Overview

  • Product name
    Recombinant Human AP-Q protein
  • Protein length
    Full length protein

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      MKVENFKTSEIQELFDIFTYSKGASMARMLSCFLNEHLFVSALKSYLKTF SYSNAEQDDLWRHFQMAIDDQSTVILPATIKNIMDSWTHQSGFPVITLNV STGVMKQEPFYLENIKNRTLLTSNDTWIVPILWIKNGTTQPLVWLDQSSK VFPEMQVSDSDHDWVILNLNMTGYYRVNYDKLGWKKLNQQLEKDPKMR
    • Amino acids
      1 to 198
    • Tags
      proprietary tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab165911 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.

    Previously labelled as Laeverin.

  • 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
    • Aminopeptidase Q
    • AMPQ_HUMAN
    • AP-Q
    • APQ
    • Aqpep
    • CHL2 antigen
    • FLJ90650
    • Laeverin
    • LVRN
    • MGC125378
    • MGC125379
    • RGD1562779
    see all
  • Function
    Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C.
  • Tissue specificity
    Specifically expressed in placenta and not in other tissues. Mainly found at the cell surface region of the extravillous trophoblasts. Detected on extravillous trophoblasts in the outer layer of the chorion laeve in the fetal membrane Not detected on either fetal amnionic epithelial cells or maternal decidual cells. Also detected in the migrating extravillous trophoblasts in the maternal decidual tissues (at protein level).
  • Sequence similarities
    Belongs to the peptidase M1 family.
  • Post-translational
    modifications
    N-glycosylated.
  • Cellular localization
    Membrane.
  • Information by UniProt

Images

  • ab165911 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab165911 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

There are currently no Customer reviews or Questions for ab165911.
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