Overview

  • Product name
    Recombinant Human DPP1 protein
  • Protein length
    Full length protein

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQR DVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYK WFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVY VNTAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGD MIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVR NQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEG GFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGG FYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPF ELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAI ESIAVAATPIPKL
    • Amino acids
      1 to 463
    • Tags
      proprietary tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab158099 in the following tested applications.

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

  • Applications

    ELISA

    Western blot

  • Form
    Liquid
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • AI047818
    • CATC
    • CATC_HUMAN
    • Cathepsin C
    • Cathepsin J
    • CPPI
    • CTSC
    • Dipeptidyl peptidase 1
    • Dipeptidyl peptidase 1 light chain
    • Dipeptidyl peptidase I
    • Dipeptidyl peptidase I exclusion domain chain
    • Dipeptidyl peptidase I heavy chain
    • Dipeptidyl peptidase I light chain
    • Dipeptidyl transferase
    • DPP I
    • DPP-I
    • DPPI
    • EC 3.4.14.1
    • HMS
    • JP
    • JPD
    • MGC126959
    • PALS
    • PDON1
    • PLS
    see all
  • Function
    Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.
  • Tissue specificity
    Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas.
  • Involvement in disease
    Papillon-Lefevre syndrome
    Haim-Munk syndrome
    Periodontititis, aggressive, 1
  • Sequence similarities
    Belongs to the peptidase C1 family.
  • Post-translational
    modifications
    N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.
    In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond.
  • Cellular localization
    Lysosome.
  • Information by UniProt

Images

  • ab158099 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab158099 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

There are currently no Customer reviews or Questions for ab158099.
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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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