the primary lesion and metastatic lymph nodes. The impact of this protein on patient prognosis varies by molecular subtype, suggesting that it plays a complex and context-dependent role in breast cancer.

. Seckinger, Anja, et al. "Targeting CEACAM5-positive solid tumors using NILK-2401, a novel CEACAM5xCD47 κλ bispecific antibody." Frontiers in Immunology 15 (2024): 1378813. https://doi.org/10.3389/fimmu.2024.1378813

Studies have shown that NILK-2401 is a bispecific antibody targeting CEACAM5 and CD47. It precisely blocks CD47 on the surface of tumor cells by binding to CEACAM5, thereby activating the phagocytosis and killing of tumors by immune cells. Preclinical studies have shown that this drug can effectively eliminate CEACam5-positive tumors, and due to its targeting characteristics, it avoids hematological toxic and side effects, demonstrating good therapeutic potential.

. Seckinger, Anja, et al. "Development and characterization of NILK-2301, a novel CEACAM5xCD3 κλ bispecific antibody for immunotherapy of CEACAM5-expressing cancers." Journal of Hematology & Oncology 16.1 (2023): 117. https://doi.org/10.1186/s13045-023-01516-3

Studies have shown that NILK-2301 is a bispecific antibody targeting CEACAM5 and CD3, which can effectively activate T cells and kill CEACam5-positive colorectal cancer, gastric cancer and lung cancer cells. Its unique structure is designed to reduce immunogenicity. Preclinical studies have shown that it has good anti-tumor activity and safety, and it is expected to enter clinical trials by the end of 2023.

. Shi, Haojun, Yiusing Tsang, and Yisi Yang. "Identification of CEACAM5 as a stemness-related inhibitory immune checkpoint in pancreatic cancer." BMC cancer 22.1 (2022): 1291. https://doi.org/10.1186/s12885-022-10397-7

Research has found that in pancreatic cancer, CEACAM5 is an immunosuppressive molecule related to the characteristics of tumor stem cells. Its high expression is associated with strong tumor invasiveness, M1 macrophage infiltration and poor prognosis of patients. The function of CEACAM5 may be regulated by the metabolic processes of prostaglandins and long-chain unsaturated fatty acids, suggesting that it can serve as a new target for precise immunotherapy against tumor heterogeneity.

Creative Biolabs: CEACAM5 Antibodies for Research

Creative Biolabs specializes in the production of high-quality CEACAM5 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom CEACAM5 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 CEACAM5 antibodies, custom preparations, or technical support, contact us at email.