Overview

Description

  • Nature

    Recombinant
  • Source

    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Sequence

      YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM LPDDDVQGIQSLYGPGDEDPN
    • Molecular weight

      19 kDa
    • Amino acids

      104 to 274

Specifications

Our Abpromise guarantee covers the use of ab134452 in the following tested applications.

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

  • Biological activity

    The specific activity is >0.5 U/mg. 1 U is the activity that hydrolyzes 1 mmol peptide (7-methoxycoumarin-4-yl) acetyl-Pro-Leu-Gly-Leu-(3-[2, 4-dinitrophenyl]-L-2, 3-diamino-propionyl)-Ala-Arg-NH2 (Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg) within 1 min.
  • Applications

    SDS-PAGE

    Functional Studies

  • Purity

    > 90 % SDS-PAGE.

  • Form

    Liquid
  • 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
    Constituents: 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

    • CLG 3
    • CLG3
    • Collagenase 3
    • Collagenase3
    • MANDP1
    • Matrix metallopeptidase 13 (collagenase 3)
    • Matrix Metalloproteinase 13
    • Matrix metalloproteinase-13
    • MMP 13
    • MMP-13
    • Mmp13
    • MMP13_HUMAN
    see all
  • Function

    Degrades collagen type I. Does not act on gelatin or casein. Could have a role in tumoral process.
  • Tissue specificity

    Seems to be specific to breast carcinomas.
  • Involvement in disease

    Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia Missouri type (SEMD-MO) [MIM:602111]. A bone disease characterized by moderate to severe metaphyseal changes, mild epiphyseal involvement, rhizomelic shortening of the lower limbs with bowing of the femora and/or tibiae, coxa vara, genu varum and pear-shaped vertebrae in childhood. Epimetaphyseal changes improve with age.
    Defects in MMP13 are the cause of metaphyseal anadysplasia type 1 (MANDP1) [MIM:602111]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.
  • 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

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

Images

  • SDS-PAGE analysis of ab134452 (4µg).

References

ab134452 has not yet been referenced specifically in any publications.

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