| Description : |
rTrypsin 3.0 is a recombinant protease that specifically hydrolyzes peptide bonds at the carboxyl side of lysine and arginine residues. Engineered with a redesigned gene sequence and methylated lysines, it offers ultra-fast protein hydrolysis, high activity, and no self-degradation. rTrypsin 3.0 is ideal for protein characterization, single-cell proteomics, and large cohort proteomics studies. |
| Form : |
Lyophilized powder with 20 μg Trehalose. |
| Bio-activity : |
15,000 units/mg |
| Molecular Mass : |
23.7 kDa |
| Purity : |
> 99.0 % based on trypsin peak area, analyzed by HPLC at 280 nm. |
| Storage : |
Store the lyophilized powder at -20 centigrade, store reconstituted enzyme at -80 centigrade. |
| CAS No. : |
9002-07-7 |
| Shelf life : |
24 months at -20 centigrade |
| Stability : |
rTrypsin 3.0 is maximally active in the pH range of 7-9 |
| Usage Notes : |
1. Suitable enzyme digestion buffers: 20 mmol Tris, 50 mmol ABC, or HEPES buffer; pH 7-9.
2. Use a 1:50 protease-to-protein ratio with a protein concentration of 0.5 μg/μL. Incubate at 37 centigrade in a dry bath for 30 minutes. |
| Specificity : |
Secukinumab antibody protein sample analyzed by ESI-MS/MS, showing > 99.8 % specificity at K and R cleavage sites. |
| Unit Definition : |
At pH 7.8 and 25 centigrade, 1.0 μmol of BAEE protein is hydrolyzed per minute at 253 nm. |
| LC-MS/MS Analysis : |
Secukinumab antibody protein was denatured, reduced, and alkylated with BT57 reagent at 60 centigrade, pH 8.0, followed by incubation at 45 centigrade for 30 minutes and HPLC-MS/MS analysis. The heavy chain showed 70 % coverage (1 missed cleavage), while the light chain had 100 % coverage. |
| Resuspension Buffer : |
Dissolved in 40 μL of 50 mmol acetic acid, concentration 0.5 μg/μL. |
