Recombinant EN-TEV Protease (mutated S219N) protein (Tagged-His Tag)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant EN-TEV Protease (mutated S219N) protein (Tagged-His Tag) is a Tobacco etch virus Full Length protein, in the 2037 to 2073 aa range, expressed in Escherichia coli, with >98%, suitable for SDS-PAGE, FuncS.
View Alternative Names
Genome polyprotein
- FuncS
Unknown
Functional Studies - Recombinant EN-TEV Protease (mutated S219N) protein (Tagged-His Tag) (AB134877)
4-12% SDS-PAGE gel. M : Protein Marker
Lane 1 : N‐terminal tag HBxAg‐11R protein before TEV enzyme digestion.
Lane 2 : N‐terminal tag HBxAg‐11R protein digested using 1/50 dilution (1µg TEV/ 50µg target protein at 4°C for overnight reaction) in buffer 20 mM Tris‐HCl, pH 8.0, 100 mM KCl.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The action of TEV protease involves recognizing and cleaving a specific sequence in fusion proteins allowing for the removal of affinity tags. Though not generally part of a complex its activity is often important for modifying proteins without interfering with their structure or function beyond the cleaved site. By providing a method to separate desired parts of proteins TEV protease enhances the study of protein functions and structures. It also assists in generating authentic recombinant proteins critical for various research applications.
Pathways
TEV protease's role mainly revolves around its function in post-translational modification processes rather than classical signaling pathways. It facilitates pathways where the removal of fusion tags is necessary for studying protein interactions and conformations. This function does not directly involve TEV protease in cellular metabolic pathways but its activity complements the activity of other proteases like Actev protease and protease assay protocol tools by providing a precise cleavage mechanism necessary for subsequent biochemical analysis and studies.
Specifications
Form
Liquid
Additional notes
ab134877 is sterile-filtered.
General info
Function
Helper component proteinase. Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus (PubMed : 2656254). Interacts with virions and aphid stylets (PubMed : 9880030). Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs (PubMed : 11414807). May have RNA-binding activity.. Cytoplasmic inclusion protein. Has helicase activity. It may be involved in replication.. 6 kDa protein 1. Indispensable for virus replication (By similarity). Reduces the abundance of host transcripts related to jasmonic acid biosynthesis therefore altering the host defenses (By similarity). In order to increase its own stability, decreases host protein degradation pathways (By similarity).. 6 kDa protein 2. Indispensable for virus replication.. Viral genome-linked protein. Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (Probable). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity).. Nuclear inclusion protein A. Has RNA-binding and proteolytic activities.. Nuclear inclusion protein B. An RNA-dependent RNA polymerase that plays an essential role in the virus replication.. Capsid protein. Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
Sequence similarities
Belongs to the potyviridae genome polyprotein family.
Post-translational modifications
Viral genome-linked protein. VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).. Genome polyprotein. Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).
Target data
Additional targets
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com