Analytical Data
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Gene name
VIPR1
- Application
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Alternative Names
VIPR1；Vasoactive intestinal polypeptide receptor 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P32241
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Expression Region
1-457aa
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AA Sequence
MRPPSPLPARWLCVLAGALAWALGPAGGQAARLQEECDYVQMIEVQHKQCLEEAQLENETIGCSKMWDNLTCWPATPRGQVVVLACPLIFKLFSSIQGRNVSRSCTDEGWTHLEPGPYPIACGLDDKAASLDEQQTMFYGSVKTGYTIGYGLSLATLLVATAILSLFRKLHCTRNYIHMHLFISFILRAAAVFIKDLALFDSGESDQCSEGSVGCKAAMVFFQYCVMANFFWLLVEGLYLYTLLAVSFFSERKYFWGYILIGWGVPSTFTMVWTIARIHFEDYGCWDTINSSLWWIIKGPILTSILVNFILFICIIRILLQKLRPPDIRKSDSSPYSRLARSTLLLIPLFGVHYIMFAFFPDNFKPEVKMVFELVVGSFQGFVVAILYCFLNGEVQAELRRKWRRWHLQGVLGWNPKYRHPSGGSNGATCSTQVSMLTRVSPGARRSSSFQAEVSLV
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Molecular Weight
51.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
VIPR1 (Vasoactive Intestinal Peptide Receptor 1) is a G protein-coupled receptor that plays a crucial role in the regulation of various physiological processes, including neurotransmission, neuroprotection, and modulation of immune responses. Its ligand, vasoactive intestinal peptide (VIP), is involved in numerous biological functions such as vasodilation, intestinal motility, and anti-inflammatory responses. The study of VIPR1 as a recombinant protein has garnered significant interest due to its potential therapeutic implications in a variety of conditions, including asthma, inflammatory bowel disease, and neurological disorders. Research in this area aims to elucidate the binding mechanism of VIP to VIPR1, understand the receptor's structural dynamics, and explore its signaling pathways. The recombinant expression of VIPR1 allows for the in-depth investigation of its functional properties in vitro and in vivo, thereby providing insights into its role in disease mechanisms and potential as a drug target. Additionally, the development of VIPR1-based therapeutic strategies, such as small molecules or peptides that can modulate its activity, may offer new avenues for treatment. Understanding the functional roles and regulatory mechanisms of VIPR1 not only contributes to the field of molecular pharmacology but also paves the way for novel interventions in gastrointestinal, respiratory, and neurodegenerative diseases.
