Analytical Data
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Gene name
VN1R5
- Application
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Alternative Names
VN1R5; V1RL5; Vomeronasal type-1 receptor 5; G-Protein coupled receptor GPCR26; hGPCR26; V1r-like receptor 5
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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
Q7Z5H4
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Expression Region
1-357 aa
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AA Sequence
MLKLVIIENMAEIMLFSLDLLLFSTDILCFNFPSKMIKLPGFITIQIFFYPQASFGISANTILLLFHIFTFVFSHRSKSIDMIISHLSLIHILLLFTQAILVSLDFFGSQNTQDDLRYKVIVFLNKVMRGLSICTPCLLSVLQAIISPSIFSLAKLKHPSASHILGFFLFSWVLNMFIGVIFCCTLRLPPVKRGQSSVCHTALFLFAHELHPQETVFHTNDFEGCHLYRVHGPLKRLHGDYFIQTIRGYLSAFTQPACPRVSPVKRASQAILLLVSFVFTYWVDFTFSFSGGVTWINDSLLVWLQVIVANSYAAISPLMLIYADNQIFKTLQMLWFKYLSPPKLMLKFNRQCGSTKK
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Molecular Weight
40,7 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
Related Products
Protein Description
VN1R5 is a member of the vomeronasal receptor (VNR) family, which plays a crucial role in the detection of pheromones and other chemical cues in the environment, a process important for social and reproductive behaviors in many animal species. Research into VN1R5 has gained momentum due to its potential implications in understanding the mechanisms underlying olfactory signaling and behavior. This receptor is expressed in the vomeronasal organ (VNO), a chemosensory structure that primarily functions in the detection of non-volatile compounds, which are vital for mate selection, predator avoidance, and social communication. The interest in VN1R5 is further amplified by its evolutionary significance, providing insights into the adaptive changes in the sensory systems of different species. Studies have indicated a high degree of variability in VN1R5 across species, highlighting its role in species-specific behavior and environmental adaptation. Recent advances in molecular biology techniques have facilitated the characterization and functional analysis of VN1R5, enabling researchers to explore its receptor-ligand interactions, signal transduction pathways, and the broader physiological roles of vomeronasal receptors. Understanding VN1R5 and its functional dynamics could lead to innovative applications in fields such as ecology, evolutionary biology, and even biotechnology, particularly in developing pheromone-based control strategies in pest management. Consequently, VN1R5 serves as a valuable model for exploring the complexities of pheromone signaling and its associated behavioral repercussions in various ecological contexts.
