Anti-Human MMP-8 – Biotin

Purified Recombinant Human MMP-8 (Accession # AAZ38714)

This biotinylated 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 50 µg of bovine serum albumin per µg of antibody with no calcium, magnesium, or preservatives present.

Lyophilized

The lyophilized, biotinylated antigen affinity purified polyclonal antibody can be stored desiccated at -20°C to -70°C for up to twelve months from date of receipt. The reconstituted bioin conjugate can be stored for at least four weeks at 2-8°C. For long-term storage of the reconstituted conjugate, 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.

Next Day Ambient

IHC (NBF/Par.): This antibody should give satisfactory staining results when used at a concentration of 5-15 µg/ml. The recommended secondary antibody for IHC is PN:A106. For chromogenic detection with high signal and low background use PN:D100 or PN:K107.

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