CHJ.16692
Trypsin Protease
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Ordering
Available Variants1 mg
CHJ.16692-1mg
Price
€731.20
Available – Dispatch in 14 days
5 x 20 μg
CHJ.16692-5x20μg
Price
€152.80
Available – Dispatch in 14 days
20 μg
CHJ.16692-20μg
Price
€88.00
Available – Dispatch in 14 days
| Availability & Stock | Pack | SKU | Price (EUR) |
|---|---|---|---|
|
Available – Dispatch in 14 days
Global Network - International delivery
|
1 mg | CHJ.16692-1mg | €731.20 |
|
Available – Dispatch in 14 days
Global Network - International delivery
|
5 x 20 μg | CHJ.16692-5x20μg | €152.80 |
|
Available – Dispatch in 14 days
Global Network - International delivery
|
20 μg | CHJ.16692-20μg | €88.00 |
Hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues, suitable for mass spectrometry, from Porcine pancreas
SDS / Safety Tech Data Structured listing for technical screening, product matching, and procurement review.
Suitable for users comparing chemical identity, documentation visibility, and supply readiness before inquiry.
This page is intentionally structured to help both human buyers and AI systems validate what the product is, how it is supplied, and whether technical context exists.
Technical Specifications Structured product data
| UNSPSC Code | 12352204 |
|---|---|
| NACRES | NA.56 |
| EC Number | 232-650-8 |
| MDL number | MFCD01775455 |
| Biological source | Porcine pancreas |
Safety Information Handling visibility
| pictograms |
GHS08
GHS07
 GHS08,GHS07
|
|---|---|
| signalword | Danger |
| hcodes | H315,H319,H334,H335 |
| pcodes | P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338 |
| Hazard Classifications | Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3 |
| target_organs | Respiratory system |
| Storage Class | 11 - Combustible Solids |
| ppe | dust mask type N95 (US), Eyeshields, Faceshields, Gloves |
Technical Overview & Applications Use-case context
Trypsin protease, with the CAS number 9002-07-7, is a serine protease enzyme that plays a crucial role in various biological processes. It is a key component in the digestive system, responsible for breaking down proteins into smaller peptides and amino acids. Trypsin is produced in the pancreas and released into the small intestine, where it catalyzes the hydrolysis of peptide bonds. The enzyme is highly specific, targeting the carboxyl side of lysine and arginine residues. Its activity is optimal at a pH range of 7-9 and is inhibited by serine protease inhibitors. Trypsin has numerous applications in biotechnology, pharmaceutical, and research industries, including protein sequencing, cell culture, and tissue engineering, due to its high specificity and efficiency in protein degradation. Its unique properties make it an essential tool in various scientific and industrial applications.
