Anti-Mouse MMP-9 – Biotin

Purified Recombinant Mouse MMP-9 (Accession # P41245)

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 biotin 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 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.
Immunocytochemistry: Suitable for use at concentration of 5-15 µg/mL.

Goat Anti-Mouse matrix metalloproteinase 9 (MMP-9) recognizes Mouse MMP-9. 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 9, also known as MMP9, is a biological enzyme that is a member of the matrix metalloproteinases (MMPs). MMP9 is thought to play a critical role in tumor cell invasion,¹ 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-9 is secreted from cells and, once activated, is thought to degrade collagen in the extracellular matrix.² MMP-9 is one of the major proteases produced by osteoclasts and possibly plays a role in osteoclastic bone resorption.³

1. Viswanadha, VP. et al. (2017) J Cell Biochem. 118(9):2865-2876.
2. Mobashery, S. et al. (1995) Cancer Res. 55: 2548
3. Tökés, ZA.et al. (1995) J Neurochem. 64: 1312
4. Kumegawa, M. et al. (1994) J Biol. Chem. 269: 15006