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Validated All-in-One™ qPCR Primer for MRC1(NM_002438.3) Search again
Powered by BiozBy 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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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
The recognition of complex carbohydrate structures on glycoproteins is an important part of several biological processes, including cell-cell recognition, serum glycoprotein turnover, and neutralization of pathogens. The protein encoded by this gene is a type I membrane receptor that mediates the endocytosis of glycoproteins by macrophages. The protein has been shown to bind high-mannose structures on the surface of potentially pathogenic viruses, bacteria, and fungi so that they can be neutralized by phagocytic engulfment. This gene is in close proximity to MRC1L1.
Gene References into function
- reduced expression in Mycobacterium tuberculosis-infected human macrophages exhibiting enhanced cellular adhesion
- Engagement of the endocytic C-type 1 mannose receptor elicits a secretory program in dendritic cells characterized by a repertoire of anti-inflammatory cytokines and chemokines and the ability to inhibit the generation of Th1-polarized immune responses.
- alveolar macrophage mannose receptor mediates Pneumocystis mediated NF-kB nuclear translocation and may represent an important mechanism of the host cell response to Pneumocystis infection
- Endocytosis of glycosylated protein by the mannose receptor does not enhance presentation of antigen. The postulated role of the mannose receptor in presentation of glycoprotein-derived antigen is reevaluated in light of these results.
- MR is a binding receptor, which requires a partner to trigger phagocytosis in some specialized cells such as macrophages.
- The mannose receptors on human AM may suppress select proinflammatory cytokine release and may serve to regulate the innate inflammatory responses to infectious challenge in the lungs.
- Engagement of the Mannose Receptor by mannose-capped lipoarabinomannan during the phagocytic process directs Mycobacterium tuberculosis to its initial phagosomal niche, thereby enhancing survival in human macrophages.
- Pc-mediated IL-8 release by human AM requires the coexpression of MR and TLR2 and further supports the concept that combinatorial interactions of macrophage innate receptors provide specificity of host defense cell responses to infectious challenge.
- Mannose receptor (MR) may serve as a binding and an entry site, but the MR-mediated pathway does not lead to productive HIV-1 infection.
- demonstrate that entry of FVIII into human dendritic cells (DC) leading to T cell activation, is mediated by mannose-terminating glycans on FVIII
- RAGE could also behave as a receptor for Mycobacterium tuberculosis
- 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.