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Validated All-in-One™ qPCR Primer for CD47(NM_001777.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene encodes a membrane protein, which is involved in the increase in intracellular calcium concentration that occurs upon cell adhesion to extracellular matrix. The encoded protein is also a receptor for the C-terminal cell binding domain of thrombospondin, and it may play a role in membrane transport and signal transduction. This gene has broad tissue distribution, and is reduced in expression on Rh erythrocytes. Four alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq].
Gene References into function
- The interaction of CD47 with SHPS-1 may contribute to the recruitment of B lymphocytes via endothelial cells under steady state conditions.
- Interactions of thrombospondins with alpha4beta1 integrin and CD47 differentially modulate T cell behavior
- regulates integrin function. Differential effects on alpha vbeta 3 and alpha 4beta1 integrin-mediated adhesion.
- mechanism of antigen-induced caspase-independent cell death in normal and leukemic cells
- An autocrine loop of the integrin alpha(V)beta(3)/CD47 receptor complex and thrombospondin-1 is identified as the molecular coupling device between mechanical loading and apoptosis.
- distribution of CD47, most restrained by cytoskeleton linkages plus a smaller fraction able to diffuse in the membrane, and colocalization with Rh protein complexes
- Evidence protein 4.2 interacts with the Rh membrane complex member CD47 obtained from red cells of patients with hereditary spherocytosis associated with complete protein 4.2 deficiency
- CD47 expressed on platelets significantly contributes to platelet adhesion on tumor necrosis factor-alpha (TNF-alpha)-stimulated vascular endothelial cells
- Ligation of CD47 by any of its known ligands rapidly induces heterotrimeric Gi alpha-dependent but caspase-independent apoptosis in Jurkat T cells and, importantly, in activated primary T cells.
- the extracellular Ig domain of IAP(CD47), when bound to thrombospondin, interacts with integrin alphaIIbbeta3 and can change alphaIIbbeta3 in a high affinity state without the requirement of intracellular signaling
- Interaction of CD47 with thrombospondin-1 contributes to the perpetuation of inflammation in rheumatoid synovitis.
- protein 4.2 strongly influences CD47 levels as well as the extent of membrane skeleton attachment in erythrocytes
- IAP gene expression is regulated by alpha-Pal
- CD47 recruits alpha(v)beta(3) and its associated signaling molecules to these domains
- CD47 has a role in inducing alpha4beta1 integrin activation and adhesion in sickle reticulocytes
- Review. The interaction between CD47 and SIRPalpha seems to be important to limit destruction of host cells in autoimmune diseases like autoimmune hemolytic anemia (AIHA), where macrophages destroy antibody or complement opsonized cells.
- CD47 short interferint RNA inhibited cell proliferation in cultures of hepatoma cells.
- Apoptosis inducing single-chain antibody fragments against cd47 antigens will be effective as a novel therapy for multiple myeloma.
- SHPS-1 negatively regulates platelet function via CD47, especially alpha(IIb)beta(3)-mediated outside-in signaling
- Novel CD47-dependent intercellular adhesion modulates cell movement.
- CD47 associates with Fas upon its activation and augments Fas-mediated apoptosis.
- SIRPalpha-CD47 interactions, which reportedly define self, exhibit cell type specificity and limited cross-species reactivity
- RhD co-localizeS with CD47 but not calreticulin or glycophorin-A on human RBCs.
- highlight major species differences in CD47-SIRPalpha interactions and CD47 integration, suggesting that signaling by CD47 in man may be qualitatively different from mouse.
- CD47 stimulation by a thrombospondin-1 peptide induces naive or memory CD4+CD25- T cells to become suppressive.
- analysis of species-specific CD47 interactions with signal regulatory protein alpha
- Genetic induction of human CD47 on porcine cells could provide inhibitory signaling to SIRPalpha on human macrophages, providing a novel approach to preventing macrophage-mediated xenograft rejection.
- In this review the authors provide mechanistic insight into the signaling pathways used by thrombospondin-1 and CD47 at the cellular and molecular level to prevent nitric oxide signaling through cyclic GMP, thereby exacerbating tissue ischemia.
- Upregulation of CD47 in sporadic inclusion body myositis.
- CD47/IAP is necessary for chondrocyte mechanotransduction. Through interactions with alpha5beta1 integrin and thrombospondin, CD47/IAP may modulate chondrocyte responses to mechanical signals.
- On both RBCs and microbeads, human CD47 potently inhibits phagocytosis as does direct inhibition of myosin. CD47-SIRPalpha interaction initiates a dephosphorylation cascade directed in part at phosphotyrosine in myosin.
- CD47 may play an inhibitory role in NK cell-mediated cytotoxicity against cancer cells, implying a possible mechanism of immune escape in human cancer.
- A T cell-negative sensor that may serve to dampen unchecked proinflammatory T helper cell type 1 (Th1) responses, such as occur during contact hypersensitivity in transgenic mice.
- CD47 is enriched at endothelial junctions, and its interaction with SIRPgamma is required for human T-cell transendothelial migration
- These results explain the specificity of CD47 for the SIRP family of paired receptors in atomic detail.
- TSP-1's C-terminal domain opens to interact with the CD-47 receptor
- Expression levels of CD47, CD35, CD55, and CD59 on red blood cells and signal-regulatory protein-alpha,beta on monocytes from patients with warm autoimmune hemolytic anemia.
- Down-regulation of the IAP antagonistis XAF1, Smac/DIABLO and HtrA2, has been related to the onset and progression of various malignancies.
