Human VIPR2 Protein 2279

$315.00 – $1,050.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Glu24-Val126

SKU: 2279parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P41587
express system	HEK293
product tag	C-mFc
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Effects of vasoactive intestinal peptide (VIP) on T cell migration are mediated by structurally distinct types I (VIPR1) and II (VIPR2) G protein-associated receptors. The two receptor types were proposed to transduce opposite effects on human T cells, since cytokine-induced chemotaxis of VIPR1-bearing HuT 78 human T cells, in contrast to T cells that express VIPR2, was inhibited by VIP.
molecular weight	The protein has a predicted MW of 37.35 kDa. Due to glycosylation, the protein migrates to 45-60 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human VIPR2 Protein 2279

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Effects of vasoactive intestinal peptide (VIP) on T cell migration are mediated by structurally distinct types I (VIPR1) and II (VIPR2) G protein-associated receptors. The two receptor types were proposed to transduce opposite effects on human T cells, since cytokine-induced chemotaxis of VIPR1-bearing HuT 78 human T cells, in contrast to T cells that express VIPR2, was inhibited by VIP.
Protein names Vasoactive intestinal polypeptide receptor 2 (VIP-R-2) (Helodermin-preferring VIP receptor) (Pituitary adenylate cyclase-activating polypeptide type III receptor) (PACAP type III receptor) (PACAP-R-3) (PACAP-R3) (VPAC2 receptor) (VPAC2R)
Gene names VIPR2,VIPR2 VIP2R
Protein family G-protein coupled receptor 2 family
Mass 49479Da
Function FUNCTION: G protein-coupled receptor activated by the neuropeptides vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (ADCYAP1/PACAP) (PubMed:7811244, PubMed:35477937, PubMed:8933357). Binds VIP and both PACAP27 and PACAP38 bioactive peptides with the following order of potency PACAP38 = VIP > PACAP27 (PubMed:35477937, PubMed:8933357). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors. Activates cAMP-dependent pathway (PubMed:7811244, PubMed:35477937, PubMed:8933357). May be coupled to phospholipase C. {ECO:0000269\|PubMed:35477937, ECO:0000269\|PubMed:7811244, ECO:0000269\|PubMed:8933357}.
Subellular location SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000269\|PubMed:35477937}.
Tissues TISSUE SPECIFICITY: Expressed in CD4+ T-cells, but not in CD8+ T-cells. Expressed in the T-cell lines Jurkat, Peer, MOLT-4, HSB, YT and SUP-T1, but not in the T-cell lines HARRIS and HuT 78. {ECO:0000269\|PubMed:8926282}.
Structure SUBUNIT: Interacts with ADCYAP1/PACAP (via N-terminal extracellular domain); activated by PACAP27 and CAPAC38 neuropeptides (Probable) (PubMed:35477937). Interacts with VIP; the interaction results in VIPR1 activation (Probable). {ECO:0000269\|PubMed:35477937, ECO:0000305\|PubMed:8933357}.
Target Relevance information above includes information from UniProt accession: P41587
The UniProt Consortium

Data

The purity of Human VIPR2 is greater than 95% as determined by SEC-HPLC.

Human VIPR2 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.