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Validated All-in-One™ qPCR Primer for RXFP1(NM_021634.3) Search again
Product ID:
HQP016173
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
LGR7, RXFPR1
Gene Description:
relaxin family peptide receptor 1
Target Gene Accession:
NM_021634.3(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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Gene References into function
- capable of mediating the action of relaxin through an adenosine 3',5'-monophosphate (cAMP)-dependent pathway
- Gene expression pattern and protein localization of LGR7 receptor in human endometrium throughout the menstrual cycle.
- Binding to and gene expression of the LGR7 relaxin receptor changes markedly with the phases of the menstrual cycle, suggesting a specific role for the hormone in the physiology of the human uterus.
- Substitution of the relaxin-3 A-chain with the A-chain from insulin-like peptide 5 results in a chimeric peptide that selectively activates GPCR135 and GPCR142 over LGR7.
- mouse and rat LGR7 share 85.2 and 85.7% identity with human LGR7
- Data describe the conformation of the relaxin-binding site of the leucine-rich G-protein-coupled receptor 7.
- Relaxin receptor (LGR7) increases the transcription of IGFBP-1 and prolactin in decidual and endometrial stromal cells through the promoter region containing multiple CCAAT/enhancer-binding proteins (C/EBP) binding sites.
- human LGR7 LDL-A module NMR studies; demonstration that calicum is required for the module to form a stable and correctly folded structure
- increase in LGR7 expression and H2 relaxin binding in the secretory phase of the menstrual cycle suggests a specific role for relaxin after ovulation in the human uterus
- Amino acid sequence analysis of the LGR7 C-terminal tail and intracellular loops revealed multiple putative phosphorylation sites, suggesting that signal switching from Gs to Gi may occur after receptor phosphorylation
- LGR7.10 splice variant is expressed at the cell surface, LGR7.2 is predominantly retained within cells and LGR7.1 is partially secreted. None stimulates cAMP production.
- Relaxin stimulates leukocyte adhesion and migration through a relaxin receptor LGR7-dependent mechanism
- The essential role of the LDLa module in LGR7 and LGR8 function is reported.
- Specific residues in the N-terminal region of the RXFP1 receptor low density lipoprotein receptor class A (LDLa) module play a key role in receptor activation.
- The LDL-A module of LGR7 influences receptor maturation, cell surface expression, and relaxin-activated signal transduction.
- The dominant-negative effects of the LGR7 splice variants expressed in the chorion and decidua could be functionally significant in the peripartal period.
- analysis of truncated human relaxin-2 and -3 (H2 and H3) relaxin peptides and their binding and cAMP activities on RXFP1, RXFP2, and RXFP3
- N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling
- RXFP1 is a constitutive dimer with negative cooperativity in ligand binding, and dimerization occurs through the 7TM domain, and that the ectodomain has a stabilizing effect on this interaction.