MMP-8 Native Protein

Product Discontinued

MMP-8 Native Protein Summary

• Description: Native MMP-8
  
  

  
  Amino Acid Sequence: (P22894)

• Details of Functionality: The latent 58-kDa form can be activated by both p-chloromercuribenzoate PCMB (0.1 mM) and trypsin (10 ug/ml) at 25 degrees C for 20 min, but PCMB is substantially more effective. The latent 58-kDa form can also be activated using 2 mM (final concentration) aminophenylmercuric acetate (APMA) or 1 mM mersalylic acid for 60 min. at 37 degrees C. Either activation method will result in the preparation having a comparable catalytic efficiency against a peptide or gelatin substrate.
• Source: Human neutrophil granulocytes (Buffy Coat)
• Protein/Peptide Type: Native Protein
• Gene: MMP8
• Purity: SDS-PAGE

Applications/Dilutions

• Dilutions:
  • Enzyme Activity
• Application Notes: Protein concentration >100 mU/mg. The activated enzyme is inhibited by tissue inhibitors of matrix metalloproteinase-1 (TIMP-1) and by chelators of divalent cations like EDTA or o-phenanthroline.
• Theoretical MW: 41 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Store at -80C. Avoid freeze-thaw cycles.
• Buffer: 50 mM Tris-HCl (pH 7), 200 mM NaCl, 5 mM CaCl2, 1 uM ZnCl2, 0.05% Brij 35
• Preservative: 0.05% Sodium Azide
• Purity: SDS-PAGE

Alternate Names for MMP-8 Native Protein

• CLG1HNC
• Collagenase 2
• EC 3.4.24
• EC 3.4.24.34
• matrix metallopeptidase 8 (neutrophil collagenase)
• matrix metalloproteinase 8 (neutrophil collagenase)
• Matrix metalloproteinase-8
• MMP8
• MMP-8
• neutrophil collagenase
• PMNL collagenase
• PMNL-CL

Background

Human neutrophil collagenase (HNC) has been purified from extracts of fresh and outdated buffy coats and from exudates of phorbol myristate acetate-stimulated neutrophils. The MMP-8 present in the starting material can either be latent or active, or have an app. relative molecular mass of 75-kDa and/or 58-kDa. The rather complex pattern of activation of the latent 58-kDa and 75-kDa species by trypsin, organomercurials and oxidants has been investigated. MMP-8 was shown to preferentially hydrolyze type I over type II, and type III collagens in solution and to be a glycoprotein that contains complex N-linked oligosaccharides leading to multiple forms of MMP-8 in SDS-PAGE. The action of endoglycosidase on the latent 58-kDa form produces 42/40-kDa species (Gao et al. 1992, Mallya et al. 1990). This indicates that MMP-8 is an N-linked, complex glycoprotein that appears to be glycosylated at multiple sites.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Bioinformatics

• Gene Symbol: MMP8