Cat: IPD-X40420

Recombinant Human PTPA Protein ,His & SUMO

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Analytical Data

  • Gene name

    PTPA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PP2A, subunit B', PR53 isoform Phosphotyrosyl phosphatase activator

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q15257

  • Expression Region

    2-358aa

  • Molecular Weight

    60.5 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

PTPA (Protein Phosphatase 2A regulatory subunit B' alpha) is a crucial protein involved in the regulation of various cellular processes, including cell growth, division, and apoptosis. As a member of the protein phosphatase family, PTPA plays a vital role in dephosphorylating serine and threonine residues on target proteins, thus modulating their activity and function. Research into PTPA has garnered significant interest due to its implications in numerous diseases, particularly cancer, where dysregulation of protein phosphorylation cascades contributes to aberrant cell signaling. Furthermore, PTPA has been implicated in the development of neurodegenerative disorders, highlighting its potential as a therapeutic target. Scientists are actively investigating the structural and functional properties of PTPA, employing techniques such as X-ray crystallography and NMR spectroscopy, to better understand its mechanisms of action. In addition, studies focused on PTPA's interactions with other proteins and its role in cellular signaling pathways are paving the way for novel therapeutic approaches. The ongoing exploration of PTPA’s function and regulation not only enhances our fundamental understanding of cellular signaling but also opens avenues for the development of targeted interventions in disease contexts where PTPA is implicated.

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