Human Recombinant CD55 protein, hFc Tag (V2LY-0526-LY2901)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
hFc Tag
Protein Construction
This product is Human Recombinant CD55 protein, hFc Tag consist of Amino Acid: 1-353 and predicts a molecular mass of 61.7 kDa.
Molecule Mass
61.7 kDa
Verified
HPLC
Sequence
Amino Acid: 1-353
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥90% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
CD55 molecule (Cromer blood group)
Research Area
Immunology
Function
This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade (PubMed:7525274).
Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage (PubMed:28657829).
(Microbial infection) Acts as a receptor for Coxsackievirus A21, coxsackieviruses B1, B3 and B5.
(Microbial infection) Acts as a receptor for Human enterovirus 70 and D68 (Probable).
(Microbial infection) Acts as a receptor for Human echoviruses 6, 7, 11, 12, 20 and 21.
Biological Process
Complement activation, classical pathway
Innate immune response
Negative regulation of complement activation
Positive regulation of CD4-positive, alpha-beta T cell activation
Positive regulation of CD4-positive, alpha-beta T cell proliferation
Positive regulation of cytosolic calcium ion concentration
Positive regulation of T cell cytokine production
Regulation of complement activation
Regulation of complement-dependent cytotoxicity
Regulation of lipopolysaccharide-mediated signaling pathway
Respiratory burst
Cellular Location
Isoform 1
Cell membrane ; Single-pass type I membrane protein
Isoform 2
Cell membrane ; Lipid-anchor, GPI-anchor
Isoform 3
Secreted
Isoform 4
Secreted
Isoform 5
Secreted
Isoform 6
Cell membrane
Isoform 7
Cell membrane
Involvement in disease
Complement hyperactivation, angiopathic thrombosis, and protein-losing enteropathy (CHAPLE):
An autosomal recessive disease characterized by abdominal pain and diarrhea, primary intestinal lymphangiectasia, edema due to hypoproteinemia, malabsorption, and less frequently, bowel inflammation, recurrent infections, and angiopathic thromboembolic disease. Patients' T lymphocytes show increased complement activation causing surface deposition of complement and the generation of soluble C5a.
PTM
The Ser/Thr-rich domain is heavily O-glycosylated.

Moreira, M., Ruggiero, A., Iaccarino, E., Barra, G., Sandomenico, A., Ruvo, M., & Berisio, R. (2021). A structure-based approach for the development of a bicyclic peptide acting as a miniaturized anti-CD55 antibody. International Journal of Biological Macromolecules, 182, 1455-1462.

Niu, M., Xu, S., Yang, J., Yao, D., Li, N., Yan, J., ... & Song, G. (2021). Structural basis for CD97 recognition of the decay-accelerating factor CD55 suggests mechanosensitive activation of adhesion GPCRs. Journal of Biological Chemistry, 296.

Lin, W. D., Fan, T. C., Hung, J. T., Yeo, H. L., Wang, S. H., Kuo, C. W., ... & Alice, L. Y. (2020). Sialylation of CD55 by ST3GAL1 facilitates immune evasion in cancer. Cancer Immunology Research.

Pérez‐Alós, L., Bayarri‐Olmos, R., Skjoedt, M. O., & Garred, P. (2019). Combining MAP‐1: CD35 or MAP‐1: CD55 fusion proteins with pattern‐recognition molecules as novel targeted modulators of the complement cascade. The FASEB Journal, 33(11), 12723-12734.

Musarrat, T. (2019). Modulation of IL-10 production by CD3/CD55 induced Type 1 regulatory (Tr1) T-cells (Doctoral dissertation, University of Nottingham).

Loniewska‐Lwowska, A., Koza, K., Mendek‐Czajkowska, E., Wieszczy, P., Adamowicz‐Salach, A., Branicka, K., ... & Fabijanska‐Mitek, J. (2018). Diminished presentation of complement regulatory protein CD 55 on red blood cells from patients with hereditary haemolytic anaemias. International journal of laboratory hematology, 40(2), 128-135.

Dho, S. H., Lim, J. C., & Kim, L. K. (2018). Beyond the role of CD55 as a complement component. Immune network, 18(1).

Li, G., Yin, Q., Ji, H., Wang, Y., Liu, H., Jiang, L., ... & Li, B. (2018). A study on screening and antitumor effect of CD55-specific ligand peptide in cervical cancer cells. Drug design, development and therapy, 12, 3899.

Ozen, A., Comrie, W. A., Ardy, R. C., Domínguez Conde, C., Dalgic, B., Beser, Ö. F., ... & Lenardo, M. J. (2017). CD55 deficiency, early-onset protein-losing enteropathy, and thrombosis. New England Journal of Medicine, 377(1), 52-61.

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For research use only. Not intended for any clinical use.

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