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MMP8 Protein (AA 21-467, C-Term)

Recombinant MMP8 protein expressed in HEK-293 Cells.
Catalog No. ABIN2666511

Quick Overview for MMP8 Protein (AA 21-467, C-Term) (ABIN2666511)

Target

See all MMP8 Proteins
MMP8 (Matrix Metallopeptidase 8 (Neutrophil Collagenase) (MMP8))

Protein Type

Recombinant

Biological Activity

Active

Origin

  • 11
  • 5
  • 4
  • 2
  • 1
Human

Source

  • 11
  • 7
  • 2
  • 1
  • 1
HEK-293 Cells

Application

Flow Cytometry (FACS)

Purity

> 95 % , as determined by Coomassie stained SDS-PAGE.
  • Protein Characteristics

    AA 21-467, C-Term

    Sterility

    0.22 μm filtered

    Endotoxin Level

    Less than 1.0 EU per μg of protein as determined by the LAL method.

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  • Application Notes

    Optimal working dilution should be determined by the investigator.

    Comment

    Biological activity: Activated human MMP-8 is able to cleave the peptide substrate Mca-KPLGL-Dpa-AR-NH2 with an activity above 375 pmol/min/μg.

    Restrictions

    For Research Use only
  • Format

    Liquid

    Reconstitution

    For maximum results, quick spin vial prior to opening.

    Buffer

    0.22 μm filtered protein solution is in TCN (25 mM TRIS, 10 mM CaCl2, 150 mM NaCl, pH 7.5).

    Handling Advice

    Avoid repeated freeze/thaw cycles.

    Storage

    -20 °C

    Storage Comment

    Unopened vial can be stored at -70°C for six months.
  • Target

    MMP8 (Matrix Metallopeptidase 8 (Neutrophil Collagenase) (MMP8))

    Alternative Name

    MMP-8

    Background

    MMP-8, also termed neutrophil collagenase, is a member of the matrix metalloproteinase family proteins (MMPs). Members of this family are structurally related, zinc-containing enzymes that degrade the extracellular matrix (ECM) and connective tissue proteins. MMP-8 consists of a prodomain that is cleaved upon activation, a catalytic domain containing the zinc binding site, a hinge region, and a carboxyl terminal domain with hemopexin-like repeats. Substrates of MMP-8 include type I, II, and III triple-helical collagens, gelatin peptides, proteoglycans, fibronectin, aggrecan, substance P, serpins, β-casein, and angiotensin. MMP-8 is released by neutrophils upon IL-1β IL-8, GM-CSF and TNF-α stimulation. Besides playing a role in phagocytosis, MMP-8 has been implicated in rheumatoid arthritis (RA) because of its high efficiency in infiltrating connective tissue and breaking down ECM. In fact, serum level of MMP-8 is a strong predictor of mortality in RA, as this is consistent with increased activation of neutrophils in RA. In addition, MMP-8 has been shown to play a crucial role in cardiovascular diseases by promoting atherosclerotic lesion formation. This is supported by the finding that MMP-8 knockout mice have less endothelial cells or plaque angiogenesis in the atherosclerotic plaques. In a clinical study, it was shown that the ratio of MMP-9/TIMP-1, as well as MMP-8 serum levels, could be a useful predictor of prognosis in patients with hepatocellular carcinomas.

    Molecular Weight

    This 460 amino acid recombinant protein has a predicted molecular mass of approximately 52.6 kDa. The protein migrates at approximately 70 kDa in DTT-reducing conditions and approximately 70 kDa in non-reducing conditions by SDS-PAGE.The predicted N-termi
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