• Product name

    Recombinant human ADAMTS5 protein
    See all ADAMTS5 proteins and peptides
  • Biological activity

    Aggrecanase activity of ab134432 is determined with recombinant aggrecan interglobular domain. ADAMTS4 hydrolyzes the aggrecanase site within this domain (peptide bond E373-A374 in Human aggrecan). The recombinant substrate is incubated at a concentration of 0.1 µM with ADAMTS5 in 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 M CaCl2, 1 µM leupeptin, 1 µM pepstatin, 1 mM Pefabloc, 0.05 % Brij 35 for 15 min at 37°C. A series of ADAMTS5 dilutions ranging from 103 - to 105 -fold is tested. Substrate cleavage at the aggrecanase-site is estimated from the appearance of the hydrolysis fragment with the novel N terminus ARGSVIL. The fragment is quantified with two monoclonal antibodies, one directed against the neoepitope ARGSVIL, the other against the sequence C terminal from the neoepitope. Under the specified conditions the hydrolysis rate is > 0.5 nmoles hydrolyzed substrate/ min x ml ADAMTS5 preparation or > 5 nmoles hydrolyzed substrate/ min x mg.
  • Purity

    >= 50 % SDS-PAGE.
    ab134432 was determined to be >50% pure by SDS-PAGE.
  • Expression system

    Baculovirus infected insect cells
  • Accession

  • Protein length

    Protein fragment
  • Animal free

  • Nature

    • Species

    • Predicted molecular weight

      41 kDa including tags
    • Tags

      His tag C-Terminus
    • Additional sequence information

      Recombinant human ADAMTS5 truncated (the sequence of aminoacids: 625-930 is missing)......


Our Abpromise guarantee covers the use of ab134432 in the following tested applications.

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

  • Applications


    Functional Studies

    Inhibition Assay

  • Form

  • Additional notes

    ab134432 contains the catalytic domain, the disintegrin domain and the thrombospondin type 1 motif of full length ADAMTS5.

  • 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: 7.50
    Preservative: 0.34% Imidazole
    Constituents: 0.05% Brij, 0.05% Calcium chloride, 0.79% Tris HCl, 0.88% Sodium chloride

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names

    • A disintegrin and metalloproteinase with thrombospondin motifs 11
    • A disintegrin and metalloproteinase with thrombospondin motifs 5
    • A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif 5
    • A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase 2)
    • A disintegrin-like and metalloprotease with thrombospondin type 1 motif, 5
    • A Disintigrin And Metalloproteinase with ThromboSpondin motif-5
    • ADAM metallopeptidase with thrombospondin type 1 motif 5
    • ADAM TS 11
    • ADAM TS 5
    • ADAM TS5
    • ADAM-TS 11
    • ADAM-TS 5
    • ADAM-TS5
    • ADAMTS 11
    • ADAMTS 5
    • ADAMTS-11
    • ADAMTS-5
    • ADAMTS11
    • ADAMTS11, formerly
    • Adamts5
    • ADMP 2
    • ADMP-2
    • ADMP2
    • Aggrecanase 2
    • Aggrecanase-2
    • ATS5_HUMAN
    • FLJ36738
    • Implantin
    • ThromboSpondin motif-5
    see all
  • Function

    Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.
  • Tissue specificity

    Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.
  • Sequence similarities

    Contains 1 disintegrin domain.
    Contains 1 peptidase M12B domain.
    Contains 2 TSP type-1 domains.
  • Domain

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
  • Post-translational

    The precursor is cleaved by a furin endopeptidase.
  • Cellular localization

    Secreted > extracellular space > extracellular matrix.
  • Information by UniProt


  • SDS-PAGE analysis of ab134432 (1.5 µg)


ab134432 has not yet been referenced specifically in any publications.

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