Overview

Description

  • Nature
    Recombinant
  • Source
    HEK 293 cells
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      FPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQE FFGLKVTGKP DAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRAD VDHAIEKAFQ LWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGP GIGGDAHFDE DERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLA QDDIDGIQAI YGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFY PEVELNFISV FWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFG FPRTVKHIDA ALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAV FMKDGFFYFF HGTRQYKFDPKTKRILTLQKANSWFNCRKNVD
    • Amino acids
      20 to 469
    • Tags
      His tag C-Terminus

Specifications

Our Abpromise guarantee covers the use of ab151662 in the following tested applications.

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

  • Applications

    SDS-PAGE

    HPLC

  • Endotoxin level
    > 1.000 Eu/µg
  • Purity
    >95% by SDS-PAGE .

  • Form
    Liquid
  • 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: 5.50
    Constituents: 0.4% MES, 0.05% Brij, 0.88% Sodium chloride

General Info

  • Alternative names
    • 27 kDa interstitial collagenase
    • CLG
    • CLGN
    • collagenase, fibroblast
    • collagenase, interstitial
    • Fibroblast collagenase
    • Interstitial collagenase
    • Matrix metallopeptidase 1 (interstitial collagenase)
    • Matrix metalloprotease 1
    • Matrix Metalloproteinase 1
    • Matrix metalloproteinase-1
    • MMP 1
    • MMP-1
    • MMP1
    • MMP1_HUMAN
    • OTTHUMP00000045866
    see all
  • Function
    Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.
  • Sequence similarities
    Belongs to the peptidase M10A family.
    Contains 4 hemopexin-like domains.
  • Domain
    There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).
    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
    Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.
  • Cellular localization
    Secreted > extracellular space > extracellular matrix.
  • Information by UniProt

References

ab151662 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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