Overview

Description

  • Nature
    Synthetic

Associated products

Specifications

Our Abpromise guarantee covers the use of ab45240 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

    Blocking - Blocking peptide for Anti-ADAMTS7 antibody (ab45044)

  • Purity
    > 95 % SDS-PAGE.

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    Preservative: None
    Constituents: 0.001% Tween 20, 30mM HEPES, 2mM EDTA, 150mM Sodium chloride, pH 6.75

General Info

  • Alternative names
    • A disintegrin and metalloprotease with thrombospondin motifs 7 preproprotein
    • A disintegrin and metalloproteinase with thrombospondin motifs 7
    • A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif 7
    • A disintegrin like and metalloprotease with thrombospondin type 1 motif 7
    • ADAM metallopeptidase with thrombospondin type 1 motif 7
    • ADAM metallopeptidase with thrombospondin type 1 motif 7 preproprotein
    • ADAM TS 7
    • ADAM TS7
    • ADAM-TS 7
    • ADAM-TS7
    • ADAMTS 7
    • ADAMTS-7
    • Adamts7
    • ATS7_HUMAN
    • COMPase
    • DKFZp434H204
    see all
  • Function
    Metalloprotease that may play a role in the degradation of COMP.
  • Tissue specificity
    Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Detected in meniscus, bone, tendon, cartilage, synovium, fat and ligaments.
  • Sequence similarities
    Contains 1 disintegrin domain.
    Contains 1 peptidase M12B domain.
    Contains 1 PLAC domain.
    Contains 8 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
    modifications
    N-glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs. N- and C-glycosylations can also facilitate secretion. O-glycosylated proteoglycan. Contains chondroitin sulfate.
    May be cleaved by a furin endopeptidase (By similarity). The precursor is sequentially processed.
  • Cellular localization
    Secreted, extracellular space, extracellular matrix. Also found associated with the external cell surface.
  • Information by UniProt

References

ab45240 has not yet been referenced specifically in any publications.

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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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