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

      GST 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.
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