Cat: PA2000-1564

Recombinant Human CD3eAP Protein,His

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Analytical Data

  • Gene name

    CD3eAP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CD3eAP;ASE1;CAST;CD3EAP;DNA-directed RNA polymerase I subunit RPA34

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O15446

  • Expression Region

    1-510aa

  • AA Sequence

    MEEPQAGDAA RFSCPPNFTA KPPASESPRF SLEALTGPDT ELWLIQAPAD FAPECFNGRH VPLSGSQIVK GKLAGKRHRY RVLSSCPQAG EATLLAPSTE AGGGLTCASA PQGTLRILEG PQQSLSGSPL QPIPASPPPQ IPPGLRPRFC AFGGNPPVTG PRSALAPNLL TSGKKKKEMQ VTEAPVTQEA VNGHGALEVD MALGSPEMDV RKKKKKKNQQ LKEPEAAGPV GTEPTVETLE PLGVLFPSTT KKRKKPKGKE TFEPEDKTVK QEQINTEPLE DTVLSPTKKR KRQKGTEGME PEEGVTVESQ PQVKVEPLEE AIPLPPTKKR KKEKGQMAMM EPGTEAMEPV EPEMKPLESP GGTMAPQQPE GAKPQAQAAL AAPKKKTKKE KQQDATVEPE TEVVGPELPD DLEPQAAPTS TKKKKKKKER GHTVTEPIQP LEPELPGEGQ PEARATPGST KKRKKQSQES RMPETVPQEE MPGPPLNSES GEEAPTGRDK KRKQQQQQPV

  • Molecular Weight

    54.9 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.

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Protein Description

CD3eAP is a crucial protein involved in the signaling pathways of T cells, specifically within the context of T cell receptor (TCR) complex. As a member of the CD3 family, CD3eAP plays a significant role in T cell development, activation, and function by facilitating the transmission of activation signals upon TCR engagement. Research on CD3eAP has gained considerable interest due to its potential implications in immunological disorders and therapeutic interventions. Specifically, dysregulation of CD3eAP can lead to impaired T cell responses, contributing to conditions such as autoimmune diseases and cancer. Recent studies have focused on the recombinant expression of CD3eAP to better understand its structure-function relationships, molecular interactions, and its role in T cell signaling pathways. The generation of recombinant CD3eAP protein allows for advanced biochemical and biophysical analyses, such as binding affinity studies, structural characterization, and the exploration of its interactions with other components of the TCR complex. This research is pivotal in elucidating the mechanisms underlying T cell activation and might pave the way for developing novel immunotherapies aimed at modulating T cell responses. Furthermore, understanding CD3eAP's role could contribute to optimizing therapeutic strategies for enhancing immune responses against tumors or infectious agents, thus holding promise for improved treatments in various immunological conditions. Overall, the study of CD3eAP represents a significant avenue in the broader field of immunology, with the potential to inform future clinical applications in immunotherapy and disease management.

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