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Mouse Anti-CD55 Recombinant Antibody (CBT2552) (V2LY-0625-LY2806)


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Tested Data
Mouse Anti-CD55 Recombinant Antibody (CBT2552) (V2LY-0625-LY2806) in WB
Mouse Anti-CD55 Recombinant Antibody (CBT2552) (V2LY-0625-LY2806) in WB
Mouse Anti-CD55 Recombinant Antibody (CBT2552) (V2LY-0625-LY2806) in WB
Mouse Anti-CD55 Recombinant Antibody (CBT2552) (V2LY-0625-LY2806) in WB
Mouse Anti-CD55 Recombinant Antibody (CBT2552) (V2LY-0625-LY2806) in FC
Mouse Anti-CD55 Recombinant Antibody (CBT2552) (V2LY-0625-LY2806) in FC
Mouse Anti-CD55 Recombinant Antibody (CBT2552) (V2LY-0625-LY2806) in ELISA
Mouse Anti-CD55 Recombinant Antibody (CBT2552) (V2LY-0625-LY2806) in ELISA

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBT2552
Antibody Isotype
IgG1
Application
WB, FC

Basic Information

Immunogen
Purified recombinant fragment of human CD55 (AA: 238-357) expressed in E. Coli.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:500-1:2,000
FC1:200-1:400
ELISA1:10,000

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

Format
Liquid
Buffer
PBS
Preservative
Sodium azide
Concentration
Batch dependent
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Entrez Gene ID
1604
UniProt ID
P08174
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.
More Infomation

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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