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Rabbit anti-Human CRABP1 Polyclonal Antibody

The antibody against CRABP1 was raised in rabbit using the Human CRABP1 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB.

ADC-48866A

The antibody against CRABP1 was raised in rabbit using the Human CRABP1 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB.

$600.00

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Specifications


Cat.No ADC-48866A ClonalityPolyclonal
Host SpeciesRabbitTarget NameCRABP1
FormLiquidSpecies ReactivityHuman, Mouse, Rat
IsotypeIgGStorage Buffer50% Glycerol, Avoid freeze / thaw cycles., PBS with 0.1% Sodium Azide
Purification MethodAntigen affinity purifiedConjugateNon-conjugated
ApplicationELISA, WBStorageUpon receipt

Immunogen Information


Immunogen DescriptionHuman CRABP1Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDP29762
Background Information
  • Uniprot Id

    P29762

  • Target Species

    Human

  • Target Name

    CRABP1

  • Target Full Name

    Cellular retinoic acid-binding protein 1

  • Target Function

    Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.

  • Target Subcellular Location

    Cytoplasm.

  • Target Protein Families

    Calycin superfamily, Fatty-acid binding protein (FABP) family

  • Target Research Area

    Transport

  • Target Synonyms

    Cellular retinoic acid binding protein 1; Cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding protein I; CRABP 1; CRABP; CRABP I; CRABP-I; Crabp1; CRABPI; RABP1_HUMAN; RBP 5; RBP5; Retinoic acid binding protein I cellular

  • Target Background

    This gene encodes a specific binding protein for a vitamin A family member and is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. It is structurally similar to the cellular retinol-binding proteins, but binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue.

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