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Study provides accurate validation of functional CGRP (show CALCA Proteins) receptor expression throughout the brainstem and the spinal cord of non-human primates: several areas in the brainstem were shown to express CLR (show DCLK3 Proteins) and RAMP1 mRNA and protein
RAMP1 exerted mucosal protection in DSS (show PMP22 Proteins)-induced colitis via attenuation of recruitment of inflammatory cells and of pro-inflammatory cytokines.
Together, these data indicate that signaling through RAMP1 and CLR (show CALCR Proteins) plays a role in mediating asthma pathology
multiple NKX3.1 (show NKX3-1 Proteins) binding sites were found in the RAMP1 locus in human prostate cancer cells and in the normal mouse prostate.
Data indicate that IL-17 (show IL17A Proteins) production is suppressed in RAMP1-deficient mice in the experimental autoimmune encephalomyelitis (EAE) model and RAMP1-deficient mice are completely resistant to EAE.
Data indicate that the lack of an intact CGRP receptor component (show CRCP Proteins) RAMP1 resulted in an increased recruitment and activation of neutrophils.
Data show that mechanical ventilation reduced the expression of receptor activity-modifying protein RAMP3 (show RAMP3 Proteins), but not of intermedin (IMD (show ADM2 Proteins)), calcitonin receptor-like receptor (CRLR (show CALCRL Proteins)), and RAMP1 and RAMP2 (show RAMP2 Proteins).
significantly diminished intestinal peristalsis was observed by the allergy induction in RAMP1-deficient mice compared with WT mice.
These findings suggest that RAMP1 may be a new therapeutic target to regulate CGRP (show CALCA Proteins)-mediated effects during disease including pathophysiological states in which Ang II (show AGT Proteins) plays a major role.
Co-expression of RAMP1 and CRLR (show CALCRL Proteins) reconstituted a CGRP (show CALCA Proteins) receptor that was able to activate the pheromone-signaling pathway with pharmacological properties similar to those observed previously in mammalian cells.
role in cell surface expression of CRLR (show CALCRL Proteins)/RAMP heterodimeric receptors
Data suggest CGRP (show S100A12 Proteins) receptor (CGRPR (show CALCRL Proteins)) ECL2 (extracellular loop 2 domain) enables interaction with N-terminal residues of CGRP (show S100A12 Proteins); this provides evidence for dual involvement of ECL2 in two-domain binding model of CGRP (show S100A12 Proteins)/CGRPR (show CALCRL Proteins) interaction; CGRPR (show CALCRL Proteins) is obligate heterodimer of CLR (show DCLK3 Proteins)/RAMP1. (CGRP (show S100A12 Proteins) = calcitonin gene-related peptide (show CALCA Proteins); CLR (show DCLK3 Proteins) = calcitonin receptor-like receptor (show CALCRL Proteins); RAMP1 = receptor [calcitonin (show CALCA Proteins)] activity modifying protein 1)
Evidence that DNA methylation (show HELLS Proteins) at RAMP1 gene promoter plays a role in migraine was described.
RAMP1 rs7590387 has a role in the transformation of episodic migraine into medication overuse headache.
Data suggest that ligand binding of a G protein-coupled receptor (GPCR (show TAS1R3 Proteins)) may inform drug development targeting calcitonin receptor-like receptor (CLR (show CALCRL Proteins)):receptor activity-modifying proteins RAMP1/2 complexes.
A novel functional role for RAMP1 in regulation of CaSR (show CASR Proteins) signalling in addition to its known role in receptor trafficking, is reported.
RAMP1 overexpression enhances the promoting effect that exogenous CGRP (show S100A12 Proteins) has on osteogenic differentiation
No significant association of the tested SNPs of the RAMP1 gene were found with migraine susceptibility.
CLR (show DCLK3 Proteins) and RAMP1 co-localize in the enteric nervous system of human stomach, ileum, and colon, and are in close proximity to their ligands CGRP (show S100A12 Proteins) and IMD (show ADM2 Proteins)
The present finding demonstrated that RAMP1 immunoreactivity was localized in many neurons and phenopalatine ganglion.
The protein encoded by this gene is a member of the RAMP family of single-transmembrane-domain proteins, called receptor (calcitonin) activity modifying proteins (RAMPs). RAMPs are type I transmembrane proteins with an extracellular N terminus and a cytoplasmic C terminus. RAMPs are required to transport calcitonin-receptor-like receptor (CRLR) to the plasma membrane. CRLR, a receptor with seven transmembrane domains, can function as either a calcitonin-gene-related peptide (CGRP) receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. In the presence of this (RAMP1) protein, CRLR functions as a CGRP receptor. The RAMP1 protein is involved in the terminal glycosylation, maturation, and presentation of the CGRP receptor to the cell surface.
receptor (calcitonin) activity modifying protein 1
, receptor activity-modifying protein 1
, receptor activity modifying protein 1
, receptor (G protein-coupled) activity modifying protein 1
, CRLR activity-modifying protein 1
, calcitonin receptor-like receptor activity modifying protein 1
, calcitonin-receptor-like receptor activity-modifying protein 1