Neutral Protease Background

Neutral protease was first crystallized and characterized in the 1950s from Bacillus subtilis, initially thought to be an extracellular product[1].

In 1993, researchers compared 16S rRNA gene sequences and defined a new genus named Paenibacillus, to which the former Bacillus polymyxa now belongs[1].

The enzyme is a non-specific metalloprotease that can cleave fibronectin, collagen IV, and to a lesser extent collagen I[1].

It is unique among Bacillus species as Paenibacillus polymyxa is one of three species that produces only a neutral protease[1].

Neutral Protease Systemic Applications

Neutral protease demonstrates remarkable versatility in systemic applications, particularly in cell and tissue research.

It is extensively used in tissue disaggregation, cell isolation, and subcultivation processes[1][2].

The enzyme has mild proteolytic action, making it especially suitable for preparing primary cells and secondary cell cultures without damaging cell membranes[2].

Its applications span various fields, including cell culture, tissue dissociation, and preparation of cells for research[1][2].

Neutral Protease for Brain and Cognition

While the search results do not provide specific information on neutral protease's direct effects on brain and cognition, its role in cellular processes suggests potential research applications.

The enzyme's ability to gently dissociate cells could be valuable in neurological research and cell studies[1][2].

Neutral Protease for Eye and Vision

Neutral protease has shown potential applications in ocular research, particularly in tissue dissociation and cell isolation[3][6].

Recent studies have explored protease inhibitors in treating ocular conditions like dry eye syndrome, suggesting the broader importance of proteases in eye health[3][6].

Research indicates that proteases play a role in molecular remodeling and may have potential therapeutic effects in neovascularization and inflammation[3].

Relevant quotes:

"Neutral protease is a non-specific metalloprotease. It cleaves fibronectin, collagen IV, and to a lesser extent collagen I" - Worthington Enzyme Manual[1]

Relevant NCBI article quotes:

"Recently, researchers have even hypothesized a possible therapeutic effect of protease-inhibitors in topical and systemic treatment of neovascularization and inflammation" - Role of Protease-Inhibitors in Ocular Diseases[3]

Functions supported or stimulated:

1. Tissue disaggregation

2. Cell isolation

3. Protein cleavage

4. Cellular research support

5. Tissue dissociation

Related benefits:

1. Gentle cell manipulation

2. Research applications

3. Potential therapeutic research

4. Tissue preparation

5. Cell culture advancement

Source Information:

Bacterial source: Paenibacillus polymyxa (formerly Bacillus polymyxa)[1]

Common names:

1. Neutral Protease

2. Dispase

3. Bacterial Neutral Protease

Citations:

[1] https://www.worthington-biochem.com/products/neutral-protease-dispase/manual

[2] https://www.worthington-biochem.com/products/neutral-protease-dispase

[3] https://pmc.ncbi.nlm.nih.gov/articles/PMC6271012/

[4] https://pmc.ncbi.nlm.nih.gov/articles/PMC6364759/

[5] https://cellsystems.eu/product/npro-dispase-neutr-protease-purified/

[6] https://www.nature.com/articles/s41598-020-74159-w

[7] https://pmc.ncbi.nlm.nih.gov/articles/PMC2974563/

[8] https://pmc.ncbi.nlm.nih.gov/articles/PMC3031458/

[9] https://pmc.ncbi.nlm.nih.gov/articles/PMC9456293/