CHJ.52426
Trypsin from bovine pancreas
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Ordering
Available Variants50 mg
CHJ.52426-50mg
Price
€82.40
Available – Dispatch in 14 days
100 mg
CHJ.52426-100mg
Price
€155.20
Available – Dispatch in 14 days
| Availability & Stock | Pack | SKU | Price (EUR) |
|---|---|---|---|
|
Available – Dispatch in 14 days
Global Network - International delivery
|
50 mg | CHJ.52426-50mg | €82.40 |
|
Available – Dispatch in 14 days
Global Network - International delivery
|
100 mg | CHJ.52426-100mg | €155.20 |
TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein
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
| CAS Number | 9002-07-7 |
|---|---|
| UNSPSC Code | 12352204 |
| NACRES | NA.54 |
| EC Number | 232-650-8 |
| MDL number | MFCD00082094 |
| Specific activity | ≥10,000 BAEE units/mg protein |
| Biological source | bovine 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 |
| wgk | WGK 1 |
| ppe | dust mask type N95 (US), Eyeshields, Faceshields, Gloves |
Technical Overview & Applications Use-case context
Trypsin from bovine pancreas, with a CAS number of 9002-07-7, is a serine protease enzyme that plays a crucial role in the digestive process of mammals. It is produced in the pancreas and secreted into the small intestine, where it hydrolyzes proteins into smaller peptides and amino acids. The enzyme is highly specific, cleaving peptide chains at the carboxyl side of lysine and arginine residues. Trypsin from bovine pancreas has been extensively used in various biochemical and biotechnological applications, including protein sequencing, peptide synthesis, and cell culture. Its high specificity and activity make it a valuable tool in research and industrial settings, and its availability in highly purified forms has facilitated its widespread adoption in many fields of study. The enzymes stability and activity are influenced by factors such as pH, temperature, and ionic strength.
