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Trypsin, 1 g

≥2500 USP-U/mg, cryst.
Examples of effect: Lead to damage to heath, cause irritation to eyes, skin or respiratory organs. Are fatal in larger quantities. Safety: As previously stated, in the event of skin irritation or contact with eyes, rinse with water or a suitable medium.
Examples of effect: Have an allergenic effect, carcinogenic, mutagenic, toxic to reproduction and cause developmental toxicity (reprotoxic) or damage to organs Safety: You must be well-informed before starting work with these substances; wear protective clothing and gloves, eye protection and mask or breathing protection.
Danger
H315-H319-H334-H335
i causes skin irritation, causes serious eye irritation, may cause allergy or asthma symptoms or breathing difficulties if inhaled, may cause respiratory irritation
P280 P302+P352 P304+P341 P305+P351+P338 P342+P311
i wear protective gloves/eye protection/face protection, IF ON SKIN: Wash with plenty of soap and water, IF INHALED: If breathing is difficult, remove victim to fresh air and keep at rest in a position comfortable for breathing, IF IN EYES: Rinse cautiously with water for several minutes. Remove contact lenses, if present and easy to do. Continue rinsing, if experiencing respiratory symptoms: Call a POISON CENTER/doctor
Pack Qty.
Pack.
Molar mass (M) ~24,000 g/mol
Storage temp. -20 °C
Transport temp. ambient temp.
WGK 1
CAS No. [9002-07-7]
EG-Nr. 232-650-8

Isolated from porcine pancreas, lyophilised.

A pancreatic serine protease with a specificity for peptide bonds between basic amino acids arginine or lysine and another non-specific amino acid.

Trypsin is frequently used to suspend cells which grow as monolayers on surfaces. Longer exposure to trypsin can damage cells, so that an inhibitor (serum or trypsin inhibitor from soya beans) should be added upon completion.
Product details

€114.50/Pack Qty. 

excl. VAT. | 1 g per Pack Qty.

Art. No. 5455.2

In procurement
from 6 Pack Qty. €108.78/Pack Qty.
from 24 Pack Qty. €103.05/Pack Qty.
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Product details


A pancreatic serine protease with a specificity for peptide bonds between basic amino acids arginine or lysine and another non-specific amino acid.

Trypsin is frequently used to suspend cells which grow as monolayers on surfaces. Longer exposure to trypsin can damage cells, so that an inhibitor (serum or trypsin inhibitor from soya beans) should be added upon completion.


Unit definition

One USP Unit will cause an increase in absorption (253 nm) per minute of 0.003 at 25 °C and pH 7.6 using BAEE as substrate.
One (international) Unit (U, 255 nm, BAEE, pH 8) is approx. 90 USP U.
One TAME Unit is approx. 20 USP Units.
One NF Unit is one USP Unit.
Ten „BAEE Units“ are approx. 3.3 USP Units.


Directions for use

pH optimum 7.2-8.5



Trypsin ≥2500 USP-U/mg, cryst.

Trypsin
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Order No. Pack Qty. Pack. Price Quantity
5455.1 100 mg glass

€27.45

5455.2 1 g glass

€114.50

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Downloads / MSDS


General information

Enzyme: a neoclassical, Greek artificial word ενζυμου, énzymon, derived from εν-, en- (in-) and ζυμη, zýmé (yeast, sourdough, archaic)
Ferments: comes from the Latin fermentum (ferments, sourdough)

There are six classes in which all enzymes are classified according to the particular reaction they catalyse:

Oxidoreductases (catalyse redox reactions)

Transferases (transfer functional groups among substrates)

Hydrolases (cleave bonds via addition of water)

Lyases/Synthases (cleave or synthesise complex products out of basic substrates without cleavage of ATP)

Isomerases (transform chemical isomers)

Ligases/Synthetases (cleave or synthesise complex products out of basic substrates via cleavage of ATP)


Certificates of Analysis

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The following analysis certificates have been found:

Type analysis

Appearancebeige to light brown hygroscopic powder
Activity≥2500 USP-U/mg Trypsin
Residue on ignition≤3,0 %
Loss on drying (60 °C)<5 %

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