Recombinant Human MMP9 protein (Proenzyme) (ab82955)

Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Amino acids
      20 to 707
    • Tags
      His tag N-Terminus
    • Additional sequence information
      Corresponding to the pro form of the protein minus the signal peptide with a N-terminal 6X his tag.

Specifications

Our Abpromise guarantee covers the use of ab82955 in the following tested applications.

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

  • Applications

    ELISA

    SDS-PAGE

    Western blot

  • 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. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 50% Glycerol, PBS, pH 7.2

General Info

  • Alternative names
    • 82 kDa matrix metalloproteinase-9
    • 92 kDa gelatinase
    • 92 kDa type IV collagenase
    • CLG 4B
    • CLG4B
    • Collagenase Type 4 beta
    • Collagenase type IV 92 KD
    • EC 3.4.24.35
    • Gelatinase 92 KD
    • Gelatinase B
    • Gelatinase beta
    • GelatinaseB
    • GELB
    • Macrophage gelatinase
    • MANDP2
    • Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
    • Matrix Metalloproteinase 9
    • MMP 9
    • MMP-9
    • MMP9
    • MMP9_HUMAN
    • Type V collagenase
    see all
  • Function
    May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-
    -Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
  • Tissue specificity
    Produced by normal alveolar macrophages and granulocytes.
  • Involvement in disease
    Intervertebral disc disease
    Metaphyseal anadysplasia 2
  • Sequence similarities
    Belongs to the peptidase M10A family.
    Contains 3 fibronectin type-II domains.
    Contains 4 hemopexin repeats.
  • 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.
  • Post-translational
    modifications
    Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
    N- and O-glycosylated.
  • Cellular localization
    Secreted, extracellular space, extracellular matrix.
  • Information by UniProt

Images

References

ab82955 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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