Analytical Data
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Gene name
5a
- Application
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Alternative Names
HTR5A；5-hydroxytryptamine receptor 5A
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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
P47898
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Expression Region
1-357aa
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AA Sequence
MDLPVNLTSFSLSTPSPLETNHSLGKDDLRPSSPLLSVFGVLILTLLGFLVAATFAWNLLVLATILRVRTFHRVPHNLVASMAVSDVLVAALVMPLSLVHELSGRRWQLGRRLCQLWIACDVLCCTASIWNVTAIALDRYWSITRHMEYTLRTRKCVSNVMIALTWALSAVISLAPLLFGWGETYSEGSEECQVSREPSYAVFSTVGAFYLPLCVVLFVYWKIYKAAKFRVGSRKTNSVSPISEAVEVKDSAKQPQMVFTVRHATVTFQPEGDTWREQKEQRAALMVGILIGVFVLCWIPFFLTELISPLCSCDIPAIWKSIFLWLGYSNSFFNPLIYTAFNKNYNSAFKNFFSRQH
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Molecular Weight
40.2 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
The study of 5a recombinant proteins has gained significant attention due to their potential applications in various fields, including medicine, biotechnology, and agriculture. 5a proteins, typically derived from viral sources such as the Foot-and-Mouth Disease Virus (FMDV), play crucial roles in viral replication and pathogenesis. Understanding the structure and function of these proteins is essential for the development of effective vaccines and therapeutics. Recent advances in molecular biology techniques, particularly in gene cloning and expression systems, have enabled researchers to produce these proteins in a more efficient and scalable manner. This has led to enhanced research capabilities for studying their interactions with host cell mechanisms and immune responses. Moreover, the ability to engineer and modify 5a proteins opens up new avenues for designing novel biotechnological tools, such as biosensors and targeted drug delivery systems. The exploration of 5a recombinant proteins not only contributes to fundamental virology research but also holds promise in addressing global health challenges and improving agricultural resilience against viral diseases.
