Analytical Data
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Gene name
TRPA1
- Application
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Alternative Names
TRPA1；ANKTM1；Transient receptor potential cation channel subfamily A 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
O75762
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Expression Region
957-1119aa
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AA Sequence
IGLAVGDIAEVQKHASLKRIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYPNKPRSGGMLFHIFCFLFCTGEIRQEIPNADKSLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISETEDDDSHCSFQDRFKKEQMEQRNSRWNTVLRAVKAKTHHLEP
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Molecular Weight
35.2kDa
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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
Transient receptor potential ankyrin 1 (TRPA1) is a non-selective cation channel that plays a critical role in sensory perception, particularly in response to noxious stimuli including temperature, pain, and inflammatory signals. TRPA1 is predominantly expressed in primary sensory neurons and is activated by a variety of endogenous and exogenous chemicals, making it a key player in nociception and the body's response to harmful stimuli. The study of TRPA1 recombinant proteins has gained significant attention in recent years, driven by its potential implications in pain management and the development of therapeutics for conditions such as chronic pain and neuroinflammatory disorders. Research has focused on characterizing the structural and functional properties of TRPA1, which can be challenging due to its complex biophysical characteristics and post-translational modifications. By producing recombinant TRPA1 in heterologous systems, researchers aim to gain insights into its activation mechanisms, ion conduction properties, and interaction with various ligands. Understanding these aspects is crucial for elucidating TRPA1's role in pathophysiological conditions and for the rational design of novel analgesics targeting this channel. This research not only enhances our basic knowledge of ion channels but also paves the way for the development of new interventions for pain-related disorders, highlighting TRPA1 as a promising target in pharmacology and therapeutic development.
