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Rabbit anti-Human PFAS Polyclonal Antibody

The antibody against PFAS was raised in rabbit using the Recombinant Human Inhibin alpha chain protein (1064-1302AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, IHC.

ADC-10919A

The antibody against PFAS was raised in rabbit using the Recombinant Human Inhibin alpha chain protein (1064-1302AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, IHC.

$299.00

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Specifications


Cat.No ADC-10919A ClonalityPolyclonal
Host SpeciesRabbitTarget NamePFAS
FormLiquidSpecies ReactivityHuman
IsotypeIgGStorage Buffer0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4
Purification Method>95%, Protein G purifiedConjugateNon-conjugated
ApplicationELISA, IHCStorageUpon receipt

Immunogen Information


Immunogen DescriptionRecombinant Human Inhibin alpha chain protein (1064-1302AA)Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDO15067
Background Information
  • Uniprot Id

    O15067

  • Target Species

    Human

  • Target Name

    PFAS

  • Target Full Name

    Phosphoribosylformylglycinamidine synthase

  • Target Function

    Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.

  • Target Subcellular Location

    Cytoplasm.

  • Target Protein Families

    FGAMS family

  • Target Synonyms

    PFAS; KIAA0361; Phosphoribosylformylglycinamidine synthase; FGAM synthase; FGAMS; EC 6.3.5.3; Formylglycinamide ribonucleotide amidotransferase; FGAR amidotransferase; FGAR-AT; Formylglycinamide ribotide amidotransferase

  • Target Background

    Purines are necessary for many cellular processes, including DNA replication, transcription, and energy metabolism. Ten enzymatic steps are required to synthesize inosine monophosphate (IMP) in the de novo pathway of purine biosynthesis. The enzyme encoded by this gene catalyzes the fourth step of IMP biosynthesis.

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