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| Product Name | Recombinant Enterokinase Light Chain with Removable Polyhistidine Tag (5 U/uL) |
| Catalog No. | IVDRM-0292 |
| Description | Enterokinase is prized for one thing: it cuts at a five-residue sequence that rarely appears by chance, so a fusion partner can be removed while leaving the target polypeptide untouched. This preparation is the light chain of the bovine enzyme, identical in sequence to the natural catalytic fragment but produced recombinantly, which means higher specific activity and no risk of contamination from animal material. It cleaves across a wide window from pH 4.5 to 9.5 and across a broad temperature range, and keeps partial activity even when detergents or denaturants are present in the reaction. A polyhistidine tag sits at the C-terminus, so once digestion is finished the enzyme itself is pulled out of the mixture with immobilised nickel, shortening the purification train considerably. |
| Intended Use | Removal of affinity tags from the N-terminus of recombinant fusion proteins, leaving the correct N-terminal sequence intact, and general processing of fusion constructs in research and preparative work. |
| Principle / Technology | The enzyme recognises the sequence Asp-Asp-Asp-Asp-Lys and hydrolyses the peptide bond on the carboxyl side of the lysine residue, so a tag joined to the target through that linker is released cleanly. |
| Sample Type | Purified or partially purified fusion protein carrying an enterokinase recognition site. |
| Performance Range / Specifications | Identical sequence to the native bovine light chain with higher cleavage activity; no contaminating protease activity and no non-specific cutting; works between pH 4.5 and 9.5 and over a wide temperature span; retains partial activity with detergents and denaturants; C-terminal polyhistidine tag allows removal on nickel affinity resin. |
| Specificity | Supplied at 5 U/uL; apparent molecular weight about 40 kDa by SDS-PAGE against a theoretical 22.7 kDa owing to glycosylation; purity at least 95%; raised in Komagataella phaffii (Pichia pastoris); activates across pH 4.5 to 9.5. |
| Reaction Conditions / Protocol | Dilute the fusion protein into a buffer containing 20 mM Tris-HCl, 50 mM sodium chloride and 2 mM calcium chloride at pH 8.0, add the calculated volume of enzyme, incubate at 25 °C for 12 to 16 hours, then pass the digest over immobilised nickel to remove the tagged enzyme. |
| Components / Formulation | Bottled enzyme solution at 5 U/uL; offered in 100 U, 500 U, 5000 U, 100 KU and 1 MU (1000 KU) quantities. |
| Storage Conditions | Store at -25 to -15 °C. |
| Shelf Life | 2 years from receipt when held at the recommended temperature. |
| Package Specifications | Supplied as liquid enzyme in volumes matched to 100 U, 500 U, 5000 U, 100 KU or 1 MU (1000 KU). |
| Product Form | Sterile liquid in a glycerol-containing protein storage solution. |
| Quality Control | Released at not less than 95% purity with identity confirmed by molecular weight and absence of other proteolytic activity verified. |
| Key Features | - Cuts only after Asp-Asp-Asp-Asp-Lys, giving clean N-terminal processing - Sequence matches the native bovine light chain with higher activity - No detectable contaminating protease or non-specific cutting - Active from pH 4.5 to 9.5 and over a broad temperature range - Polyhistidine tag lets the enzyme be removed on nickel resin after digestion |
| Purity | At least 95%. |
| Concentration | 5 U/uL. |
| Activity / Unit Definition | One unit cleaves 95% of 50 ug of a fusion substrate of about 64.6 kDa bearing the recognition site during 12 to 16 hours at 25 °C in 20 mM Tris-HCl, 50 mM sodium chloride, 2 mM calcium chloride at pH 8.0. |
| Molecular Weight | Theoretical 22.7 kDa; apparent roughly 40 kDa on SDS-PAGE because of glycosylation. |
| Source / Origin | Recombinantly expressed in Komagataella phaffii; no animal-derived raw material is used. |
| pH Range / Optimal pH | Supplied in 50 mM Tris-HCl, 250 mM sodium chloride, 2 mM calcium chloride and 50% glycerol at pH 8.0. |
| Shipping Conditions | Shipped cold. |
| Expiration Date / Stability | Stable across the stated shelf life when held at the recommended temperature and kept sealed. |
| Regulatory / Compliance | Restricted to research applications; not for clinical use. |
| Compatibility | Tolerates detergents and denaturants with partial activity retained and works in nickel affinity purification workflows through its polyhistidine tag. |
| Recommended Buffer System | Storage solution of 50 mM Tris-HCl, 250 mM sodium chloride, 2 mM calcium chloride, 50% glycerol at pH 8.0; digestion recommended in the lower-salt buffer above. |
| Application Notes / Precautions | Scaling from small substrates does not follow a simple ratio, because smaller proteins are cut more efficiently; the stated unit value is defined against a large substrate, so expect higher apparent activity on oligopeptides. |
| Batch-to-Batch Consistency | Each production lot is released against fixed acceptance criteria so performance stays consistent between orders. |
| Model Type | Site-specific fusion tag protease |
| Starting Material / Tissue Site | Recombinant catalytic light chain expressed in Komagataella phaffii |
| Delivery Standard | Liquid enzyme in vials matched to the ordered activity unit |
| Turnaround Time | No lead time is published on the product page; availability is confirmed when the order is placed. |
| Readouts / Downstream Assays | Extent of tag removal judged by SDS-PAGE shift or mass difference of the target protein. |
For in vitro diagnostic use.
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