Cat: IPD-X33831

Recombinant Human ADSL/Adenylosuccinate Lyase Protein,His

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Analytical Data

  • Gene name

    ADSL/Adenylosuccinate Lyase

  • 简介

    ADSL/Adenylosuccinate Lyase Protein catalyzes two non-sequential steps in de novo AMP synthesis. It converts SAICAR to fumarate and 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, contributing to de novo IMP synthesis. Additionally, it converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. ADSL/Adenylosuccinate Lyase Protein, Human (His) is the recombinant human-derived ADSL/Adenylosuccinate Lyase protein, expressed by E. coli , with N-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Adenylosuccinate lyase; ADSL; ASL; Asase; AMPS

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-6*His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P30566-1

  • Expression Region

    M1-L484

  • AA Sequence

    MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKAELCL

  • Protein Length

    Full Length of Isoform-1

  • Molecular Weight

    56 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

Adenylosuccinate lyase (ADSL) is a crucial enzyme involved in the purine nucleotide synthesis pathway, catalyzing the conversion of adenylosuccinate to adenine monophosphate (AMP) and fumarate. Mutations in the ADSL gene can lead to a rare but severe genetic disorder known as adenylosuccinate lyase deficiency, which is characterized by a range of neurological symptoms, intellectual disability, and developmental delays. The exploration of ADSL has garnered significant attention in biochemistry and molecular biology, particularly regarding the mechanisms underlying its enzymatic function and the repercussions of genetic mutations. The recombinant production of ADSL protein enables researchers to study its structure and function in depth, assess the effects of specific mutations, and explore potential therapeutic interventions. Characterizing the enzyme's kinetics and identifying inhibitors could yield insights into drug design for related metabolic disorders. Understanding ADSL not only sheds light on fundamental biochemical pathways but also has implications for the development of targeted therapies for patients afflicted with ADSL deficiency. As recombinant protein technology continues to evolve, ongoing research aims to enhance our understanding of this critical enzyme, paving the way for novel diagnostic and therapeutic strategies.

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