Overview

  • Product name

    Recombinant Human CCP5 protein
  • Protein length

    Protein fragment

Description

  • Nature

    Recombinant
  • Source

    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Molecular weight

      28 kDa
    • Amino acids

      150 to 396
    • Tags

      His-DHFR tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab127254 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

  • Form

    Lyophilised
  • Additional notes

     This product was previously labelled as AGBL5

     

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20ºC.

    Constituents: 0.32% Tris HCl, 0.58% Sodium chloride

  • Reconstitution
    Reconstitute with water to desired concentration.

General Info

  • Alternative names

    • AGBL5
    • ATP/GTP binding protein like 5
    • ATP/GTP-binding protein-like 5
    • CBPC5_HUMAN
    • CCP5
    • Cytosolic carboxypeptidase like protein 5
    • Cytosolic carboxypeptidase-like protein 5
    • FLJ21839
    • Hypothetical protein FLJ21839
    see all
  • Function

    Metallocarboxypeptidase that mediates tubulin deglutamylation. Specifically catalyzes the deglutamylation of the branching point glutamate side chains generated by post-translational glutamylation in proteins such as tubulins. In contrast, it is not able to act as a long-chain deglutamylase that shortens long polyglutamate chains, a process catalyzed by AGTPBP1/ CCP1, AGBL1/CCP4 and AGBL4/CCP6.
  • Tissue specificity

    Expressed in brain.
  • Sequence similarities

    Belongs to the peptidase M14 family.
  • Cellular localization

    Cytoplasm > cytosol. Nucleus. Mainly cytoplasmic. Slight accumulation in the nucleus is observed.
  • Information by UniProt

References

ab127254 has not yet been referenced specifically in any publications.

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