Recombinant Human CRABP2 protein (ab117162)

Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL ILTMTADDVV CTRVYVRE
    • Molecular weight
      16 kDa
    • Amino acids
      1 to 138
    • Additional sequence information
      CRABP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids and having a molecular mass of 15.6 kDa.

Specifications

Our Abpromise guarantee covers the use of ab117162 in the following tested applications.

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

  • Applications

    SDS-PAGE

  • Purity
    > 95 % SDS-PAGE.
    ab117162 is purified by proprietary chromatographic techniques and filter sterilized.
  • Form
    Liquid
  • Additional notes
    For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
  • 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 long term. Avoid freeze / thaw cycle.

    pH: 8.00
    Constituents: 0.32% Tris HCl, 20% Glycerol

General Info

  • Alternative names
    • Cellular retinoic acid binding protein 2
    • Cellular retinoic acid binding protein II
    • Cellular retinoic acid-binding protein 2
    • Cellular retinoic acid-binding protein II
    • CRABP II
    • CRABP-II
    • Crabp2
    • CRABPII
    • RABP2_HUMAN
    • RBP6
    • Rretinoic acid-binding protein, cellular, type II
    see all
  • Function
    Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.
  • Sequence similarities
    Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.
  • Domain
    Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
  • Cellular localization
    Cytoplasm. Nucleus. Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus.
  • Information by UniProt

References

ab117162 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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