Anti-Human MMP-13

NS0 - Derived Human MMP-13

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: This antibody has been used to immunoprecipitate recombinant human MMP-13 from conditioned media of transfected NS0 myeloma cells. The recovered recombinant human MMP-13 can be detected by Western blot analysis using monoclonal antibodies.
Immunocytochemistry: This antibody can be used at 5-15 μg/ml to detect human MMP-13 in 10-15 μm thick paraffin-embedded tissue sections.

Goat Anti-Human Matrix Metalloproteinase-13 (MMP-13) recognizes Human MMP-13. 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 13 (collagenase 3), also known as MMP13, is a glycosylated protein¹ and a member of the matrix metalloproteinase (MMP) family of neutral endopeptidases, which is expressed in the skeleton during embryonic development² and 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. MMP-13 is tightly bound to tissues and utilizes heparan sulfate proteoglycans as extracellular docking molecules. It is produced by many different cell types as an inactive proform that requires proteolytic activation to gain activity.³ Mutations causing lack of MMP-13 expression have been shown to be associated with skeletal disorders characterized by defective growth and modeling of the spine and long bones (spondyloepimetaphyseal dysplasias).⁴

1. Knäuper, V. et al. (1996) J Biol. Chem. 271: 17124
2. Krane, SM. et al. (2004) National Acad. Scien.
3. Woessner, JF. et al. (2000) J Biol. Chem. 275: 4183
4. Kennedy, AM. et al. (2005) J Clin. Invest. 115: 2832