BCAM Antibodies

Structure of BCAM

BCAM is a transmembrane immunoglobulin protein with a molecular weight of approximately 70-80 kDa. Its precise molecular weight varies slightly depending on the degree of glycosylation modification. This protein exhibits high structural conservation across different species, but there are differences in key amino acids in specific functional domains.

The BCAM protein is composed of multiple immunoglobulin-like (Ig-like) domains, forming a typical "beaded" spatial conformation. Its extracellular region contains highly conserved laminin binding sites (located at the junction of domains 2-3), while the transmembrane region is anchored to the cell membrane by hydrophobic amino acids. The key functional residues include arginine at position 132 (involved in ligand recognition) and cysteine at position 198 (maintaining disulfide bond stability), and these features collectively maintain its cell adhesion function. The glycosylation modification on the surface of proteins (especially N-linked sugar chains) significantly affects their interaction ability with the microenvironment.

Fig. 1 Molecular modeling of the transmembrane dimerization region of Lu/BCAM.¹

Key structural properties of BCAM:

• Immunoglobulin-like (Ig-like) domains
• Conserved laminin binding sites
• Transmembrane hydrophobic zone
• Regulatory disulfide bonds
• N-glycosylation modification site

Functions of BCAM

The core function of the BCAM gene-encoded protein is to mediate cell adhesion and signal transduction, and it also plays a key role in various pathophysiological processes.

The binding curve of BCAM to its ligand shows typical allosteric effect characteristics. The conformational change of its third immunoglobulin domain can significantly improve the binding efficiency of laminin. This feature enables it to play a dual role as both a "molecular sensor" and a "mechanical transducer" in tissue repair and pathological processes.

Applications of BCAM and BCAM Antibody in Literature

1. Piteau, Marianne, et al. "Lu/BCAM adhesion glycoprotein is a receptor for Escherichia coli Cytotoxic Necrotizing Factor 1 (CNF1)." PLoS pathogens 10.1 (2014): e1003884.https://doi.org/10.1371/journal.ppat.1003884

Research has found that the cell receptor of the pathogenic Escherichia coli toxin CNF1 is Lutheran adhesion glycoprotein/basal cell adhesion molecule (Lu/BCAM). Experiments have confirmed that the 720-1014 amino acid region of CNF1 binds to Lu/BCAM, a receptor that is crucial for toxin-binding cells and co-mediates toxin action with p37LRP.

2. Zhao, Junjie, et al. "Integrated multi-omics analyses reveal that BCAM is associated with epigenetic modification and tumor microenvironment subtypes of clear cell renal cell carcinoma." Clinical Epigenetics 14.1 (2022): 99.https://doi.org/10.1186/s13148-022-01319-2

Research has found that in clear cell renal cell carcinoma (ccRCC), low expression of BCAM is associated with a poor prognosis and is significantly linked to BAP1 mutations and CpG methylation levels. Patients with low BCAM expression have enhanced immune infiltration and may benefit more from immunotherapy, while those with high BCAM expression are enriched with angiogenic pathways and are more sensitive to anti-angiogenic drugs. BCAM can serve as a potential biomarker for the prognosis and treatment options of ccRCC.

3. Akiyama, Hirotada, et al. "The FBI1/Akirin2 target gene, BCAM, acts as a suppressive oncogene." PLoS One 8.11 (2013): e78716.https://doi.org/10.1371/journal.pone.0078716

Research has found that BCAM is a laminin α5 receptor and has a tumor suppressor effect in liver cancer. Research has found that the 14-3-3β-FBI1/Akirin2 complex promotes the malignant phenotype of tumors by inhibiting BCAM transcription, indicating that the down-regulation of BCAM is associated with the occurrence and metastasis of liver cancer.

4. Jin, Juan, et al. "Upregulation of BCAM and its sense lncRNA BAN are associated with gastric cancer metastasis and poor prognosis." Molecular oncology 14.4 (2020): 829-845. https://doi.org/10.1002/1878-0261.12638

Studies have found that BCAM is highly expressed in metastatic gastric cancer and is associated with a poor prognosis. Studies have found that BCAM and its antisense lncRNA BAN jointly promote gastric cancer metastasis. BAN enhances tumor invasion ability by regulating BCAM expression. Both can serve as potential markers and therapeutic targets for gastric cancer metastasis.

5. Miura, Yasushi, et al. "Differential expression of Lutheran/BCAM regulates biliary tissue remodeling in ductular reaction during liver regeneration." Elife 7 (2018): e36572. https://doi.org/10.7554/eLife.36572

Research has found that the Lutheran/BCAM protein dominates the morphogenesis of bile duct response (DR) in liver injury models by regulating the motility and ductal formation ability of bile duct cells. Lu-deficient mice exhibited severe DR Defects, indicating that Lu/BCAM is a key regulatory factor for the phenotypic heterogeneity of DR In different liver disease models.

Creative Biolabs: BCAM Antibodies for Research

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

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