Overview

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      WVIEEWGECSKSCELGWQRRLVECRDINGQPASECAKEVKPASTRPCADH PCPQWQLGEWSSCSKTCGKGYKKRSLKCLSHDGGVLSHESCDPLKKPKHF IDFCTMAECS
    • Amino acids
      858 to 967
    • Tags
      proprietary tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab152994 in the following tested applications.

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

  • Applications

    Western blot

    ELISA

  • 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
    • A disintegrin and metalloproteinase with thrombospondin motifs 1
    • ADAM-TS 1
    • ADAM-TS1
    • ADAMTS
    • ADAMTS 1
    • ADAMTS-1
    • Adamts1
    • ATS1_HUMAN
    • C3 C5
    • KIAA1346,
    • METH 1
    • METH-1
    see all
  • Function
    Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture.
  • Sequence similarities
    Contains 1 disintegrin domain.
    Contains 1 peptidase M12B domain.
    Contains 3 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
    The precursor is cleaved by a furin endopeptidase.
  • Cellular localization
    Secreted > extracellular space > extracellular matrix.
  • Information by UniProt

Images

  • ab152994 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab152994 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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