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hrv 3c protease cleavage  (TaKaRa)


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    TaKaRa hrv 3c protease cleavage
    Hrv 3c Protease Cleavage, supplied by TaKaRa, used in various techniques. Bioz Stars score: 95/100, based on 176 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hrv+3c+protease/HRV+3C+Protease/10__1016_slash_j__cellin__2026__100367-270-8-12
    Average 95 stars, based on 176 article reviews
    hrv 3c protease cleavage - by Bioz Stars, 2026-11
    95/100 stars

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    Related Articles

    Incubation:

    Article Title: A CRISPR/Cas9-based genome-editing platform enabling efficient and precise gene replacement in Lipomyces starkeyi.
    Article Snippet: .. The eluate containing His-GST-Cas9SV40 was incubated with HRV 3C protease (10 U per 1 mg protein; Takara Bio) at 4°C for 16 h to cleave the His-GST tag. .. Then, Ni-NTA agarose (QIAGEN, Hilden, Germany) was added, and the mixture was incubated at room temperature for 30 min. After centrifugation (500 × g, 10 min), the His-GST tag was retained by the resin, and the flow-through containing recombinant Cas9SV40 was collected.

    Immunoprecipitation:

    Article Title: Mechanisms of HSV-1 helicase–primase inhibition and replication fork complex assembly
    Article Snippet: The supernatant was incubated with amylose resin (NEB Cat# E8021S) at 4 °C for 1 h and washed with wash buffer (25 mM HEPES-NaOH, pH 7.5, 300 mM NaCl, 5 mM MgCl 2 , 0.5 mM EDTA, and 1 mM DTT). .. Immunoprecipitated HSV H/P complex was subjected to on-column digestion overnight with HRV-3C protease (TaKaRa Cat# 7360). .. The eluate fractions within the elution buffer (25 mM HEPES-NaOH, pH 7.5, 150 mM NaCl, 2 mM MgCl 2 and 1 mM DTT) were concentrated at 1.1 mg ml -1 for further purification using a Superdex 200 Increase (Cytiva Cat# 28990944) SEC column.

    Purification:

    Article Title: A therapeutic multi-epitope protein vaccine targeting HPV16 E6 E7 elicits potent tumor regression and cytotoxic immune responses.
    Article Snippet: The protein was then purified using an His-tag protein purification kit (P2229S; Beyotime, Shanghai, China) according to the manufacturer’s instructions, yielding a protein with the TF tag. .. The TF tag was subsequently removed by HRV 3C protease (7360; TAKARA, Shiga, Japan) cleavage and purified using BeyoGold His-tag Purification Resin (P2233; Beyotime). ..

    Article Title: Olfactory recognition of peanut-derived volatiles mediated by odorant-binding protein PintGOBP2 in Plodia interpunctella
    Article Snippet: Understanding the olfactory recognition mechanisms underlying peanut-derived volatile organic compounds (VOCs) that mediate oviposition preference in Plodia interpunctella is essential for developing attractant-based pest control strategies.. We identified a general odorant-binding protein gene, PintGOBP2, highly expressed in female antennae.. It was expressed in a prokaryotic system, and fluorescence competitive binding assays with 15 peanut-derived VOCs revealed the strong binding affinities to octanal, 1-octen-3-ol, and acetophenone.

    Recombinant:

    Article Title: Metabolism of L-threonate, an ascorbate degradation product, requires a protein with L-threonate metabolizing domains in Arabidopsis
    Article Snippet: Recombinant proteins were purified using a TALON Metal Affinity Resin column (Clontech) and concentrated using a 30-kDa cutoff ultrafiltration device (Amicon Ultra-4, Millipore). .. We attempted to cleave the TF tag from the recombinant protein using HRV 3C Protease (Takara); however, the tag could not be separated from the target protein, likely due to incomplete cleavage or tight association with the protein. ..



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    ( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). <t>Unmodeled</t> <t>N-terminal</t> extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.
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    ( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). <t>Unmodeled</t> <t>N-terminal</t> extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.
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    ( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). <t>Unmodeled</t> <t>N-terminal</t> extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.
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    Image Search Results


    ( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). Unmodeled N-terminal extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.

    Journal: bioRxiv

    Article Title: Conserved assembly architecture of the essential herpesvirus packaging accessory factor

    doi: 10.64898/2026.01.22.701024

    Figure Lengend Snippet: ( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). Unmodeled N-terminal extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.

    Article Snippet: The coding region of UL52 was subcloned from a pcDNA4/TO-2xStrep vector (Addgene #162628) into a pHEK293 UltraExpression I vector (Clontech) that encodes an N-terminal Twin-Strep tag and HRV 3C protease cleavage site (pUE1-TSP) to generate pUE1-TSP-UL52.

    Techniques: Sequencing

    (a) Cryo-EM density map (transparent, moderate contour level) and model (cartoon, colored as in ) of the UL32 tripentamer interface helix and additional stabilizing density modeled as P5-S11 of the N-terminal extension. ( b ) UL32 tripentamer interface helix (green) and corresponding helices from UL52 (blue) and ORF68 (grey). ( c ) Schematic of transient complementation assay. ( d ) Model of tripentamer interface highlighting charge swap mutant R440E. Model displayed colored as in . ( e ) Representative western blot for expression of UL32 WT and mutants in transient complementation assay. ( f ) Graph of total viral yield of UL32 mutants in a transient complementation assay from three independent biological replicates.

    Journal: bioRxiv

    Article Title: Conserved assembly architecture of the essential herpesvirus packaging accessory factor

    doi: 10.64898/2026.01.22.701024

    Figure Lengend Snippet: (a) Cryo-EM density map (transparent, moderate contour level) and model (cartoon, colored as in ) of the UL32 tripentamer interface helix and additional stabilizing density modeled as P5-S11 of the N-terminal extension. ( b ) UL32 tripentamer interface helix (green) and corresponding helices from UL52 (blue) and ORF68 (grey). ( c ) Schematic of transient complementation assay. ( d ) Model of tripentamer interface highlighting charge swap mutant R440E. Model displayed colored as in . ( e ) Representative western blot for expression of UL32 WT and mutants in transient complementation assay. ( f ) Graph of total viral yield of UL32 mutants in a transient complementation assay from three independent biological replicates.

    Article Snippet: The coding region of UL52 was subcloned from a pcDNA4/TO-2xStrep vector (Addgene #162628) into a pHEK293 UltraExpression I vector (Clontech) that encodes an N-terminal Twin-Strep tag and HRV 3C protease cleavage site (pUE1-TSP) to generate pUE1-TSP-UL52.

    Techniques: Cryo-EM Sample Prep, Mutagenesis, Western Blot, Expressing