| Species : |
Streptomyces mobaraensis |
| Source : |
E.coli |
| Description : |
Transglutaminases are a family of enzymes (EC 2.3.2.13) that catalyze the formation of a covalent bond between a free amine group of protein- or peptide-bound lysine (acyl acceptors) and the gamma-carboxamide group of protein- or peptide-bound glutamine (acyl donors). |
| Form : |
White lyophilized solid |
| Bio-activity : |
> 30 U/mg |
| Molecular Mass : |
38334.0 Da |
| Endotoxin : |
< 0.004 EU/U |
| Purity : |
> 98% |
| Applications : |
Labeling, immobilisation, conjugation, and modification of proteins. |
| Notes : |
INTENDED FOR RESEARCH USE ONLY, NOT FOR USE IN HUMAN, THERAPEUTIC OR DIAGNOSTIC APPLICATIONS. |
| Storage : |
Store at -80 centigrade. Upon reconstitution, store working aliquots undiluted.
If storage at -80 centigrade is not possible, storage at ≤ -20 centigrade is recommended. |
| Concentration : |
9-11 mg/mL |
| Storage Buffer : |
The purified transglutaminase is lyophilized from 50 mM HEPES pH 7.4. |
| Reconstitution : |
Add the volume of H2O the protein is lyophilized from (see Certificate of Analysis) to the vial of lyophilized powder. Rotate vial gently until solid dissolves. |
