Cat: PA2000-608DB

Recombinant Human Trp Protein,His

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Analytical Data

  • Gene name

    Trp

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Trp;TRP1;Short transient receptor potential channel 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P07477

  • Expression Region

    24-247aa

  • AA Sequence

    IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS

  • Molecular Weight

    26.9 kDa

  • 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 recombinant proteins, particularly those involving the Trp (tryptophan) biosynthetic pathway, has gained significant attention in recent years due to their importance in various biological processes and potential applications in biotechnology and medicine. Tryptophan is an essential amino acid and a precursor for several bioactive molecules, including neurotransmitters such as serotonin and melatonin, which play critical roles in mood regulation and circadian rhythms. The Trp biosynthetic pathway is intricately linked to numerous metabolic pathways, making it a focal point for understanding cellular functions and stress responses. Advances in molecular biology techniques have enabled researchers to manipulate and express Trp-related genes in various host organisms, facilitating the production of recombinant Trp proteins for in-depth functional studies. These studies aim to elucidate the biochemical mechanisms underlying Trp metabolism and its impact on health, as well as to explore the potential of recombinant Trp proteins as therapeutic agents or agricultural enhancers. By employing tools such as CRISPR-Cas9 and synthetic biology, scientists are unraveling the complexities of Trp biosynthesis and its regulation, offering insights into how to harness these pathways for innovative solutions in health and nutrition. Overall, the exploration of Trp recombinant proteins represents a promising avenue for research with implications for medical therapies, agricultural productivity, and a deeper understanding of fundamental biological processes.

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