SAE0147
Thrombin protease, biotin-tagged
human recombinant,expressed in HEK 293 cells, ≥5000 units/mL
Synonym(e):
Factor IIa, fibrinogenase, thrombase
About This Item
Biologische Quelle
human
Rekombinant
expressed in HEK 293 cells
Konzentration
≥5000 units/mL
Methode(n)
protein extraction: suitable
Eignung
suitable for additive or modifier in the separation of proteins or peptides
Anwendung(en)
life science and biopharma
Versandbedingung
dry ice
Lagertemp.
−20°C
Allgemeine Beschreibung
The optimal cleavage sites for thrombin are as follows:
1. A-B-Pro-Arg-||-X-Y, where A and B are hydrophobic amino acids, and X and Y are nonacidic amino acids.
2. Gly-Arg-||-Gly
Recombinant human thrombin protease is expressed in human HEK 293 cells as a glycoprotein heterodimer. The DTT-reduced protein migrates as two bands of ∼31 kDa (heavy chain) and ∼6 kDa (light chain) on SDS-PAGE. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher activity of the protein.
This thrombin protease is useful for cleaving recombinant proteins that are expressed as fusion proteins with this sequence between the carrier domain and the protein of interest.
Anwendung
This method is advantageous over post-elution cleavage for several reasons:
- It eliminates most impurities normally associated with purification on Ni-chelating columns.
- It allows gentler elution conditions, with added flexibility in the elution buffer composition. This can mitigate protein aggregation and inactivation.
Leistungsmerkmale und Vorteile
Catalytic pH range:11.5–10
Optimal pH:11-8.3
(Note: thrombin precipitates at pH ≤5)
Molecular mass:4,12 37.4 kDa
Human isozymes pI range:6.35–7.6
E280 (1%):12 -18.3
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 1
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