CD55 Antibodies

Structure of CD55

CD55 is a glycosylated membrane protein with a relatively small molecular weight. The molecular weight of its core polypeptide is approximately 35-40 kDa. However, due to different degrees of glycosylation, the actual molecular weight varies within the range of 55-75 kDa. This difference mainly stems from the degree of modification of multiple N-linked and O-linked glycosylation sites in its amino acid sequence.

This protein is composed of a polypeptide chain of approximately 350 amino acid residues, and its primary structure folds into a characteristic short common repeat sequence (SCR domain), usually containing four such domains. The protein structure of CD55 is anchored to the cell membrane by a glycosylphosphatidylinositol (GPI) at the C-terminal, and this anchoring method makes it fluid on the membrane. The SCR domain at its N-terminal is responsible for interacting with complement proteins and performs regulatory functions by accelerating the decay of C3/C5 convertase. The N-linked and O-linked sugar chains on the surface of proteins not only contribute to their apparent molecular weight, but also directly participate in their specific recognition with complement components.

Fig. 1 The CD97–CD55 binding pattern and our chimeric construct.¹

Key structural properties of CD55:

• By multiple short of tandem repeat (SCR) structure domain constitute extracellular region
• Anchored to the cell membrane surface by glycosylphosphatidylinositol (GPI)
• SCR domains mediate specific binding to complement components C3/C4b

Functions of CD55

The core function of CD55 is to protect host cells from accidental damage by the complement system, and its mechanism of action also involves multiple immune regulatory processes.

The regulation of complement by CD55 does not rely on other cofactors. This autonomous mechanism of action enables it to respond rapidly to complement activation signals in the microenvironment, ensuring the immediality of cell protection.

Applications of CD55 and CD55 Antibody in Literature

1. Shakya, Bikash, et al. "Erythrocyte CD55 mediates the internalization of Plasmodium falciparum parasites." Elife 10 (2021): e61516. https://doi.org/10.7554/eLife.61516

The article indicates that research on the invasion of red blood cells by Plasmodium falciparum has found that CD55 is a key factor in the internalization process of the parasite. This protein plays a role in the mobile connection stage, does not affect the previous attachment but is necessary for invasion. Its function is broad-spectrum, suggesting that CD55 and related pathways can serve as potential therapeutic targets for malaria.

2. Li, L., et al. "CD55 is over-expressed in the tumour environment." British journal of cancer 84.1 (2001): 80-86. https://doi.org/10.1054/bjoc.2000.1570

Studies have shown that CD55 is significantly upregulated in tumor cells and stroma. The CD55 on the surface of tumor cells can be a hundred times higher than that of normal cells and can be deposited in the extracellular matrix. This high expression characteristic in the tumor environment makes it an ideal target for tumor imaging and immunotherapy.

3. Mikesch, Jan-Henrik, et al. "The expression and action of decay‐accelerating factor (CD55) in human malignancies and cancer therapy." Analytical Cellular Pathology 28.5-6 (2006): 223-232. https://doi.org/10.1155/2006/814816

Studies have shown that CD55 is highly expressed in various malignant tumors, and its function far exceeds immune regulation. It promotes tumorigenesis, angiogenesis, metastasis and helps tumor cells escape through multiple signaling pathways, and thus has become a highly promising new target for cancer treatment.

4. Gaykema, Lonneke H., et al. "Inhibition of complement activation by CD55 overexpression in human induced pluripotent stem cell derived kidney organoids." Frontiers in Immunology 13 (2023): 1058763. https://doi.org/10.3389/fimmu.2022.1058763

Studies have shown that to address immune rejection in stem cell-derived kidney transplantation, human-induced pluripotent stem cell lines overexpressing CD55 have been constructed. The results show that CD55 can effectively inhibit complement activation, providing a novel protective strategy against humoral immunity for tissue transplantation.

5. Kaneko, Kazuyo, et al. "The active form of Helicobacter pylori vacuolating cytotoxin induces decay‐accelerating factor CD55 in association with intestinal metaplasia in the human gastric mucosa." The Journal of pathology 258.2 (2022): 199-209. https://doi.org/10.1002/path.5990

Studies have shown that infection with Helicobacter pylori vacA i1 strain can induce an increase in the expression of CD55 in gastric mucosa and is associated with intestinal metaplasia. CD55 partially regulates inflammatory responses in gastric epithelial cells, suggesting that it may become a potential target in intestinal metaplasia and gastric cancer management.

Creative Biolabs: CD55 Antibodies for Research

Creative Biolabs specializes in the production of high-quality CD55 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom CD55 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 CD55 antibodies, custom preparations, or technical support, contact us at email.