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Rabbit Anti-CD47 Recombinant Antibody (CBFYC-1335) (CBMAB-C1393-FY)

This product is rabbit antibody that recognizes CD47. The antibody CBFYC-1335 can be used for immunoassay techniques such as: ELISA.
See all CD47 antibodies

Summary

Host Animal
Rabbit
Specificity
Human
Clone
CBFYC-1335
Antibody Isotype
IgG
Application
ELISA

Basic Information

Immunogen
Recombinant human CD47 protein
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Buffer
PBS
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
CD47 Molecule
Introduction
CD47 (CD47 Molecule) is a Protein Coding gene. Diseases associated with CD47 include Hereditary Spherocytosis and Neonatal Meningitis. Among its related pathways are Response to elevated platelet cytosolic Ca2+ and Innate Immune System. Gene Ontology (GO) annotations related to this gene include thrombospondin receptor activity.
Entrez Gene ID
UniProt ID
Alternative Names
CD47 Molecule; Antigenic Surface Determinant Protein OA3; CD47 Antigen (Rh-Related Antigen, Integrin-Associated Signal Transducer); Antigen Identified By Monoclonal Antibody 1D8; Leukocyte Surface Antigen CD47; Integrin Associated Protein; Rh-Related Antigen; CD47 Glycoprotein
Function
Has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins. Plays an important role in memory formation and synaptic plasticity in the hippocampus (By similarity).
Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. May play a role in membrane transport and/or integrin dependent signal transduction. May prevent premature elimination of red blood cells. May be involved in membrane permeability changes induced following virus infection.
Biological Process
ATP export Source: ARUK-UCL
Cell migration Source: ARUK-UCL
Cellular response to interferon-gamma Source: ARUK-UCL
Cellular response to interleukin-1 Source: ARUK-UCL
Cellular response to interleukin-12 Source: ARUK-UCL
Extracellular matrix organization Source: Reactome
Integrin-mediated signaling pathway Source: ProtInc
Leukocyte migration Source: Reactome
Monocyte extravasation Source: ARUK-UCL
Negative regulation of Fc-gamma receptor signaling pathway involved in phagocytosis Source: ARUK-UCL
Neutrophil degranulation Source: Reactome
Positive regulation of cell-cell adhesion Source: UniProtKB
Positive regulation of cell population proliferation Source: UniProtKB
Positive regulation of inflammatory response Source: GO_Central
Positive regulation of phagocytosis Source: GO_Central
Positive regulation of stress fiber assembly Source: ARUK-UCL
Positive regulation of T cell activation Source: UniProtKB
Regulation of interferon-gamma production Source: ARUK-UCL
Regulation of interleukin-10 production Source: ARUK-UCL
Regulation of interleukin-12 production Source: ARUK-UCL
Regulation of interleukin-6 production Source: ARUK-UCL
Regulation of nitric oxide biosynthetic process Source: ARUK-UCL
Regulation of tumor necrosis factor production Source: ARUK-UCL
Cellular Location
Cell membrane
Topology
Extracellular: 19-141
Helical: 142-162
Cytoplasmic: 163-176
Helical: 177-197
Extracellular: 198-207
Helical: 208-228
Cytoplasmic: 229-235
Helical: 236-256
Extracellular: 257-268
Helical: 269-289
Cytoplasmic: 290-323

Yu, W. B., Ye, Z. H., Chen, X., Shi, J. J., & Lu, J. J. (2021). The development of small-molecule inhibitors targeting CD47. Drug Discovery Today, 26(2), 561-568.

Lin, A., Razzokov, J., Verswyvel, H., Privat-Maldonado, A., De Backer, J., Yusupov, M., ... & Bogaerts, A. (2021). Oxidation of innate immune checkpoint cd47 on cancer cells with non-thermal plasma. Cancers, 13(3), 579.

Wang, F., Liu, Y. H., Zhang, T., Gao, J., Xu, Y., Xie, G. Y., ... & Yang, Y. G. (2020). Aging‐associated changes in CD47 arrangement and interaction with thrombospondin‐1 on red blood cells visualized by super‐resolution imaging. Aging cell, 19(10), e13224.

Nigro, A., Ricciardi, L., Salvato, I., Sabbatino, F., Vitale, M., Crescenzi, M. A., ... & Dal Col, J. (2020). Enhanced expression of CD47 is associated with off-target resistance to tyrosine kinase inhibitor gefitinib in NSCLC. Frontiers in immunology, 10, 3135.

Logtenberg, M. E., Scheeren, F. A., & Schumacher, T. N. (2020). The CD47-SIRPα immune checkpoint. Immunity, 52(5), 742-752.

Tal, M. C., Torrez Dulgeroff, L. B., Myers, L., Cham, L. B., Mayer-Barber, K. D., Bohrer, A. C., ... & Hasenkrug, K. J. (2020). Upregulation of CD47 is a host checkpoint response to pathogen recognition. Mbio, 11(3), e01293-20.

Hayat, S. M. G., Bianconi, V., Pirro, M., & Sahebkar, A. (2019). Stealth functionalization of biomaterials and nanoparticles by CD47 mimicry. International journal of pharmaceutics, 569, 118628.

Petralia, M. C., Mazzon, E., Fagone, P., Russo, A., Longo, A., Avitabile, T., ... & Basile, M. S. (2019). Characterization of the pathophysiological role of CD47 in uveal melanoma. Molecules, 24(13), 2450.

Lian, S., Xie, X., Lu, Y., & Jia, L. (2019). Checkpoint CD47 function on tumor metastasis and immune therapy. OncoTargets and therapy, 12, 9105.

Veillette, A., & Chen, J. (2018). SIRPα–CD47 immune checkpoint blockade in anticancer therapy. Trends in immunology, 39(3), 173-184.

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

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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