Review



adp  (TargetMol)


Bioz Verified Symbol TargetMol is a verified supplier
Bioz Manufacturer Symbol TargetMol manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 94
      Buy from Supplier

    Structured Review

    TargetMol adp
    Adp, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/Adenosine+5'-diphosphate/10__1038_slash_s41598___026___72824___0-64-25-26
    Average 94 stars, based on 9 article reviews
    adp - by Bioz Stars, 2026-11
    94/100 stars

    Images

    Related Articles

    other:

    Article Title: Gegen Qinlian pills alleviate carrageenan-induced thrombosis in mice model by regulating the HMGB1/NF-κB/NLRP3 signaling
    Article Snippet: Adenosine diphosphate (ADP) was purchased from TargetMol (Wellesley Hills, MA, USA).

    Article Title: Ginsenoside Rg1 attenuates platelet activation under shear stress via multi-target suppression of PI3K/AKT and ERK1/2 pathways: an in vitro microfluidic study.
    Article Snippet: 1 Central Laboratory, The Affiliated Yongchuan Hospital of Chongqing Medical University, Chongqing 402160, China 2 Clinical Laboratory of Liuzhou People’s Hospital affiliated to Guangxi Medical University, Liuzhou 545006, China 3 Department of Ophthalmology, The Second Affiliated Hospital of Chongqing Medical University, Chongqing 400010, China 4 Clinical Laboratory, The Affiliated Yongchuan Hospital of Chongqing Medical University, Chongqing 402160, China 5 Key Laboratory of Laboratory Medical Diagnostics, Ministry of Education, Department of Laboratory Medicine, Chongqing Medical University, Chongqing 400016, China 6 Clinical Laboratory of The Affiliated Rehabilitation Hospital, Chongqing Medical University, Chongqing 400050, China 7 Chongqing Municipality Clinical Research Center for Geriatric Diseases (the Affiliated Yongchuan Hospital of Chongqing Medical University), Chongqing 402160, China 8 Western Institute of Digital-Intelligent Medicine, Chongqing 401329, China Abstract Ginsenoside Rg1, a key bioactive component of Panax ginseng, is recognized for its cardiovascular protective effects, yet its role in modulating platelet activation under high shear stress remains incompletely understood.. This study aimed to systematically evaluate the in vitro effects and underlying mechanisms of Rg1 on platelet aggregation under high shear stress using a microfluidic chip system.. In this study, blood flow environments at venous (300 s−1), arterial (1500 s−1), and pathological arterial (5000 s−1) shear rates were simulated using microfluidic chips.



    Similar Products

    adp  (TargetMol)
    94
    TargetMol adp
    Adp, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/Adenosine+5'-diphosphate/10__1038_slash_s41598___026___72824___0-64-25-26
    Average 94 stars, based on 1 article reviews
    adp - by Bioz Stars, 2026-11
    94/100 stars
    		  Buy from Supplier
    adp mce cat  (MedChemExpress)
    94
    MedChemExpress adp mce cat
    Adp Mce Cat, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/Adenosine+5'-diphosphate/pm42776840-718-78-79
    Average 94 stars, based on 1 article reviews
    adp mce cat - by Bioz Stars, 2026-11
    94/100 stars
    		  Buy from Supplier
    adenosine diphosphate adp  (TargetMol)
    94
    TargetMol adenosine diphosphate adp
    Adenosine Diphosphate Adp, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/Adenosine+5'-diphosphate/pm42418135-43-0-6
    Average 94 stars, based on 1 article reviews
    adenosine diphosphate adp - by Bioz Stars, 2026-11
    94/100 stars
    		  Buy from Supplier
    adp standard  (MedChemExpress)
    94
    MedChemExpress adp standard
    Adp Standard, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/Adenosine+5'-diphosphate/pmc13198262-73-0-3
    Average 94 stars, based on 1 article reviews
    adp standard - by Bioz Stars, 2026-11
    94/100 stars
    		  Buy from Supplier
    adenosine diphosphate  (Tokyo Chemical Industry)
    86
    Tokyo Chemical Industry adenosine diphosphate
    Adenosine Diphosphate, supplied by Tokyo Chemical Industry, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/adenosine+diphosphate/10__1096_slash_fj__202504538rr-27-7-10
    Average 86 stars, based on 1 article reviews
    adenosine diphosphate - by Bioz Stars, 2026-11
    86/100 stars
    		  Buy from Supplier
    adp  (Selleck Chemicals)
    91
    Selleck Chemicals adp
    a , b , pMEK1-catalyzed dephosphorylation of pY-ERK1. In <t>an</t> <t>ATP-,</t> <t>ADP-,</t> or AMP-PNP-containing buffer, or a nucleotide-free buffer, pY-ERK1 was incubated with various concentrations of pMEK1 at 30, after 3 minutes, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( a ) and quantified ( b ). c , d , pMEK1-catalyzed dephosphorylation of pTY-ERK1. In an ADP- or AMP-PNP-containing buffer, or a nucleotide-free buffer, pTY-ERK1 was incubated with pMEK1 at 30. At each time point, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( c ) and quantified ( d ). e , f , Effect of mutations of the nucleotide-binding pocket of MEK1 on the activity of pMEK1 to catalyze phosphate group transfer from ERK1 Y204 to T202. In a nucleotide-free buffer, pY-ERK1 was incubated with wild-type (WT) or mutant pMEK1 at 30, and then the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( e ) and quantified ( f ). The gels in ( a ), ( c ) and ( e ) are the results of a representative experiment out of three independent experiments. The data in ( b ), ( d ) and ( f ) represent the mean ± SD of three independent measurements.
    Adp, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/Adenosine+5%E2%80%B2-diphosphate+sodium+salt/bio_rxiv__64898__2026__03__13__710243-304-1-2
    Average 91 stars, based on 1 article reviews
    adp - by Bioz Stars, 2026-11
    91/100 stars
    		  Buy from Supplier
    adenosine diphosphate adp  (Nacalai)
    86
    Nacalai adenosine diphosphate adp
    a , b , pMEK1-catalyzed dephosphorylation of pY-ERK1. In <t>an</t> <t>ATP-,</t> <t>ADP-,</t> or AMP-PNP-containing buffer, or a nucleotide-free buffer, pY-ERK1 was incubated with various concentrations of pMEK1 at 30, after 3 minutes, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( a ) and quantified ( b ). c , d , pMEK1-catalyzed dephosphorylation of pTY-ERK1. In an ADP- or AMP-PNP-containing buffer, or a nucleotide-free buffer, pTY-ERK1 was incubated with pMEK1 at 30. At each time point, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( c ) and quantified ( d ). e , f , Effect of mutations of the nucleotide-binding pocket of MEK1 on the activity of pMEK1 to catalyze phosphate group transfer from ERK1 Y204 to T202. In a nucleotide-free buffer, pY-ERK1 was incubated with wild-type (WT) or mutant pMEK1 at 30, and then the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( e ) and quantified ( f ). The gels in ( a ), ( c ) and ( e ) are the results of a representative experiment out of three independent experiments. The data in ( b ), ( d ) and ( f ) represent the mean ± SD of three independent measurements.
    Adenosine Diphosphate Adp, supplied by Nacalai, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/adenosine+adp+diphosphate/pm41817700-39-0-10
    Average 86 stars, based on 1 article reviews
    adenosine diphosphate adp - by Bioz Stars, 2026-11
    86/100 stars
    		  Buy from Supplier
    adenosine diphosphate  (Sysmex Corporation)
    86
    Sysmex Corporation adenosine diphosphate
    a , b , pMEK1-catalyzed dephosphorylation of pY-ERK1. In <t>an</t> <t>ATP-,</t> <t>ADP-,</t> or AMP-PNP-containing buffer, or a nucleotide-free buffer, pY-ERK1 was incubated with various concentrations of pMEK1 at 30, after 3 minutes, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( a ) and quantified ( b ). c , d , pMEK1-catalyzed dephosphorylation of pTY-ERK1. In an ADP- or AMP-PNP-containing buffer, or a nucleotide-free buffer, pTY-ERK1 was incubated with pMEK1 at 30. At each time point, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( c ) and quantified ( d ). e , f , Effect of mutations of the nucleotide-binding pocket of MEK1 on the activity of pMEK1 to catalyze phosphate group transfer from ERK1 Y204 to T202. In a nucleotide-free buffer, pY-ERK1 was incubated with wild-type (WT) or mutant pMEK1 at 30, and then the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( e ) and quantified ( f ). The gels in ( a ), ( c ) and ( e ) are the results of a representative experiment out of three independent experiments. The data in ( b ), ( d ) and ( f ) represent the mean ± SD of three independent measurements.
    Adenosine Diphosphate, supplied by Sysmex Corporation, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/adenosine+diphosphate/10__4103_slash_wjtcm__wjtcm_70_25-65-0-6
    Average 86 stars, based on 1 article reviews
    adenosine diphosphate - by Bioz Stars, 2026-11
    86/100 stars
    		  Buy from Supplier
    adp adenosine  (Jena Bioscience)
    94
    Jena Bioscience adp adenosine
    A, Extension of a 20-mer RNA substrate oligo (oligo 1) using rTENT4B and ATP analogs demonstrating differential incorporation. (AMP: Adenosine-5’-monophosphate; ADP: <t>Adenosine-5’-diphosphate;</t> ATP: Adenosine-5’-triphosphate. n=3 replicates, one representative shown. B, Utilization of nucleotide diphosphates (NDPs) by rTENT4B. rTENT4B along with a 20-mer RNA-substrate oligo (oligo 2) was incubated in the presence of four canonical NDPs, in RNA-substrate extension assays, and reaction products were resolved using denaturing TBE/Urea-acrylamide gel followed by Sybr gold staining. C , rTENT4B was incubated with four canonical NDPs plus 5’-Cy5-labeled ATP as substrate. NDP incorporation was confirmed via detecting generation of Cy5-labeled RNA chains after 30 min in no RNA-substrate added reactions. D , De novo ADP polymerization using rTENT4B. rTENT4B along with increasing concentrations of ADP was subjected to RNA-substrate extension assay in the absence of an RNA-substrate, and generation of de novo synthesized RNA products were detected using denaturing TBE/Urea-acrylamide gel followed by Sybr gold staining. E , Consumption of ADP by rTENT4B via analysis of Pi yield, in the presence/ absence of inorganic pyrophosphatase (PPA) as a measure of ATP contamination (ADP + Pi), in the presence/absence of an RNA-substrate oligo, compared to that of rTENT4B alone versus rTENT4B plus ATP. n=4 biological replicates. Mean + S.D. shown, 2-way ANOVA, ns- not significant, ****p<0.001.
    Adp Adenosine, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/ADP+-+Solid/bio_rxiv__64898__2026__03__05__709691-54-6-9
    Average 94 stars, based on 1 article reviews
    adp adenosine - by Bioz Stars, 2026-11
    94/100 stars
    		  Buy from Supplier
    adenosine diphosphate adp  (MedChemExpress)
    94
    MedChemExpress adenosine diphosphate adp
    A, Extension of a 20-mer RNA substrate oligo (oligo 1) using rTENT4B and ATP analogs demonstrating differential incorporation. (AMP: Adenosine-5’-monophosphate; ADP: <t>Adenosine-5’-diphosphate;</t> ATP: Adenosine-5’-triphosphate. n=3 replicates, one representative shown. B, Utilization of nucleotide diphosphates (NDPs) by rTENT4B. rTENT4B along with a 20-mer RNA-substrate oligo (oligo 2) was incubated in the presence of four canonical NDPs, in RNA-substrate extension assays, and reaction products were resolved using denaturing TBE/Urea-acrylamide gel followed by Sybr gold staining. C , rTENT4B was incubated with four canonical NDPs plus 5’-Cy5-labeled ATP as substrate. NDP incorporation was confirmed via detecting generation of Cy5-labeled RNA chains after 30 min in no RNA-substrate added reactions. D , De novo ADP polymerization using rTENT4B. rTENT4B along with increasing concentrations of ADP was subjected to RNA-substrate extension assay in the absence of an RNA-substrate, and generation of de novo synthesized RNA products were detected using denaturing TBE/Urea-acrylamide gel followed by Sybr gold staining. E , Consumption of ADP by rTENT4B via analysis of Pi yield, in the presence/ absence of inorganic pyrophosphatase (PPA) as a measure of ATP contamination (ADP + Pi), in the presence/absence of an RNA-substrate oligo, compared to that of rTENT4B alone versus rTENT4B plus ATP. n=4 biological replicates. Mean + S.D. shown, 2-way ANOVA, ns- not significant, ****p<0.001.
    Adenosine Diphosphate Adp, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adenosine+diphosphate+adp/Adenosine+5'-diphosphate/10__1016_slash_j__celbio__2026__100383-218-3-9
    Average 94 stars, based on 1 article reviews
    adenosine diphosphate adp - by Bioz Stars, 2026-11
    94/100 stars
    		  Buy from Supplier

    Image Search Results


    a , b , pMEK1-catalyzed dephosphorylation of pY-ERK1. In an ATP-, ADP-, or AMP-PNP-containing buffer, or a nucleotide-free buffer, pY-ERK1 was incubated with various concentrations of pMEK1 at 30, after 3 minutes, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( a ) and quantified ( b ). c , d , pMEK1-catalyzed dephosphorylation of pTY-ERK1. In an ADP- or AMP-PNP-containing buffer, or a nucleotide-free buffer, pTY-ERK1 was incubated with pMEK1 at 30. At each time point, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( c ) and quantified ( d ). e , f , Effect of mutations of the nucleotide-binding pocket of MEK1 on the activity of pMEK1 to catalyze phosphate group transfer from ERK1 Y204 to T202. In a nucleotide-free buffer, pY-ERK1 was incubated with wild-type (WT) or mutant pMEK1 at 30, and then the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( e ) and quantified ( f ). The gels in ( a ), ( c ) and ( e ) are the results of a representative experiment out of three independent experiments. The data in ( b ), ( d ) and ( f ) represent the mean ± SD of three independent measurements.

    Journal: bioRxiv

    Article Title: Mechanistic insight into the phosphorylation of ERK by MEK

    doi: 10.64898/2026.03.13.710243

    Figure Lengend Snippet: a , b , pMEK1-catalyzed dephosphorylation of pY-ERK1. In an ATP-, ADP-, or AMP-PNP-containing buffer, or a nucleotide-free buffer, pY-ERK1 was incubated with various concentrations of pMEK1 at 30, after 3 minutes, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( a ) and quantified ( b ). c , d , pMEK1-catalyzed dephosphorylation of pTY-ERK1. In an ADP- or AMP-PNP-containing buffer, or a nucleotide-free buffer, pTY-ERK1 was incubated with pMEK1 at 30. At each time point, the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( c ) and quantified ( d ). e , f , Effect of mutations of the nucleotide-binding pocket of MEK1 on the activity of pMEK1 to catalyze phosphate group transfer from ERK1 Y204 to T202. In a nucleotide-free buffer, pY-ERK1 was incubated with wild-type (WT) or mutant pMEK1 at 30, and then the phosphorylation of ERK1 T202 and Y204 was evaluated using Western blotting ( e ) and quantified ( f ). The gels in ( a ), ( c ) and ( e ) are the results of a representative experiment out of three independent experiments. The data in ( b ), ( d ) and ( f ) represent the mean ± SD of three independent measurements.

    Article Snippet: ATP, ADP (Selleck, Cat# S6325, 100 mM stock in H 2 O) and AMP-PNP (Sigma, Cat# A2647, 100 mM stock in H 2 O) were each prepared as a 4× stock in the reaction buffer.

    Techniques: De-Phosphorylation Assay, Incubation, Phospho-proteomics, Western Blot, Binding Assay, Activity Assay, Mutagenesis

    a , Summary of the dissociation constants ( K d ) for the binding between MEK1 (uMEK1 or pMEK1) and ERK1 (uERK1 or thio-pTY-ERK1) in the absence or presence of ADP or AMP-PNP. The K d values were measured using Isothermal Titration Calorimetry (ITC). b , Cycle of the pMEK1-catalyzed ERK1 phosphorylation reaction. In addition to the canonical sequential mechanism for pMEK1 (where Y204 and T202 are phosphorylated sequentially by ATP), we proposed a relay mechanism to explain the phosphorylation process of ERK1 T202: Y204 is phosphorylated first, its phosphate group is then transferred to T202, and Y204 is phosphorylated again by ATP to generate dual-phosphorylated ERK1.

    Journal: bioRxiv

    Article Title: Mechanistic insight into the phosphorylation of ERK by MEK

    doi: 10.64898/2026.03.13.710243

    Figure Lengend Snippet: a , Summary of the dissociation constants ( K d ) for the binding between MEK1 (uMEK1 or pMEK1) and ERK1 (uERK1 or thio-pTY-ERK1) in the absence or presence of ADP or AMP-PNP. The K d values were measured using Isothermal Titration Calorimetry (ITC). b , Cycle of the pMEK1-catalyzed ERK1 phosphorylation reaction. In addition to the canonical sequential mechanism for pMEK1 (where Y204 and T202 are phosphorylated sequentially by ATP), we proposed a relay mechanism to explain the phosphorylation process of ERK1 T202: Y204 is phosphorylated first, its phosphate group is then transferred to T202, and Y204 is phosphorylated again by ATP to generate dual-phosphorylated ERK1.

    Article Snippet: ATP, ADP (Selleck, Cat# S6325, 100 mM stock in H 2 O) and AMP-PNP (Sigma, Cat# A2647, 100 mM stock in H 2 O) were each prepared as a 4× stock in the reaction buffer.

    Techniques: Binding Assay, Isothermal Titration Calorimetry, Phospho-proteomics

    a , Purified unphosphorylated (uERK1), phosphorylated (pY-ERK1 and pTY-ERK1), and thio-phosphorylated ERK1 (thio-pTY-ERK1) were examined by SDS–PAGE and visualized by Coomassie blue staining. b , Comparison of the ATP consumption rate of thio-pTY-ERK1 with those of uERK1, pY-ERK1, and pTY-ERK1. The ATP consumption was measured using an ADP-Glo Kinase Assay. The MBP peptide FFKNIVTPRTPPPSQGK was used as the substrate of ERK1. The data represent the mean ± SD of three independent measurements. c , d , pMEK1-catalyzed dephosphorylation of pTY-ERK1 ( c ) and thio-pTY-ERK1 ( d ) in an ADP-containing buffer. The percentage of ERK1 in different phosphorylation states was determined by LC-MS.

    Journal: bioRxiv

    Article Title: Mechanistic insight into the phosphorylation of ERK by MEK

    doi: 10.64898/2026.03.13.710243

    Figure Lengend Snippet: a , Purified unphosphorylated (uERK1), phosphorylated (pY-ERK1 and pTY-ERK1), and thio-phosphorylated ERK1 (thio-pTY-ERK1) were examined by SDS–PAGE and visualized by Coomassie blue staining. b , Comparison of the ATP consumption rate of thio-pTY-ERK1 with those of uERK1, pY-ERK1, and pTY-ERK1. The ATP consumption was measured using an ADP-Glo Kinase Assay. The MBP peptide FFKNIVTPRTPPPSQGK was used as the substrate of ERK1. The data represent the mean ± SD of three independent measurements. c , d , pMEK1-catalyzed dephosphorylation of pTY-ERK1 ( c ) and thio-pTY-ERK1 ( d ) in an ADP-containing buffer. The percentage of ERK1 in different phosphorylation states was determined by LC-MS.

    Article Snippet: ATP, ADP (Selleck, Cat# S6325, 100 mM stock in H 2 O) and AMP-PNP (Sigma, Cat# A2647, 100 mM stock in H 2 O) were each prepared as a 4× stock in the reaction buffer.

    Techniques: Purification, SDS Page, Staining, Comparison, Kinase Assay, De-Phosphorylation Assay, Phospho-proteomics, Liquid Chromatography with Mass Spectroscopy

    A, Extension of a 20-mer RNA substrate oligo (oligo 1) using rTENT4B and ATP analogs demonstrating differential incorporation. (AMP: Adenosine-5’-monophosphate; ADP: Adenosine-5’-diphosphate; ATP: Adenosine-5’-triphosphate. n=3 replicates, one representative shown. B, Utilization of nucleotide diphosphates (NDPs) by rTENT4B. rTENT4B along with a 20-mer RNA-substrate oligo (oligo 2) was incubated in the presence of four canonical NDPs, in RNA-substrate extension assays, and reaction products were resolved using denaturing TBE/Urea-acrylamide gel followed by Sybr gold staining. C , rTENT4B was incubated with four canonical NDPs plus 5’-Cy5-labeled ATP as substrate. NDP incorporation was confirmed via detecting generation of Cy5-labeled RNA chains after 30 min in no RNA-substrate added reactions. D , De novo ADP polymerization using rTENT4B. rTENT4B along with increasing concentrations of ADP was subjected to RNA-substrate extension assay in the absence of an RNA-substrate, and generation of de novo synthesized RNA products were detected using denaturing TBE/Urea-acrylamide gel followed by Sybr gold staining. E , Consumption of ADP by rTENT4B via analysis of Pi yield, in the presence/ absence of inorganic pyrophosphatase (PPA) as a measure of ATP contamination (ADP + Pi), in the presence/absence of an RNA-substrate oligo, compared to that of rTENT4B alone versus rTENT4B plus ATP. n=4 biological replicates. Mean + S.D. shown, 2-way ANOVA, ns- not significant, ****p<0.001.

    Journal: bioRxiv

    Article Title: Primer- and template-independent RNA polymerization by terminal nucleotidyltransferase TENT4B

    doi: 10.64898/2026.03.05.709691

    Figure Lengend Snippet: A, Extension of a 20-mer RNA substrate oligo (oligo 1) using rTENT4B and ATP analogs demonstrating differential incorporation. (AMP: Adenosine-5’-monophosphate; ADP: Adenosine-5’-diphosphate; ATP: Adenosine-5’-triphosphate. n=3 replicates, one representative shown. B, Utilization of nucleotide diphosphates (NDPs) by rTENT4B. rTENT4B along with a 20-mer RNA-substrate oligo (oligo 2) was incubated in the presence of four canonical NDPs, in RNA-substrate extension assays, and reaction products were resolved using denaturing TBE/Urea-acrylamide gel followed by Sybr gold staining. C , rTENT4B was incubated with four canonical NDPs plus 5’-Cy5-labeled ATP as substrate. NDP incorporation was confirmed via detecting generation of Cy5-labeled RNA chains after 30 min in no RNA-substrate added reactions. D , De novo ADP polymerization using rTENT4B. rTENT4B along with increasing concentrations of ADP was subjected to RNA-substrate extension assay in the absence of an RNA-substrate, and generation of de novo synthesized RNA products were detected using denaturing TBE/Urea-acrylamide gel followed by Sybr gold staining. E , Consumption of ADP by rTENT4B via analysis of Pi yield, in the presence/ absence of inorganic pyrophosphatase (PPA) as a measure of ATP contamination (ADP + Pi), in the presence/absence of an RNA-substrate oligo, compared to that of rTENT4B alone versus rTENT4B plus ATP. n=4 biological replicates. Mean + S.D. shown, 2-way ANOVA, ns- not significant, ****p<0.001.

    Article Snippet: ATP- Adenosine-5’-triphosphate (N0450, New England Biolabs) ADP- Adenosine-5’-diphosphate (NU-1198, Jena Bioscience) AMP- Adenosine-5’-monophosphate (A1752, Sigma) GTP- Guanosine-5’-triphosphate (N0450, New England Biolabs) GDP- Guanosine-5’-diphosphate (G7127, Sigma) CTP- Cytidine-5’-triphosphate (N0450, New England Biolabs) CDP- Cytidine-5’-diphosphate (C9755, Sigma) UTP- Uridine-5’-triphosphate (N0450, New England Biolabs) UDP- Uridine-5’-diphosphate (94330, Sigma) Cy5-ATP- γ-(6-Aminohexyl)-ATP-Cy5- (NU-833-CY5, Jena Bioscience) Cy5-GTP- γ-(6-Aminohexyl)-GTP-Cy5- (NU-834-CY5, Jena Bioscience)

    Techniques: Incubation, Acrylamide Gel Assay, Staining, Labeling, Synthesized