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Recombinant Human DNA polymerase epsilon subunit 3 (POLE3)

ACP11202

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP11202 Target NamePOLE3
FormLyophilized powderExpression SystemCustom Production. Please inquire and provide the desire expression system.
Expression Range2-147Protein LengthFull Length of Mature Protein
Purity>85% (SDS-PAGE)Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDQ9NRF9
Background Information
  • Uniprot Id

    Q9NRF9

  • Target Species

    Human

  • Target Name

    POLE3

  • Target Full Name

    DNA polymerase epsilon subunit 3

  • Target Function

    Accessory component of the DNA polymerase epsilon complex. Participates in DNA repair and in chromosomal DNA replication. Forms a complex with CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1. Does not enhance nucleosome sliding activity of the ACF-5 ISWI chromatin remodeling complex.

  • Target Subcellular Location

    Nucleus.

  • Target Tissue Specificity

    Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

  • Target Synonyms

    Arsenic transactivated protein; Arsenic-transactivated protein; ASTP; CHARAC 17; CHARAC17; CHRAC 17 ; CHRAC-17; CHRAC17; Chromatin Accessibility Complex 17; Chromatin accessibility complex 17 kDa protein; DNA Polymerase Epsilon p17 Subunit; DNA polymerase epsilon subunit 3; DNA polymerase epsilon subunit p17; DNA polymerase II subunit 3; DPOE3_HUMAN; Histone fold protein CHRAC17; HuCHRAC 17; HuCHRAC17; p17; p17 subunit; POL E3; POLE 3; POLE3; Polymerase (DNA directed) epsilon 3; YBL 1; YBL1

  • Target Background

    POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexes for DNA transcription, replication, and packaging.

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