Cat: PA2000-825DB

Recombinant Human GALP Protein,His

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Analytical Data

  • Gene name

    GALP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    GALP;Galanin-like peptide

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9UBC7

  • Expression Region

    25-84aa

  • AA Sequence

    APAHRG RGGWTLNSAG YLLGPVLHLP QMGDQDGKRE TALEILDLWK AIDGLPYSHP PQPS

  • Molecular Weight

    12.5 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.

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Protein Description

GALP (Galanin-like peptide) is a neuropeptide that has gained attention in the field of biomedical research due to its involvement in several physiological processes, including appetite regulation, energy homeostasis, and stress responses. Originating from the hypothalamus, GALP interacts with galanin receptors, influencing neuroendocrine functions and potentially serving as a target for obesity and metabolic disorder treatments. Research on GALP is pivotal as it provides insights into its roles in neurobiology and metabolic regulation. The structural characteristics and conformational dynamics of GALP, as well as its interaction with receptors, are crucial for understanding its functional mechanisms. Recombinant GALP production allows scientists to study its properties in a controlled environment, enabling investigations into its pharmacological applications. Understanding the structure-function relationship of GALP can lead to the discovery of novel therapeutic approaches for obesity and related metabolic conditions. As research progresses, the potential of GALP as a biomarker or therapeutic target may unveil new pathways for treating metabolic disorders and improving health outcomes.

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