Analytical Data
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Gene name
VN1R1
- Application
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Alternative Names
VN1R1; V1RL1; VNR19I1; Vomeronasal type-1 receptor 1; G-Protein coupled receptor GPCR24; hGPCR24; V1r-like receptor 1; V3r-related gene Protein; Vomeronasal olfactory receptor chromosome 19 subtype I member 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
Q9GZP7
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Expression Region
1-353aa
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AA Sequence
MVGDTLKLLSPLMTRYFFLLFYSTDSSDLNENQHPLDFDEMAFGKVKSGISFLIQTGVGILGNSFLLCFYNLILFTGHKLRPTDLILSQLALANSMVLFFKGIPQTMAAFGLKYLLNDTGCKFVFYYHRVGTRVSLSTICLLNGFQAIKLNPSICRWMEIKIRSPRFIDFCCLLCWAPHVLMNASVLLLVNGPLNSKNSSAKNNYGYCSYKASKRFSSLHAVLYFSPDFMSLGFMVWASGSMVFFLYRHKQQVQHNHSNRLSCRPSQEARATHTIMVLVSSFFVFYSVHSFLTIWTTVVANPGQWIVTNSVLVASCFPARSPFVLIMSDTHISQFCFACRTRKTLFPNLVVMP
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Molecular Weight
40 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
VN1R1, a member of the vomeronasal receptor gene family, plays a critical role in the detection of pheromones and other chemical signals in mammals. This receptor is predominantly expressed in the vomeronasal organ (VNO), an accessory olfactory structure that contributes to the modulation of social and reproductive behaviors. Research into VN1R1 has gained momentum due to its potential implications in understanding the molecular basis of chemosensation and its evolutionary significance among vertebrates. VN1R1's unique structure, characterized by a seven-transmembrane domain, presents an intriguing target for investigations aimed at uncovering the mechanisms of ligand binding and signal transduction. Furthermore, the study of VN1R1 not only enhances our understanding of the chemosensory systems but also provides insights into the biological interactions that underpin complex behaviors. Recent advances in recombinant protein technology have facilitated the production and characterization of VN1R1 in vitro, paving the way for functional assays that explore its interaction with various ligands. This research is crucial for elucidating the receptor’s specific roles in behavior modulation and may have broader implications for studying olfactory pathways and their associated neural circuitry. As such, VN1R1 represents a significant focus in sensory biology, with potential applications in fields ranging from behavioral ecology to the development of biomimetic sensors.
