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Validated All-in-One™ qPCR Primer for CD209(NM_021155.3) Search again
Product ID:
HQP008808
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CDSIGN, CLEC4L, DC-SIGN, DC-SIGN1, hDC-SIGN
Gene Description:
CD209 molecule
Target Gene Accession:
NM_021155.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
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:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a transmembrane receptor and is often referred to as DC-SIGN because of its expression on the surface of dendritic cells and macrophages. The encoded protein is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses with a large impact on public health. The protein is organized into three distinct domains: an N-terminal transmembrane domain, a tandem-repeat neck domain and C-type lectin carbohydrate recognition domain. The extracellular region consisting of the C-type lectin and neck domains has a dual function as a pathogen recognition receptor and a cell adhesion receptor by binding carbohydrate ligands on the surface of microbes and endogenous cells. The neck region is important for homo-oligomerization which allows the receptor to bind multivalent ligands with high avidity.
Gene References into function
- Crystal structures of carbohydrate-recognition domains of DC-SIGN bound to oligosaccharide, in combination with binding studies, reveal that it selectively recognizes endogenous high-mannose oligosaccharides
- identification of binding sites for intercellular adhesion molecule 3 and HIV-1
- DC-SIGN internalizes antigen for presentation to T cells
- DC-SIGN is specifically expressed on IL-4-treated monocytes and is subjected to a tight regulation by numerous cytokines and growth factors.
- interactions with ICAM-3 does not promote DC-SIGN mediated HIV-1 transmission
- carbohydrate/protein recognition profile and other features of DC-SIGN that contribute to the potency of DC to control immunity
- mediates cellular entry by Ebola virus in cis and in trans
- role of CD209 as Leishmania amastigote receptor in human cells
- Review. This article reviews the interaction of DC-SIGN & DC-SIGNR with HIV and Ebola & discusses the mechanism of DC-SIGN-mediated viral transmission.
- Addition of a single gp120 glycan confers increased binding to dendritic cell-specific ICAM-3-grabbing nonintegrin and neutralization escape to human immunodeficiency virus type 1
- DC-SIGN (DC-specific ICAM-3-grabbing nonintegrin) was only expressed by CD14(+)CDla(lo) dermal DCs
- cytomegalovirus envelope glycoprotein B is a viral ligand for DC-SIGN. It extend DC-SIGN implication in virus propagation
- This cell surface receptor discriminates between Mycobacterium species through selective recognition of the mannose caps on lipoarabinomannan
- Mycobacteria target DC-SIGN to suppress dendritic cell function
- DC-SIGN is the major Mycobacterium tuberculosis receptor on human dendritic cells.
- Expression of DC-SIGN and its ligand, ICAM-3, is found in substantial amounts only in RA synovium, suggesting that their interaction is implicated in the additional activation of synovial macrophages that leads to the production of EMMPRIN and MMP-1.
- Increased expression of DC-SIGN+IL-12+IL-18+ and CD83+IL-12-IL-18- dendritic cell populations in the colonic mucosa of patients with Crohn's disease
- Appears in the decidua of early pregnancy.
- DC-SIGN may function in pathogen recognition by interaction with the carbohydrate antigens Lex and possibly LDNF, found on important human pathogens, such as schistosomes and the bacterium Helicobacter pylori
- DC-SIGN is an exquisite pathogen-uptake receptor that captures not only viruses but also fungi.
- DC-SIGN facilitates capture and accumulation of HIV-1 viral particles in a vesicular compartment and inhibits viral fusion. Competition between CD4 and DC-SIGN for Env binding likely affects virus access to the cytosol and syncytium formation.
- differential use of DC-SIGN by viral envelope glycoproteins may account for the immunopathogenesis of dengue virus
- DC-SIGN regulation in monocyte-derived macrophages does not singly predict the transmission potential of HIV in this cell type.
- DC-SIGN, can function both as an adhesion receptor and as a phagocytic pathogen-recognition receptor [Review]
- DC-SIGN expression in B-cell lines dramatically enhances viral internalization.
- DC-SIGN is a receptor for promastigote and amastigote infective stages from both visceral (Leishmania infantum) and New World cutaneous (Leishmania pifanoi) Leishmania species, but not for Leishmania major metacyclic promastigotes.
- Organization of DC-SIGN in microdomains on the plasma membrane is important for binding and internalization of virus particles, suggesting that these multimolecular assemblies of DC-SIGN act as a docking site for pathogens like HIV-1 to invade the host
- human DC-SIGN also captures feline immunodeficiency virus via high-affinity (1 nM), Ca(2+)-dependent, D-mannose-inhibited binding to the major envelope glycoprotein, gp95
- soluble DC-SIGN bound to gp120-Fc more than 100- and 50-fold better than ICAM-2-Fc and ICAM-3-Fc, respectively. Binding sites are described.
- the influx or proliferation of DC-SIGN+ immature and mature DCs and L-SIGN+ cells is dynamically regulated
- data demonstrate for the first time that lectins DC-SIGN and L-SIGN differ in their carbohydrate binding profiles
- immature DCs owe part of their outstanding Ag-independent T cell stimulatory ability to chemokines and ICAM-1, but not DC-specific ICAM-3-grabbing nonintegrin.
- variations in the DC-SIGN repeat region may have a protective effect on transmission of HIV-1
- expressed on dendritic cells; results demonstrate that hepatitis C pseudoviruses captured by L-SIGN+ or DC-SIGN+ cells efficiently transinfect adjacent human liver cells
- DC-SIGN tetramers are essential for high affinity interactions with pathogens like HIV
- RNA interference of DC-SIGN expression inhibited the attachment of HIV-1 envelope gp120 in dendritic cells (DCs) negative for DC-SIGN and the transfer of HIV-1 from DCs to T cells.
- DC-SIGN specifically interacts with clinical isolates of Aspergillus fumigatus and is involved in the initial stages of pulmonary infection as well as in fungal spreading during invasive aspergillosis.
- extended neck regions stabilize tetramers
- polymorphism in promoter associated with increased risk for parenteral acquisition of Hiv-1 infection
- a role for enhanced avidity during DC-SIGN-mediated intercellular adhesion
- We report that transfer of HIV-1 to target cells is markedly reduced when DC-SIGN(+) cells are preincubated with Leishmania amastigotes before pulsing with virions.
- These data suggest that DC-SIGN cannot be considered as the unique DC receptor for BCG internalization, and it is more interesting that the mycobacteria-induced immunosuppression cannot be attributed to the engagement of a single receptor.
- propose that DC-SIGN concentrates mosquito-derived DV particles at the cell surface to allow efficient interaction with an as yet unidentified entry factor that is ultimately responsible for DV internalization and pH-dependent fusion into dendritic cells
- Expression of DC-SIGN and CD1b in human leprosy.
- DC-SIGN is coordinately expressed uon classical and alternative macrophage activation and during dendritic cell maturation.
- A change in the number of DC-SIGN repeats may influence its normal functions as well as its binding capacity to viral and nonviral pathogens.
- results reveal that the molecular basis of M. tuberculosis binding to DC-SIGN is more complicated than previously thought and provides further insight into the mechanisms of M. tuberculosis recognition by the immune system
- Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins during infection in humans and inhibits ENV interaction with DC-SIGN
- DC-SIGN mediates adhesion of DCs to authentic glycolipids derived from Schistosoma mansoni cercariae and their excretory/secretory products.
- DC-SIGN has the potential to contribute to macrophage function in normal human lymph node; dendritic cells do not require DC-SIGN to transmit HIV or to initiate T cell responses.
- Binding of DC-SIGN to both CEACAM1 and Mac-1 is required to establish cellular interactions with neutrophils.
- The promoter variant DC-SIGN1-336 confers protection against the severity of dengue by affecting transcription factor Sp1 binding.
- significant association found for the CD209 promoter variants together with their phylogenetic status and frequency distribution strongly suggests that the -871G and -336A alleles may reduce the risk of developing TB
- Recognizes pathogens and contributes to innate immunity.
- platelets and megakaryocytes can internalize lentiviruses in a pathway, which either provide a shelter to lentiviral particles or alternatively disrupts viral integrity. The receptor DC-SIGN is involved in this function.
- DC-SIGN serves as a portal for immune dysfunction and oncogenesis caused by human herpesvirus 8 (HHV-8) infection.
- One carbohydrate recognition domain monomer was found to bind to two glycosylation sites at Asn67 of two neighboring glycoproteins in each icosahedral asymmetric unit, leaving the third Asn67 residue vacant, in complex with dengue virus.
- Cooperates with HIV entry receptors to facilitate cis-infection of immature dendritic cells and subsequent viral transfer to T cells.
- Facilitating role of DC-SIGN in syncytium formation by human T-cell leukemia virus type 1 (HTLV-1) is mediated by its interaction with ICAM-2 and ICAM-3.
- DC-SIGN recognizes M. leprae.
- Real-time RT-PCR confirmed up-regulation of IL-8, osteopontin, and TNFRSF14 and down-regulation of SAMeS and CD209 in AH.
- The dendritic morphology is shown to contribute directly to an enhanced ability to capture dendritic cell specific ICAM-3 grabbing nonintegrin (DC-SIGN)-coated beads.
- Transmission of HIV-1 from B cells to T cells through this DC-SIGN pathway could be important in the pathogenesis of HIV-1 infection.
- The -336G CD209 allele seems to be involved in celiac disease susceptibility in HLA-DQ2 (-) patients.
- DC-SIGN and DC-SIGNR genotypes and alleles distribution in Chinese Han population are significantly different from Caucasian population and with Chinese own population genetic characteristics, compared with Caucasians.
- platelets capture and transfer infectious HIV-1 via DC-SIGN and CLEC-2, thereby possibly facilitating HIV-1 dissemination in infected patients
- CD209L recognizes glycosylated flaviviruses with broad specificity, whereas CD209 is selective for flaviviruses bearing mannose-rich glycans
- binds to BSSL (bile salt stimulated lipase) from human milk and inhibits HIV-1 transfer to CD4+ T cells.
- used recombinant baculoviruses expressing different lengths of SARS-CoV spike (S) protein in a capture assay to deduce the minimal DC-SIGN binding region
- 336G/A single nucleotide polymorphisms in the promoter region and insertion/deletion polymorphisms in the "neck" region of CD209, are not relevant risk factors for developing tuberculosis in Northwestern Colombian individuals.
- DC-SIGN is selective in its recognition of specific types of fucosylated glycans and subsets of oligomannose- and complex-type N-glycans.
- The potential of carbohydrate binding proteins to impair DC-SIGN-expressing cells in their capacity of transmitting HIV to T lymphocytes might be taken into consideration in the eventual choice of anti-HIV agentts.
- The results suggest that ICAM-3 assists in the interaction of granulocytes with DC-SIGN of dendritic cells.
- demonstrated the role of DC-SIGN in complement opsonized virus uptake and infection
- different pathogens (ie. Mycobacterium tuberculosis, M. leprae, Candida albicans, measles virus, and HIV-1) interacted with DC-SIGN to activate the Raf-1-acetylation-dependent signaling pathway to modulate signaling by different TLRs
- HIV sequestration by and stimulation of DC-SIGN helps HIV evade immune responses and spread to cells
- results suggest that RANTES -28G was associated with delayed AIDS progression, while DC-SIGN -139C was associated with accelerated AIDS progression in HIV-1-infected Japanese hemophiliacs.
- findings support previous data showing that VDR SNPs modulate the risk for pulmonary tuberculosis in West Africans and suggest that variation within DC-SIGN and PTX3 also affect the disease outcome
- We show that DC-SIGN recognizes glycans involved in SIV sensitivity to neutralizing antibodies and that binding to DC-SIGN confers neutralization resistance to an otherwise sensitive SIV variant.
- DC-SIGN- and L-SIGN-mediated severe acute respiratory syndrome coronavirus entry requires specific asparagine-linked glycosylation sites
- DC-SIGN genotype and allele distribution was fairly similar in HIV-1-exposed seronegative, HIV-1 seropositive, and HIV-1 seronegative control. There was no statistical significance in the differences in the distribution of DC-SIGN genotypes
- Human seminal plasma inhibits the recognition of HIV-1 gp120 by DC-SIGN-positive DCs.
- DC-SIGN is not an Ebola virus receptor but, rather, is an attachment-promoting factor that boosts entry into B cell lines.
- DC-SIGN effectively block HIV budding from infected cells.
- A functional variant in the CD209 gene, rs4804803, does not seem to be influencing Crohn's disease susceptibility. However, it could be involved in the etiology or pathology of ulcerative colitis in HLA-DR3-positive individuals
- presence of allelic variants or a high level of expression of neck domain splicing isoforms might influence the presence and stability of DC-SIGN multimers on the cell surface
- DC-sign+ CD163+ macrophages expressing hyaluronan receptor LYVE-1 are located within chorion villi of the placenta.
- data showed that neither promoter variants nor length variation in the neck region of DC-SIGN is associated with susceptibility to tuberculosis in Tunisian patients
- The binding partner of DC-SIGN on endothelial cells is the glycan epitope Lewis(Y) (Le(Y)), expressed on ICAM-2.
- CD209 -336G variant allele is associated with significant protection against tuberculosis in individuals from sub-Saharan Africa and, furthermore, cases with -336GG were significantly less likely to develop tuberculosis-induced lung cavitation
- The polymorphism in DC-SIGN neck repeats region was rare and not associated with HIV-1 susceptibility among North Indians.
- DC-SIGN clusters move from the leading edge--where the dendritic cell is likely to encounter pathogens in tissue--to a medial lamellar site where clusters enter the cell via endocytosis
- This study shows that human DC-SIGN is a receptor for Y. pestis that promotes phagocytosis by DCs in vitro.
- DC-SIGN is involved in the interaction of dendritic cells with SW1116 colorectal carcinoma cells through the recognition of aberrantly glycosylated forms of Lewis a/Lewis b glycans.
- These glycodendrons inhibit the binding of gp120 to 2G12 and recombinant dimeric DC-SIGN with IC(50) in the nanomolar range.
- Variations of dendritic cell-specific intercellualar adhesion molecule-3-grabing nonintegrin neck region in HIV infected individuals.
- the expression of DC-SIGN is essential for productive HHV-8 infection of and replication in B cells.
- Dermal dendritic cells comprise two distinct populations: CD1+ dendritic cells and CD209+ macrophages.
- The expressions of CD105, DC-SIGN and MMR were the strongest in decidua basalis of mid pregnancy and indicate the importance of decidual macrophages in tissue homeostasis at the uteroplacental interface.
- differentiation of monocytes into CD209(+) macrophages and CD1b(+) dendritic cells distinctly mediate the innate immune response to Propionibacterium acnes
- when B-ALL cells enter the blood circulation and are able to interact with DC-SIGN and L-SIGN the immune response is shifted toward tolerance.
- DC-SIGN enhances cell infection by glycosylated West Nile virus.
- Genetic variations in DC-specific intercellular adhesion molecule-3-grabbing nonintegrin is associated with HIV-1 infection
- human DC-SIGN may have evolved as a pathogen receptor promoting protection by limiting tuberculosis-induced pathology.
- The carrier frequency of a DC-SIGN allele with <5 repeat units in the neck-region was 0.9% in HIV-1-positive and 3.8% in HIV-1-negative individuals (P=.007), an observation suggesting that this DC-SIGN variation plays a role in HIV-1 transmission.
- Mutation in the DC-SIGN cytoplasmic triacidic cluster motif markedly attenuates receptor activity for phagocytosis and endocytosis of mannose-containing ligands by human myeloid cells.
- DC-SIGN, DC-SIGNR and SDF-1 polymorphism was detected in high risk seronegative and HIV-1 patients in Northern Asian Indians.
- HSV-1 and HSV-2 interact with DC-SIGN via glycoproteins gB and gC. DC-Sign is an attachemnt receptor for HSV-1 that contributes to infectivity and transmission of HSV.
- It was found that Ca(2+) binding sites in the CRD of DC-SIGN were involved in phagocytosis of bacteria as well as multimerization of DC-SIGN, and the neck region played a role in efficiency of binding to microbes as well as multimerization of the protein
- human monocyte dendritic cells CD209 binds preferentially to Penicillium marneffei yeast;suggested role as receptor for systemic infection