TEV Protease
Cat. No.
E027
Unit
100 μl
Price
$49.00
| Cat. No. | E027 | ||||||||
| Name | TEV Protease | ||||||||
| Unit | 100 μl | ||||||||
| Category | Molecular Biology Enzymes and Kits | ||||||||
| Description |
abm’s TEV Protease is an enhanced version of the site-specific protease derived from Tobacco Etch Virus (TEV). This optimized enzyme offers superior activity, stability, and site-specificity compared to the native form. TEV Protease cleaves fusion proteins with high precision at the Gln-Gly or Gln-Ser bond within the seven-amino acid recognition sequence Glu-Asn-Leu-Tyr-Phe-Gln-Gly/Ser (ENLYFQ(G/S)). The enzyme is highly effective across a broad range of temperatures (4–30°C, with an optimum at 30°C) and pH values (5.5–9.0), enabling flexible experimental conditions. Under optimal conditions, up to 99% cleavage can be achieved in just 1–2 hours. Additionally, the inclusion of a 6X-His tag at the N-terminus allows for convenient removal of TEV Protease post-cleavage using Ni-IDA Agarose Beads (Cat. No. G250) via affinity chromatography.
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| Application |
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| Concentration | 10U/ul | ||||||||
| Material Citation | If use of this material results in a scientific publication, please cite the material in the following manner: Applied Biological Materials Inc, Cat. No. E027 |
Datasheet
Search CoA here
MSDS
| Does this enzyme contain a tag? | |
|
Yes, our TEV Protease (E027) contains a His tag.
|
| What is the molecular weight of this product? | |
|
The full molecular weight of E027 is around 28kDa.
|
| What is an Enzyme Unit defined as? | |
|
One unit is defined as the amount of TEV Protease that is required to cleave >90% of 3 µg of control substrate in a 30 µl reaction for 1 hour at 30°C in 1X TEV Protease Reaction Buffer supplemented with 1 mM DTT.
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| What buffer is the enzyme supplied with? | |
|
Enzyme supplied with 20X Reaction Buffer.
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Issaro, N., Kongkaew, A., Jittmittraphap, A., Leaungwutiwong, P., Nimlamool, W., & Takuathung, M. N. (2023). Expression of polyprotein and 3D polymerase protein in Sf9 cells and immunogenicity against enterovirus A71B5 (Thailand strain). Journal of Applied Pharmaceutical Science, 13(9), 027-036. https://dx.doi.org/10.7324/JAPS.2023.93192
Liu, H., Yamaguchi, H., Kikkawa, M., & Shima, T. (2024). Heterogeneous local structures of the microtubule lattice revealed by cryo-ET and non-averaging analysis. bioRxiv, 2024-04. https://doi.org/10.1101/2024.04.30.591984
Mori, S., Nagae, M., & Yamasaki, S. (2024). Crystal structure of the complex of CLEC12A and an antibody that interferes with binding of diverse ligands. International Immunology, 36(6), 279-290. https://doi.org/10.1093/intimm/dxae006
Ogasawara, S., & Yamada, A. (2022). RNA editing with viral RNA-dependent RNA polymerase. ACS Synthetic Biology, 11(1), 46-52. https://doi.org/10.1021/acssynbio.1c00332
Takagi, M., Nagatani, A., Kawano, K., Hata, A., Yokoyama, A., Hayashida, K., ... & Matsuzaki, K. (2024). Stable and Minimum Size Solubilization of Membrane Proteins with Cocktails of Phospholipid Analogues. ACS Applied Materials & Interfaces, 16(46), 63358-63367. https://doi.org/10.1021/acsami.4c15697
Takahasi, K., Onomoto, K., Horiuchi, M., Kato, H., Fujita, T., & Yoneyama, M. (2019). Identification of a new autoinhibitory domain of interferon-beta promoter stimulator-1 (IPS-1) for the tight regulation of oligomerization-driven signal activation. Biochemical and Biophysical Research Communications, 517(4), 662-669. https://doi.org/10.1016/j.bbrc.2019.07.099
Tobita, Y., Hirano, K., Miura, D., Hatano, Y., Tsugawa, W., Ikebukuro, K., ... & Asano, R. (2025). A Versatile Method to Create Antibody/Split‐Enzyme Complexes and Its Application to a Rapid, Homogeneous, and Universal Electrochemical Immunosensing System. Advanced Sensor Research, 4(1), 2400112. https://doi.org/10.1002/adsr.202400112
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rel=\u0022noopener\u0022\u003EG138\u003C\/a\u003E\u003C\/td\u003E\n\u003Ctd style=\u0022text-align: left;\u0022\u003E4,000 U (100 \u0026micro;l)\u003C\/td\u003E\n\u003Ctd class=\u0022product-price\u0022 data-product=\u0022G138\u0022 data-type=\u0022molecular\u0022\u003E$80.00\u003C\/td\u003E\n\u003C\/tr\u003E\n\u003Ctr\u003E\n\u003Ctd style=\u0022text-align: left;\u0022\u003E\u003Ca class=\u0022orange-link\u0022 href=\u0022\/rnaseoff-ribonuclease-inhibitor-g591.html\u0022 rel=\u0022noopener\u0022\u003ERNaseOFF Ribonuclease Inhibitor\u003C\/a\u003E\u003C\/td\u003E\n\u003Ctd style=\u0022text-align: left;\u0022\u003E\u003Ca class=\u0022orange-link\u0022 href=\u0022\/rnaseoff-ribonuclease-inhibitor-g591.html\u0022 rel=\u0022noopener\u0022\u003EG591\u003C\/a\u003E\u003C\/td\u003E\n\u003Ctd style=\u0022text-align: left;\u0022\u003E100,000 U (2 x 1.25 ml)\u003C\/td\u003E\n\u003Ctd class=\u0022product-price\u0022 data-product=\u0022G591\u0022 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01:04:45"},"info":{"id":16615,"cat_no_base":"E027","parent_id":755,"description":"\u003Cp\u003E\u003Cstrong\u003Eabm\u0026rsquo;s TEV Protease\u003C\/strong\u003E is an enhanced version of the site-specific protease derived from \u003Cem\u003ETobacco Etch Virus\u003C\/em\u003E (TEV). This optimized enzyme offers superior \u003Cstrong\u003Eactivity\u003C\/strong\u003E, \u003Cstrong\u003Estability\u003C\/strong\u003E, and \u003Cstrong\u003Esite-specificity\u003C\/strong\u003E compared to the native form. TEV Protease cleaves fusion proteins with high precision at the \u003Cstrong\u003EGln-Gly\u003C\/strong\u003E or \u003Cstrong\u003EGln-Ser\u003C\/strong\u003E bond within the seven-amino acid recognition sequence \u003Cstrong\u003EGlu-Asn-Leu-Tyr-Phe-Gln-Gly\/Ser\u003C\/strong\u003E (ENLYFQ(G\/S)).\u003C\/p\u003E\n\u003Cp\u003EThe enzyme is highly effective across a broad range of temperatures (\u003Cstrong\u003E4\u0026ndash;30\u0026deg;C\u003C\/strong\u003E, with an optimum at \u003Cstrong\u003E30\u0026deg;C\u003C\/strong\u003E) and pH values (\u003Cstrong\u003E5.5\u0026ndash;9.0\u003C\/strong\u003E), enabling flexible experimental conditions. Under optimal conditions, up to \u003Cstrong\u003E99% cleavage\u003C\/strong\u003E can be achieved in just \u003Cstrong\u003E1\u0026ndash;2 hours\u003C\/strong\u003E. Additionally, the inclusion of a \u003Cstrong\u003E6X-His tag\u003C\/strong\u003E at the N-terminus allows for convenient removal of TEV Protease post-cleavage using \u003Cstrong\u003ENi-IDA Agarose Beads\u003C\/strong\u003E (\u003Ca href=\u0022\/ni-ida-agarose-resins-g250.html\u0022\u003ECat. No. G250\u003C\/a\u003E) via affinity chromatography.\u003C\/p\u003E\n\u003Ctable class=\u0022bootstrap-table bootstrap-table-hover abm-service-table abm-perfect-table2\u0022 style=\u0022margin: 30px 0;\u0022\u003E\n\u003Cthead\u003E\n\u003Ctr\u003E\n\u003Cth\u003E\u003Cstrong\u003EProduct Component\u003C\/strong\u003E\u003C\/th\u003E\n\u003Cth\u003E\u003Cstrong\u003EQuantity\u003C\/strong\u003E\u003C\/th\u003E\n\u003C\/tr\u003E\n\u003C\/thead\u003E\n\u003Ctfoot\u003E\n\u003Ctr\u003E\n\u003Ctd\u003ETEV Protease (10 U\/\u0026micro;l)\u003C\/td\u003E\n\u003Ctd\u003E100 \u0026micro;l\u003C\/td\u003E\n\u003C\/tr\u003E\n\u003Ctr\u003E\n\u003Ctd\u003E20X TEV Protease Reaction Buffer\u003C\/td\u003E\n\u003Ctd\u003E1.0 ml\u003C\/td\u003E\n\u003C\/tr\u003E\n\u003Ctr\u003E\n\u003Ctd\u003E100 mM DTT\u003C\/td\u003E\n\u003Ctd\u003E500 \u0026micro;l\u003C\/td\u003E\n\u003C\/tr\u003E\n\u003C\/tfoot\u003E\n\u003C\/table\u003E","disclaimer":null,"application":"\u003Cul\u003E\n\u003Cli\u003ECleavage of tags from recombinant fusion proteins containing a TEV recognition site\u003C\/li\u003E\n\u003Cli\u003EOne step affinity removal of His-tagged TEV after cleavage\u003C\/li\u003E\n\u003C\/ul\u003E","components":null,"cas9_origin":null,"concentration":"10U\/ul","enzymes_size":null,"genecraft_series":null,"guarantee":null,"population":null,"qc":null,"format_general":null,"including_screening_kit":null,"expression_system_general":null,"purity":null,"image":"\/t\/e\/tev-protease-corrected.png","insert_size":null,"shipping_conditions":null,"source_catalog_number":null,"inactivation_protocol":null,"led_viewer_compatibility":null,"unit_definition":null,"vector":null,"reaction_buffer":null,"storage_buffer":null,"caution":null,"storage_condition":null,"product_volume":null,"reporter":null,"safeview_series":null,"source_catno":"abm","stain_color":null,"supplier":"ABM","internal_supplier":null,"internal_note":null,"inventory_location":"Extra Freezer 1","note":null,"recommend":null,"depositor":null,"licensor_name":null,"licensor_contact_information":null,"contract_termination_date":null,"royalty_rates":null,"cas_type":null,"cas_origin":null,"cas_protein_marker":null,"source":null,"endotoxin_level":null,"additional_information":null,"titer":null,"nucleotide_format":null,"protocol_overview":null,"source_price":null,"created_at":"2022-09-09 07:12:40","updated_at":"2025-03-13 20:30:11","short_description":null,"reaction_definition":null,"specificity":null,"promotions":null},"maps":[],"media":[{"id":379474,"parent_id":755,"parent_type":"App\\Models\\CatalogBaseMolecular","file_path":"\/t\/e\/tev-protease-corrected.png","title":null,"text":null,"file_type":"image","alt":null,"url":null,"position":1,"status":0,"entity_id_m2":18084831,"sku_in_m2":"E027","value_id_m2":49910076,"attribute_id":90,"created_at":"2022-07-19 04:36:22","updated_at":"2023-04-10 05:39:28"}],"gene":null}