Anti-MMP-9 (Active) Antibody, clone 4A3

Stable for 1 year at 2-8°C from date of receipt.

Control
Active form of MMP-9

Evaluated by Western Blot with the active form of MMP-9.

Western Blot Analysis: A 1:250 dilution from a reprsentative lot detected the active form of MMP-9 in WB.

Research Category
Cell Structure

Research Sub Category
MMPs & TIMPs

This Anti-MMP-9 (Active) Antibody, clone 4A3 is validated for use in Western Blotting, IHC for the detection of MMP-9 (Active).

Western Blot Analysis: A representative lot from an independent laboratory detected the active form of MMP-9 in WB (Duncan, M. E., et al. 1998. Eur J Biochem. 258(1):37-43).

Immunohistochemistry Analysis: A representative lot from an independent laboratory detected the active form of MMP-9 in oesophageal cancer tissues (Duncan, M. E., et al. 1998. Eur J Biochem. 258(1):37-43).

This antibody recognizes the N-terminus of MMP-9 (Active).

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Matrix metalloproteinase 9 (MMP-9), a member of the peptidase M10A family, is a multidomain zinc metalloproteinase enzyme, which is highly expressed in neurons and glia of the hippocampus, cerebral cortex, and cerebellum. The active MMP-9 is formed upon cell stimulation by enzymatic cleavage of the precursor, proMMP-9. Because of its function in tissue degradation, MMP-9 is tightly regulated by multiple mechanisms, including glycosylation, inhibition by TIMP1, internalization, and sequestration. MMP-9 plays an important role in long-term potentiation, synaptic plasticity, and memory. Several studies have reported an increase in levels of MMP-9 after CNS injury, as well during the development of various cancers.

~67 kDa observed. Under reducing conditions in SDS-PAGE, MMP-9 monomer (proenzyme) is observed as a major band at ~ 92 kDa Activation of MMP-9 proenzyme with trypsin yields different active forms at ~64, ~67, and ~82 kDa in a time dependent manner (Duncan, M. E., et al. 1998. Eur J Biochem. 258(1):37-43).

Epitope: N-terminus

Ovalbumin-conjugated linear peptide corresponding to the N-terminus of human MMP-9 (Active).

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.