Cat: IPD-X25150

Recombinant Human TrpA Protein,His

  • Price
  • Size
  • Number

    Order now. For delivery time, please consult customer service

  • Pre-sale guidance and worry-free after-sale service
  • Quality assurance for cold chain transportation

Analytical Data

  • Gene name

    TrpA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ANKTM1; Ankyrin-like with transmembrane domains protein 1; Transformation-sensitive protein p120

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O75762

  • Expression Region

    Asp63~Ile370

  • Molecular Weight

    38kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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 TrpA recombinant proteins has gained significant attention due to their crucial role in various biological processes and their potential applications in biotechnology and medicine. TrpA, or transient receptor potential cation channel subfamily A, refers to a group of proteins that serve as ion channels, playing essential roles in sensation, thermoregulation, and cellular signaling. These proteins are involved in the detection of environmental stimuli such as temperature and chemical irritants. Research has shown that TrpA channels are implicated in various physiological and pathological conditions, including pain perception, inflammation, and neurodegenerative diseases. Consequently, understanding the structure, function, and regulatory mechanisms of TrpA proteins through recombinant expression systems is vital for elucidating their roles in human health and disease. By producing TrpA proteins in a recombinant form, researchers can study their functional characteristics in vitro, develop specific inhibitors, or design therapeutic agents targeting these channels. Moreover, recombinant TrpA proteins can serve as valuable tools in drug discovery and development, enabling high-throughput screening of compounds that modulate their activity. Overall, the investigation of TrpA recombinant proteins not only enhances our understanding of fundamental biological mechanisms but also paves the way for innovations in therapeutic interventions for conditions associated with TrpA dysregulation.

E-mail

sales@ipodix.com

Sales

+1 2092920560


Contact us via WhatsApp

IPODIX Biotech Inc

2108 N ST, STE N
Sacramento, CA 95816, USA

For Product Information and Orders

sales@ipodix.com

For Business Collaboration

sales@ipodix.com

For CRO Services

sales@ipodix.com

For Technical Support

sales@ipodix.com
  • 50000+

    Recombinant Proteins

  • 100+

    Researchers

  • 100+

    Countries Served

  • ISO

    Certified Quality

Committed to Quality
Driven by Innovation

Learn More About US