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Recombinant Human VIPR2 Fc Chimera Protein, CF

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2 μg/lane of Recombinant Human VIPR2 Fc Chimera Protein (Catalog # 11003-VR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human VIPR2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Growth Hormone-Releasing Factor is immobilized at 2.00 μg/mL, 100 μL/well, Recombinant Human VIPR2 Fc Chimera binds with an ED50 of 7.00-42.0 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human VIPR2 protein
Recombinant Human VIPR2
(Arg26-Val126)
Accession # P41587.2
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Arg26
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
38 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
45-60 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human VIPR2 Fc Chimera Protein, CF

  • FLJ16511
  • Helodermin-preferring VIP receptor
  • PACAP type III receptor
  • PACAPR3
  • PACAP-R3
  • PACAP-R-3
  • Pituitary adenylate cyclase-activating polypeptide type III receptor
  • vasoactive intestinal peptide receptor 2
  • vasoactive intestinal polypeptide receptor 2
  • VIP R2
  • VIP2R
  • VIPR2
  • VIP-R-2
  • VPAC2
  • VPCAP2R

Background

Vasoactive intestinal polypeptide receptor 2 (VIPR2 or VPAC2) is a transmembrane receptor that belongs to the B class G protein coupled receptor family of proteins (1). Mature, human VIPR2 consists of an extracellular domain (ECD) with a hormone receptor region followed by seven transmembrane regions and a short cytoplasmic domain. The ECD of human VIPR2 shares 90% amino acid sequence identity with both mouse and rat VIPR2. Human VIPR2 is expressed predominantly in skeletal muscle, and to a lesser extent in the brain, heart, pancreas, and placenta (1). VIPR2 is coupled to a cAMP mediated signal transduction pathway and binds two homologous neuropeptides, vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (PACAP), with high affinity (1). VIP plays several roles during neural development, including stimulating neurogenesis, promoting survival of neurons, and assisting in neuron repair (1, 2). Additionally, VIP signaling via VIPR2 has been implicated in regulating immune responses (3). VIPR2 gene duplication and altered signaling of VIP has been associated with the pathogenesis of schizophrenia and may also play a role in autism (4-6). VIPR2 activation has been linked to disruption of cortical neuronal maturation in mice (7). Studies suggest that VIPR2 could be a potential target in the development of novel antipsychotic drugs (5).
  1. Lutz, E. M. et al. (1999) FEBS Letters. 458:197.
  2. Hill, J. et al. (2007) Curr. Pharm. Des. 13:1079.
  3. Abad, C. and Var Tan, Y. (2016) J Clin Exp Neuroimmunol 1:104.
  4. Vacic, V. et al. (2011) Nature. 471:499.
  5. Levinson, D. et al. (2011) Ameri. J. Psych. 168:302.
  6. Firouzabadi, S. G. et al. (2017) Molec. Neuobio. 54:7019.
  7. Takeuchi, S. et al. (2020) Front. Neurosci. 14:521.

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