Cat: PA1000-8146

Recombinant Human ChAT Protein,His

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Analytical Data

  • Gene name

    ChAT

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ChAT;Choline O-acetyltransferase

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P28329

  • Expression Region

    120-733aa

  • AA Sequence

    AAKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQQKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSEWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHVTQSSRKLIRADSVSELPAPRRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQLAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLLKDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRDLCSLLPPTESKPL

  • Molecular Weight

    76.1 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

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Protein Description

ChAT, or choline acetyltransferase, is a crucial enzyme involved in the biosynthesis of acetylcholine, a key neurotransmitter that plays a vital role in various physiological processes, including muscle activation and cognitive function. Research into ChAT has gained significant attention due to its implications in neurodegenerative diseases, particularly in conditions such as Alzheimer's disease, where reduced levels of acetylcholine are observed. Understanding the structure and function of ChAT can lead to better insights into the mechanisms underlying these diseases and potentially aid in the development of targeted therapies. Recombinant ChAT proteins are essential for this research as they enable detailed studies of the enzyme's biochemical properties, interactions, and potential as a therapeutic target. By utilizing advanced protein engineering techniques, scientists can produce ChAT with specific modifications, offering a platform for discovering new drugs that could enhance cholinergic signaling in the brain. Furthermore, investigating ChAT through recombinant approaches can help elucidate its role in synaptic transmission and plasticity, thereby advancing our understanding of neurological disorders associated with acetylcholine dysfunction. Overall, the study of recombinant ChAT proteins is a promising avenue for unraveling the complexities of cholinergic signaling and its implications in health and disease.

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