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What is TrypLE used for?

What is TrypLE used for?

Gibco TrypLE reagents are highly purified, recombinant cell-dissociation enzymes that replace porcine trypsin. These reagents are ideal for dissociating attachment-dependent cell lines in both serum-containing and serum-free conditions, and can be directly substituted for trypsin without protocol changes.

What is TrypLE made of?

TrypLE™ Express is a high purity, recombinant fungal enzyme produced by fermentation. It is known to be a serine protease with trypsin-like activity (i.e. it cleaves at the same two amino acid sites–arginine and lysine–as trypsin and has a similar pH activity profile).

Is EDTA a TrypLE?

Unlike porcine trypsin, TrypLE™ Express is free of animal-derived components….This TrypLE™ Express is modified as follows:

With Without
• EDTA • Phenol Red

How do I cancel TrypLE?

The TrypLE enzyme activity is inactivated by dilution using the following procedure: After cell dissociation, transfer the cell suspension to a 15-mL conical tube. Centrifuge at 100 x g for 5-10 min to remove residual enzyme activity.

Does TrypLE need to be neutralized?

TrypLE is easy to use, gentle on cells and we do not have to worry about neutralizing TrypLE – we can leave our cells in it for extended periods of time with no adverse effects on viability. TrypLE is also stable at room temperature, making it very convenient to store and use compared to Trypsin.”

How does trypsin work?

Function. In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides. The peptide products are then further hydrolyzed into amino acids via other proteases, rendering them available for absorption into the blood stream.

What is the difference between TrypLE Express and TrypLE select?

Firstly, the difference between TrypLE Express and TrypLE Select is that Select is manufactured on animal origin free (AOF) machinery. TrypLE Express is also AOF but not manufactured on AOF machinery. Express and Select are both a single recombinant enzyme.

What does trypsin inhibitor do?

A trypsin inhibitor (TI) is a protein and a type of serine protease inhibitor (serpin) that reduces the biological activity of trypsin by controlling the activation and catalytic reactions of proteins.

How does Y-27632 work?

Overview. Y-27632 is a cell-permeable, highly potent and selective inhibitor of Rho-associated, coiled-coil containing protein kinase (ROCK). Y-27632 inhibits both ROCK1 (Ki = 220 nM) and ROCK2 (Ki = 300 nM) by competing with ATP for binding to the catalytic site (Davies et al.; Ishizaki et al.).

How long is Accutase good for?

How long can I store StemPro Accutase at 4°C? A. Once thawed, it is recommended to use it within 2 months. However, the internal stability data suggests stable enzyme activity even after 1 year.

Are trypsin inhibitors bad?

Trypsin inhibitor is present in various foods such as soybeans, grains, cereals and various additional legumes. The main function of trypsin inhibitors in these foods is to act as a defense mechanism. By having this harmful component wild animals learn that any food that contains trypsin inhibitor is a food to avoid.

What is life technology™?

Transformational Technology For Mind Body And Soul. Life Technology™ Are A Leading Pioneer In The Fields Of Alternative / Holistic / Spiritual Healthcare, Vibrational Medicine And Subtle Energy Technology. At Life Technology™ We Look At The Whole Spectrum Of Wellness.

How many employees does Life Technologies have?

The joint sales of the combined companies were about $3.5 billion; they had about 9,500 employees, and owned more than 3,600 licenses and patents. The name “Life Technologies” was an old name from the history of Invitrogen.

Is Life Technologies owned by Fisher Scientific?

In 2013, Thermo Fisher agreed to buy Life Technologies for $13.6 billion. They completed the sale on 3 February 2014, and the Life Technologies brand became part of the Life Sciences Solutions Group of Thermo Fisher Scientific.