Cat: PA1000-2966

Recombinant Human SNAPAP Protein,His

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Analytical Data

  • Gene name

    SNAPAP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    SNAPIN;BLOC1S7;SNAP25BP;SNAPAP;SNARE-associated Protein Snapin

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O95295

  • Expression Region

    2-136aa

  • AA Sequence

    AGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK

  • 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

SNAPAP, a member of the synaptosomal-associated protein family, has garnered significant attention in the field of neurobiology due to its potential role in synaptic transmission and plasticity. Research into SNAPAP began with its identification in synaptic vesicles, where it is believed to play a critical role in the regulation of neurotransmitter release. The protein’s involvement in synaptic mechanisms suggests that it may contribute to various neurological processes, including learning and memory. Recent studies have focused on the structural and functional characterization of recombinant SNAPAP, enabling scientists to investigate its interactions with other proteins involved in synaptic function. Additionally, the potential link between SNAPAP and neurodegenerative diseases has prompted further exploration, as alterations in synaptic proteins are often observed in conditions such as Alzheimer’s and Parkinson’s disease. Understanding the biochemical pathways associated with SNAPAP could provide insights into therapeutic targets for these disorders, making it a pivotal focus of current research in neurobiology and protein engineering.

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