Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      MASMTGGQQMGRGHHHHHHENLYFQGGEFFVLTEGNPRWEQTHLTYRIEN YTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRD NSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHEL GHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPI GPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVF WPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGF PRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFP GIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN
    • Molecular weight
      46 kDa including tags
    • Amino acids
      100 to 469
    • Additional sequence information
      22kDa interstitial collagenase fragment. constructed with codon optimization and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal. NCBI Accession No. NP_002412.

Specifications

Our Abpromise guarantee covers the use of ab185605 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

  • Purity
    >90% by SDS-PAGE.
    The final product was refolded using temperature shift inclusion body refolding technology and chromatographically purified.
  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

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

ab185605 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

There are currently no Customer reviews or Questions for ab185605.
Please use the links above to contact us or submit feedback about this product.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

Sign up