Anti-Human MMP-8

NS0-Derived Recombinant Human MMP-8

This antigen affinity purified polyclonal antibody has been 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 containing 5.0% w/v trehalose with no calcium, magnesium, or preservatives present.

Lyophilized

The lyophilized antigen affinity purified polyclonal antibody can be stored desiccated at -20°C to -70°C for twelve months from date of receipt. The reconstituted antibody can be stored for at least four weeks at 2-8°C. For long-term storage of the reconstituted antibody, aseptically aliquot into working volumes and store at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. No detectable loss of activity was observed after six months.

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Immunoprecipitation: The antibody has been used to immunoprecipitate rhMMP-8 from conditioned media of transfected NS0 cells. The recovered rhMMP-8 can be detected by western blot analysis using a mouse monoclonal antibody.
Immunocytochemistry: The antibodies have been used at 5 μg/mL and 15 μg/mL to detect human MMP-8 in transfected cells.
Immunohistochemistry: Suitable for use at concentration of 5-15 µg/mL.

Goat Anti-Human Matrix Metalloproteinase-8 (MMP-8) recognizes Human MMP-8. This antigen affinity purified polyclonal antibody was purified using a proprietary chromatographic technique that includes covalently immobilizing the antigen proteins or peptides to agarose based beads. This purification method enhances specificity, reduces nonspecific binding of extraneous IgG and provides you with the most reliable reagent available for your early discovery research.

Matrix metallopeptidase 8 (neutrophil collagenase), also known as MMP8, is a part of the MMP family which are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by MMP8 is stored in secondary granules within neutrophils and is activated by autolytic cleavage. MMP8 is a neutral metalloproteinase of the fibrillar collagenase family that also includes MMP-1 and MMP-13. In contrast to the other collagenases, MMP-8 has a very limited tissue distribution, thought to be restricted to neutrophils and chondrocytes.¹ Its function is degradation of type I, II and III collagens. MMP-8 is the predominant collagenase present in normal healing wounds and suggests that overexpression and activation of this collagenase may be involved in the pathogenesis of nonhealing chronic ulcers.² MMP-8 might also be useful in monitoring periodontal disease in diabetes.³

1. Klebe, RJ. et al. (2001) Matrix Biol. 20: 577
2. Yager, DR. et al. (1999) J Surg Res. 81: 189
3. Uusitupa, M. et al. (2000) J Periodontal Res. 35: 259