Cat: IPD-X30616

Recombinant E.coli DNA helicase II/uvrD Protein

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Analytical Data

  • Gene name

    DNA helicase II/uvrD

  • 简介

    DNA helicase II/uvrD Protein, E.coli encodes an 82-kDa protein with both ATPase and helicase activities. DNA helicase II/uvrD Protein, E.coli unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present. DNA helicase II/uvrD Protein, E.coli is involved in methyl-directed mismatch repair and nucleotide excision repair of DNA[1][2][3] DNA helicase II/uvrD Protein, E.coli is the recombinant E. coli-derived DNA helicase II/uvrD protein, expressed by E. coli , with tag free.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    pdeB; DNA helicase II

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    Tag Free

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P03018

  • Expression Region

    M1-V720

  • AA Sequence

    MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQLRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGADGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAECAILYRSNAQSRVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIANRNDDAAFERVVNTPTRGIGDRTLDVVRQTSRDRQLTLWQACRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQTDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAALEAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAYVGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMGTPMVENDSGYKLGQRVRHAKFGEGTIVNMEGSGEHSRLQVAFQGQGIKWLVAAYARLESV

  • Protein Length

    Full Length

  • Molecular Weight

    82.0 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

DNA helicase II, also known as UvrD, plays a crucial role in the maintenance of genomic stability by unwinding double-stranded DNA during processes such as DNA repair and replication. UvrD is classified as a DNA helicase, which catalyzes the separation of the two DNA strands, allowing access for various repair and replication machinery. This protein is particularly significant in the context of nucleotide excision repair (NER), where it helps to remove damaged DNA segments. Mutations or malfunctions in UvrD can lead to increased susceptibility to DNA damage and genomic instability, which are hallmarks of various cancers and genetic disorders. The study of UvrD is thus pivotal for understanding the molecular mechanisms underlying DNA repair and its implications in disease. Research into the biochemical properties and structural characteristics of UvrD not only enhances our knowledge of its function but may also unveil potential therapeutic targets for diseases linked to DNA repair deficiencies. Consequently, the investigation of UvrD’s catalytic mechanisms and interactions with other proteins involved in DNA processing remains a significant area of interest in molecular biology and genetics.

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