Recombinant Human Dihydrofolate reductase (DHFR) protein (ab104018)

Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionP00374
    • SpeciesHuman
    • SequenceMGSSHHHHHH SSGLVPRGSH MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFKYFQRMTT TSSVEGKQNL VIMGRKTWFS IPEKNRPLKD RINIVLSREL KEPPRGAHFL AKSLDDALRL IEQPELASKV DMVWIVGGSS VYQEAMNQPG HLRLFVTRIM QEFESDTFFP EIDLGKYKLL PEYPGVLSEV QEEKGIKYKF EVYEKKD
    • Molecular weight24 kDa including tags
    • Amino acids1 to 187
    • TagsHis tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab104018 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Mass Spectrometry

    SDS-PAGE

  • Mass spectrometry
    MALDI-TOF
  • Purity> 95 % SDS-PAGE.

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    Preservative: None
    Constituents: 10% Glycerol, 20mM Tris HCl, 2mM DTT, 100mM Sodium chloride, pH 8

General Info

  • Alternative names
    • DHFR
    • DHFRP1
    • Dihydrofolate reductase
    • DYR
    • DYR_HUMAN
    • EC 1.5.1.3
    see all
  • FunctionKey enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
  • PathwayCofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
  • Sequence similaritiesBelongs to the dihydrofolate reductase family.
    Contains 1 DHFR (dihydrofolate reductase) domain.
  • Information by UniProt

Recombinant Human Dihydrofolate reductase (DHFR) protein images

  • 15% SDS-PAGE analysis of ab104018 (3 µg).

References for Recombinant Human Dihydrofolate reductase (DHFR) protein (ab104018)

ab104018 has not yet been referenced specifically in any publications.

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