Recombinant Mouse Cathepsin E protein (ab185383)

Overview

Description

  • Nature
    Recombinant
  • Source
    HEK 293 cells
  • Amino Acid Sequence
    • Accession
    • Species
      Mouse
    • Sequence
      SCNVYSSVNEPLINYLDMEYFGTISIGTPPQNFTVIFDTGSSNLWVPSVY CTSPACKAHPVFHPSQSDTYTEVGNHFSIQYGTGSLTGIIGADQVSVEGL TVDGQQFGESVKEPGQTFVNAEFDGILGLGYPSLAAGGVTPVFDNMMAQN LVALPMFSVYLSSDPQGGSGSELTFGGYDPSHFSGSLNWIPVTKQAYWQI ALDGIQVGDTVMFCSEGCQAIVDTGTSLITGPPDKIKQLQEAIGATPIDG EYAVDCATLDTMPNVTFLINEVSYTLNPTDYILPDLVEGMQFCGSGFQGL DIPPPAGPLWILGDVFIRQFYSVFDRGNNQVGLAPAVPVDHHHHHH
    • Molecular weight
      37 kDa including tags
    • Amino acids
      61 to 397
    • Tags
      His tag C-Terminus
    • Additional sequence information
      Mature form.

Specifications

Our Abpromise guarantee covers the use of ab185383 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

    HPLC

  • Endotoxin level
    < 1.000 Eu/µg
  • Purity
    >95% by SDS-PAGE .

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.

    pH: 5.0
    Constituents: 0.39% MES, 0.88% Sodium chloride

    0.2 µM filtered

General Info

  • Alternative names
    • CATE
    • CATE_HUMAN
    • Cathepsin E
    • Cathepsin E form II
    • CTSE
    • Erythrocyte membrane aspartic proteinase
    • Slow moving proteinase
    see all
  • Function
    May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain.
  • Tissue specificity
    Expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. Not expressed in resting B-lymphocytes.
  • Sequence similarities
    Belongs to the peptidase A1 family.
  • Post-translational
    modifications
    Glycosylated. The nature of the carbohydrate chain varies between cell types. In fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In erythrocyte membranes, both the proenzyme and mature enzyme contain a complex-type oligosaccharide.
    Two forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57.
  • Cellular localization
    Endosome. The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome.
  • Information by UniProt

References

ab185383 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

There are currently no Customer reviews or Questions for ab185383.
Please use the links above to contact us or submit feedback about this product.

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

Sign up