Cat: PA1000-9065

Recombinant Human GPAM Protein,His

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Analytical Data

  • Gene name

    GPAM

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    GPAM;GPAT1;KIAA1560;Glycerol-3-phosphate acyltransferase 1. mitochondrial

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9HCL2

  • Expression Region

    1-828aa

  • AA Sequence

    MDESALTLGTIDVSYLPHSSEYSVGRCKHTSEEWGECGFRPTIFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKRILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDVLYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNVIPDILIIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSALLSLEQALLPAILPSRPSDAADEGRDTSINESRNATDESLRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCVTITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLNKRGLGGPTSTPPNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCHETVGKFIQYGILTVAEHDDQEDISPSLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAIFVHNFSGPVPEPEYLQKLHKYLITRTERNVAVYAESATYCLVKNAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL

  • Molecular Weight

    93.7 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

GPAM (Glycerol-3-Phosphate Acyltransferase) is an important enzyme involved in lipid metabolism, particularly in the synthesis of glycerolipids, which are critical components of cell membranes and energy storage in organisms. The study of GPAM has gained significance due to its role in various metabolic disorders, including obesity, diabetes, and cardiovascular diseases. As a key regulator of diacylglycerol and triglyceride levels, GPAM influences energy homeostasis and lipid composition in adipose tissue and other cell types. Researchers have been increasingly focused on understanding the structure and function of GPAM, exploring its enzymatic mechanisms and regulatory pathways. The identification of GPAM's specific isoforms and their distinct roles in different tissues opens new avenues for therapeutic interventions aimed at managing lipid-related diseases. Additionally, GPAM's involvement in fatty acid composition and its potential as a target for drug development have prompted the synthesis of recombinant GPAM proteins for in vitro studies. These recombinant proteins facilitate a deeper understanding of GPAM's biochemical properties, substrate specificity, and interactions with other metabolic enzymes. By elucidating the functional aspects of GPAM through recombinant protein research, scientists aim to uncover novel strategies to modulate lipid metabolism and develop new dietary or pharmaceutical approaches to treat metabolic disorders effectively. Therefore, ongoing research into GPAM not only enhances our biological understanding but also holds promise for potential clinical applications in combating lipid metabolism-related diseases.

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