Overview

Description

  • Nature
    Native
  • Source
    Native
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      FPVSSKEKNTKTVQDYLEKFYQLPSNQYQSTRKNGTNVIVEKLKEMQRFF GLNVTGKPNEETLDMMKKPRCGVPDSGGFMLTPGNPKWERTNLTYRIRNY TPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDN SPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFG HSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYGLSSNPIQP TGPSTPKPCDPSLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISL FWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGYDILQGYPKDISNYGF PSSVQAIDAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGI ESKVDAVFQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG
    • Molecular weight
      85 kDa
    • Amino acids
      21 to 467

Specifications

Our Abpromise guarantee covers the use of ab168050 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

    SDS-PAGE

  • Purity
    >90% by SDS-PAGE.

  • Form
    Liquid
  • Additional notes
    Precursor enzyme needs activation using 2mM AMPA (aminophenylmercuric acetate) or 1mM mersalylic acid for 60 min. at 37°C. Alternatively use 0.1mM PCMB (p-chloromercuribenzoate) or 10µg/ml trypsin for 20 min. at 25°C; PCMB is substantially more effective.

    The active enzyme is inhibited by TIMP-1 (tissue inhibitor of matrix metalloproteinase-1) and by chelators of divalent cations like EDTA or o-phenantroline. =60mU/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol 2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    pH: 7.00
    Preservative: 0.05% Sodium azide
    Constituents: 0.05% Brij, 0.06% Calcium chloride, 0.00001% Zinc chloride, 0.79% Tris HCl, 1.17% Sodium chloride

General Info

  • Alternative names
    • CLG 1
    • CLG1
    • Collagenase 1
    • Collagenase 1 neutrophil
    • HNC
    • Matrix metallopeptidase 8 (neutrophil collagenase)
    • Matrix metalloprotease 8
    • Matrix metalloproteinase-8
    • MMP 8
    • MMP-8
    • Mmp8
    • MMP8_HUMAN
    • Neutrophil collagenase
    • PMNL CL
    • PMNL collagenase
    • PMNL-CL
    • PMNLCL
    see all
  • Function
    Can degrade fibrillar type I, II, and III collagens.
  • Tissue specificity
    Neutrophils.
  • Sequence similarities
    Belongs to the peptidase M10A family.
    Contains 4 hemopexin-like domains.
  • Domain
    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.
  • Cellular localization
    Cytoplasmic granule. Secreted > extracellular space > extracellular matrix. Stored in intracellular granules.
  • Information by UniProt

References

ab168050 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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