cct2 Search Results


negative mce2  (MedChemExpress)
93
MedChemExpress negative mce2
Negative Mce2, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/CCT2%2C+Human/10__69588_slash_mjer__v29i18__4263-76-122-119
Average 93 stars, based on 1 article reviews
negative mce2 - by Bioz Stars, 2026-11
93/100 stars
  Buy from Supplier
cct2  (Cell Signaling Technology Inc)
93
Cell Signaling Technology Inc cct2
Cct2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/CCT2+Antibody/pmc04179493-208-35-40
Average 93 stars, based on 1 article reviews
cct2 - by Bioz Stars, 2026-11
93/100 stars
  Buy from Supplier
a303 479a  (Bethyl)
93
Bethyl a303 479a
A303 479a, supplied by Bethyl, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/CCT2+Antibody/pm39879985-629-85-83
Average 93 stars, based on 1 article reviews
a303 479a - by Bioz Stars, 2026-11
93/100 stars
  Buy from Supplier
rabbit polyclonal cct2 antibody  (Proteintech)
93
Proteintech rabbit polyclonal cct2 antibody
Rabbit Polyclonal Cct2 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/CCT2+Antibody/pmc12373839-541-20-24
Average 93 stars, based on 1 article reviews
rabbit polyclonal cct2 antibody - by Bioz Stars, 2026-11
93/100 stars
  Buy from Supplier
rat anti cct1  (OriGene)
91
OriGene rat anti cct1
Rat Anti Cct1, supplied by OriGene, 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/cct2/TCP1+beta+(CCT2)+Rat+Monoclonal+Antibody/bio_rxiv__2023__07__31__551324-37-55-59
Average 91 stars, based on 1 article reviews
rat anti cct1 - by Bioz Stars, 2026-11
91/100 stars
  Buy from Supplier
cct8  (ABclonal Biotechnology)
94
ABclonal Biotechnology cct8
( A ) Sequence identities among HDAC1, HDAC2, HDAC3, and HDAC8. AlphaFold2- predicted HDAC3 model was aligned with HDAC1 and HDAC8, respectively. ( B ) Co-immunoprecipitation (co-IP) assays show that TRiC (monitored by <t>CCT8)</t> interacts with Flag-tagged HDAC1 and HDAC3, but displays no detectable binding to HDAC8. mNG2 serves as a negative control. ( C ) Top and side views of the closed-state TRiC-HDAC1-S1 cryo-EM map, exhibiting extra densities (medium violet red) within TRiC chamber. ( D ) The extra chamber density matches the HDAC1 model, with the N terminus less well ordered. ( E ) Comparison of substrate positions in TRiC-HDAC1-S1 and TRiC-HDAC3-S2, with their structures superimposed (HDAC3 density transparent seagrass green, HDAC1 violet red). ( F ) XL-MS analysis of the TRiC-HDAC1 complex, showing cross-links between HDAC1 and TRiC, between HDAC1 and PFD, and between PFD and TRiC. ( G ) HDAC8 refolding assay. HDAC8 was denatured in 6 M guanidine hydrochloride and dialyzed to remove the denaturant, with activity recovery monitored during dialysis. The schematic at left outlines the unfolding/refolding protocol; the bar graph at right quantifies HDAC8 activity relative to native protein (100%) at refold1–3 stages. “Unfolded” denotes activity in denaturant-containing buffer. Data are mean ± SEM ( n = 3). Statistical significance was assessed by one-way ANOVA: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. Analyzed with GraphPad Prism. ( H ) Electrostatic surface property analysis shows that, when aligned with HDAC1 and HDAC3 in the closed TRiC chamber, the putative TRiC-interaction surface of HDAC8 is predominantly positively charged, opposite to those of HDAC1 and HDAC3, disfavoring TRiC binding.
Cct8, supplied by ABclonal Biotechnology, 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/cct2/CCT2+Rabbit+pAb/pmc13371886-200-23-24
Average 94 stars, based on 1 article reviews
cct8 - by Bioz Stars, 2026-11
94/100 stars
  Buy from Supplier
anti-cct2  (Merck KGaA)
90
Merck KGaA anti-cct2
( A ) Sequence identities among HDAC1, HDAC2, HDAC3, and HDAC8. AlphaFold2- predicted HDAC3 model was aligned with HDAC1 and HDAC8, respectively. ( B ) Co-immunoprecipitation (co-IP) assays show that TRiC (monitored by <t>CCT8)</t> interacts with Flag-tagged HDAC1 and HDAC3, but displays no detectable binding to HDAC8. mNG2 serves as a negative control. ( C ) Top and side views of the closed-state TRiC-HDAC1-S1 cryo-EM map, exhibiting extra densities (medium violet red) within TRiC chamber. ( D ) The extra chamber density matches the HDAC1 model, with the N terminus less well ordered. ( E ) Comparison of substrate positions in TRiC-HDAC1-S1 and TRiC-HDAC3-S2, with their structures superimposed (HDAC3 density transparent seagrass green, HDAC1 violet red). ( F ) XL-MS analysis of the TRiC-HDAC1 complex, showing cross-links between HDAC1 and TRiC, between HDAC1 and PFD, and between PFD and TRiC. ( G ) HDAC8 refolding assay. HDAC8 was denatured in 6 M guanidine hydrochloride and dialyzed to remove the denaturant, with activity recovery monitored during dialysis. The schematic at left outlines the unfolding/refolding protocol; the bar graph at right quantifies HDAC8 activity relative to native protein (100%) at refold1–3 stages. “Unfolded” denotes activity in denaturant-containing buffer. Data are mean ± SEM ( n = 3). Statistical significance was assessed by one-way ANOVA: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. Analyzed with GraphPad Prism. ( H ) Electrostatic surface property analysis shows that, when aligned with HDAC1 and HDAC3 in the closed TRiC chamber, the putative TRiC-interaction surface of HDAC8 is predominantly positively charged, opposite to those of HDAC1 and HDAC3, disfavoring TRiC binding.
Anti Cct2, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/anti+cct2/pm37328936-39-26-29
Average 90 stars, based on 1 article reviews
anti-cct2 - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
pcdna-cct2  (GenScript corporation)
90
GenScript corporation pcdna-cct2
( A ) Sequence identities among HDAC1, HDAC2, HDAC3, and HDAC8. AlphaFold2- predicted HDAC3 model was aligned with HDAC1 and HDAC8, respectively. ( B ) Co-immunoprecipitation (co-IP) assays show that TRiC (monitored by <t>CCT8)</t> interacts with Flag-tagged HDAC1 and HDAC3, but displays no detectable binding to HDAC8. mNG2 serves as a negative control. ( C ) Top and side views of the closed-state TRiC-HDAC1-S1 cryo-EM map, exhibiting extra densities (medium violet red) within TRiC chamber. ( D ) The extra chamber density matches the HDAC1 model, with the N terminus less well ordered. ( E ) Comparison of substrate positions in TRiC-HDAC1-S1 and TRiC-HDAC3-S2, with their structures superimposed (HDAC3 density transparent seagrass green, HDAC1 violet red). ( F ) XL-MS analysis of the TRiC-HDAC1 complex, showing cross-links between HDAC1 and TRiC, between HDAC1 and PFD, and between PFD and TRiC. ( G ) HDAC8 refolding assay. HDAC8 was denatured in 6 M guanidine hydrochloride and dialyzed to remove the denaturant, with activity recovery monitored during dialysis. The schematic at left outlines the unfolding/refolding protocol; the bar graph at right quantifies HDAC8 activity relative to native protein (100%) at refold1–3 stages. “Unfolded” denotes activity in denaturant-containing buffer. Data are mean ± SEM ( n = 3). Statistical significance was assessed by one-way ANOVA: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. Analyzed with GraphPad Prism. ( H ) Electrostatic surface property analysis shows that, when aligned with HDAC1 and HDAC3 in the closed TRiC chamber, the putative TRiC-interaction surface of HDAC8 is predominantly positively charged, opposite to those of HDAC1 and HDAC3, disfavoring TRiC binding.
Pcdna Cct2, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/pcdna+cct2/10__1158_slash_1078___0432__ccr___15___2502-140-14-15
Average 90 stars, based on 1 article reviews
pcdna-cct2 - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
shrnas against circ-cct2  (Ribobio co)
90
Ribobio co shrnas against circ-cct2
( A ) Sequence identities among HDAC1, HDAC2, HDAC3, and HDAC8. AlphaFold2- predicted HDAC3 model was aligned with HDAC1 and HDAC8, respectively. ( B ) Co-immunoprecipitation (co-IP) assays show that TRiC (monitored by <t>CCT8)</t> interacts with Flag-tagged HDAC1 and HDAC3, but displays no detectable binding to HDAC8. mNG2 serves as a negative control. ( C ) Top and side views of the closed-state TRiC-HDAC1-S1 cryo-EM map, exhibiting extra densities (medium violet red) within TRiC chamber. ( D ) The extra chamber density matches the HDAC1 model, with the N terminus less well ordered. ( E ) Comparison of substrate positions in TRiC-HDAC1-S1 and TRiC-HDAC3-S2, with their structures superimposed (HDAC3 density transparent seagrass green, HDAC1 violet red). ( F ) XL-MS analysis of the TRiC-HDAC1 complex, showing cross-links between HDAC1 and TRiC, between HDAC1 and PFD, and between PFD and TRiC. ( G ) HDAC8 refolding assay. HDAC8 was denatured in 6 M guanidine hydrochloride and dialyzed to remove the denaturant, with activity recovery monitored during dialysis. The schematic at left outlines the unfolding/refolding protocol; the bar graph at right quantifies HDAC8 activity relative to native protein (100%) at refold1–3 stages. “Unfolded” denotes activity in denaturant-containing buffer. Data are mean ± SEM ( n = 3). Statistical significance was assessed by one-way ANOVA: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. Analyzed with GraphPad Prism. ( H ) Electrostatic surface property analysis shows that, when aligned with HDAC1 and HDAC3 in the closed TRiC chamber, the putative TRiC-interaction surface of HDAC8 is predominantly positively charged, opposite to those of HDAC1 and HDAC3, disfavoring TRiC binding.
Shrnas Against Circ Cct2, supplied by Ribobio co, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/alexa+fluor+594+conjugated+circ+cct2+probe/pm37866478-163-0-16
Average 90 stars, based on 1 article reviews
shrnas against circ-cct2 - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
cct.2 cryo consoletm cryoablation catheter  (CryoCath Technologies)
90
CryoCath Technologies cct.2 cryo consoletm cryoablation catheter
( A ) Sequence identities among HDAC1, HDAC2, HDAC3, and HDAC8. AlphaFold2- predicted HDAC3 model was aligned with HDAC1 and HDAC8, respectively. ( B ) Co-immunoprecipitation (co-IP) assays show that TRiC (monitored by <t>CCT8)</t> interacts with Flag-tagged HDAC1 and HDAC3, but displays no detectable binding to HDAC8. mNG2 serves as a negative control. ( C ) Top and side views of the closed-state TRiC-HDAC1-S1 cryo-EM map, exhibiting extra densities (medium violet red) within TRiC chamber. ( D ) The extra chamber density matches the HDAC1 model, with the N terminus less well ordered. ( E ) Comparison of substrate positions in TRiC-HDAC1-S1 and TRiC-HDAC3-S2, with their structures superimposed (HDAC3 density transparent seagrass green, HDAC1 violet red). ( F ) XL-MS analysis of the TRiC-HDAC1 complex, showing cross-links between HDAC1 and TRiC, between HDAC1 and PFD, and between PFD and TRiC. ( G ) HDAC8 refolding assay. HDAC8 was denatured in 6 M guanidine hydrochloride and dialyzed to remove the denaturant, with activity recovery monitored during dialysis. The schematic at left outlines the unfolding/refolding protocol; the bar graph at right quantifies HDAC8 activity relative to native protein (100%) at refold1–3 stages. “Unfolded” denotes activity in denaturant-containing buffer. Data are mean ± SEM ( n = 3). Statistical significance was assessed by one-way ANOVA: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. Analyzed with GraphPad Prism. ( H ) Electrostatic surface property analysis shows that, when aligned with HDAC1 and HDAC3 in the closed TRiC chamber, the putative TRiC-interaction surface of HDAC8 is predominantly positively charged, opposite to those of HDAC1 and HDAC3, disfavoring TRiC binding.
Cct.2 Cryo Consoletm Cryoablation Catheter, supplied by CryoCath Technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/cct2+cryoconsole/10__1016_slash_j__eupc__2004__04__002-650-13-10
Average 90 stars, based on 1 article reviews
cct.2 cryo consoletm cryoablation catheter - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
sirna targeting cct2  (Shanghai GenePharma)
90
Shanghai GenePharma sirna targeting cct2
( A ) Sequence identities among HDAC1, HDAC2, HDAC3, and HDAC8. AlphaFold2- predicted HDAC3 model was aligned with HDAC1 and HDAC8, respectively. ( B ) Co-immunoprecipitation (co-IP) assays show that TRiC (monitored by <t>CCT8)</t> interacts with Flag-tagged HDAC1 and HDAC3, but displays no detectable binding to HDAC8. mNG2 serves as a negative control. ( C ) Top and side views of the closed-state TRiC-HDAC1-S1 cryo-EM map, exhibiting extra densities (medium violet red) within TRiC chamber. ( D ) The extra chamber density matches the HDAC1 model, with the N terminus less well ordered. ( E ) Comparison of substrate positions in TRiC-HDAC1-S1 and TRiC-HDAC3-S2, with their structures superimposed (HDAC3 density transparent seagrass green, HDAC1 violet red). ( F ) XL-MS analysis of the TRiC-HDAC1 complex, showing cross-links between HDAC1 and TRiC, between HDAC1 and PFD, and between PFD and TRiC. ( G ) HDAC8 refolding assay. HDAC8 was denatured in 6 M guanidine hydrochloride and dialyzed to remove the denaturant, with activity recovery monitored during dialysis. The schematic at left outlines the unfolding/refolding protocol; the bar graph at right quantifies HDAC8 activity relative to native protein (100%) at refold1–3 stages. “Unfolded” denotes activity in denaturant-containing buffer. Data are mean ± SEM ( n = 3). Statistical significance was assessed by one-way ANOVA: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. Analyzed with GraphPad Prism. ( H ) Electrostatic surface property analysis shows that, when aligned with HDAC1 and HDAC3 in the closed TRiC chamber, the putative TRiC-interaction surface of HDAC8 is predominantly positively charged, opposite to those of HDAC1 and HDAC3, disfavoring TRiC binding.
Sirna Targeting Cct2, supplied by Shanghai GenePharma, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/sirna+targeting+cct2/pm38165547-63-4-39
Average 90 stars, based on 1 article reviews
sirna targeting cct2 - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
anti-cct2 (#r26528)  (ZenBio)
90
ZenBio anti-cct2 (#r26528)
( A ) Sequence identities among HDAC1, HDAC2, HDAC3, and HDAC8. AlphaFold2- predicted HDAC3 model was aligned with HDAC1 and HDAC8, respectively. ( B ) Co-immunoprecipitation (co-IP) assays show that TRiC (monitored by <t>CCT8)</t> interacts with Flag-tagged HDAC1 and HDAC3, but displays no detectable binding to HDAC8. mNG2 serves as a negative control. ( C ) Top and side views of the closed-state TRiC-HDAC1-S1 cryo-EM map, exhibiting extra densities (medium violet red) within TRiC chamber. ( D ) The extra chamber density matches the HDAC1 model, with the N terminus less well ordered. ( E ) Comparison of substrate positions in TRiC-HDAC1-S1 and TRiC-HDAC3-S2, with their structures superimposed (HDAC3 density transparent seagrass green, HDAC1 violet red). ( F ) XL-MS analysis of the TRiC-HDAC1 complex, showing cross-links between HDAC1 and TRiC, between HDAC1 and PFD, and between PFD and TRiC. ( G ) HDAC8 refolding assay. HDAC8 was denatured in 6 M guanidine hydrochloride and dialyzed to remove the denaturant, with activity recovery monitored during dialysis. The schematic at left outlines the unfolding/refolding protocol; the bar graph at right quantifies HDAC8 activity relative to native protein (100%) at refold1–3 stages. “Unfolded” denotes activity in denaturant-containing buffer. Data are mean ± SEM ( n = 3). Statistical significance was assessed by one-way ANOVA: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. Analyzed with GraphPad Prism. ( H ) Electrostatic surface property analysis shows that, when aligned with HDAC1 and HDAC3 in the closed TRiC chamber, the putative TRiC-interaction surface of HDAC8 is predominantly positively charged, opposite to those of HDAC1 and HDAC3, disfavoring TRiC binding.
Anti Cct2 (#R26528), supplied by ZenBio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cct2/anti+cct2+++r26528+/ppr0694988-56-5-10
Average 90 stars, based on 1 article reviews
anti-cct2 (#r26528) - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier

Image Search Results


( A ) Sequence identities among HDAC1, HDAC2, HDAC3, and HDAC8. AlphaFold2- predicted HDAC3 model was aligned with HDAC1 and HDAC8, respectively. ( B ) Co-immunoprecipitation (co-IP) assays show that TRiC (monitored by CCT8) interacts with Flag-tagged HDAC1 and HDAC3, but displays no detectable binding to HDAC8. mNG2 serves as a negative control. ( C ) Top and side views of the closed-state TRiC-HDAC1-S1 cryo-EM map, exhibiting extra densities (medium violet red) within TRiC chamber. ( D ) The extra chamber density matches the HDAC1 model, with the N terminus less well ordered. ( E ) Comparison of substrate positions in TRiC-HDAC1-S1 and TRiC-HDAC3-S2, with their structures superimposed (HDAC3 density transparent seagrass green, HDAC1 violet red). ( F ) XL-MS analysis of the TRiC-HDAC1 complex, showing cross-links between HDAC1 and TRiC, between HDAC1 and PFD, and between PFD and TRiC. ( G ) HDAC8 refolding assay. HDAC8 was denatured in 6 M guanidine hydrochloride and dialyzed to remove the denaturant, with activity recovery monitored during dialysis. The schematic at left outlines the unfolding/refolding protocol; the bar graph at right quantifies HDAC8 activity relative to native protein (100%) at refold1–3 stages. “Unfolded” denotes activity in denaturant-containing buffer. Data are mean ± SEM ( n = 3). Statistical significance was assessed by one-way ANOVA: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. Analyzed with GraphPad Prism. ( H ) Electrostatic surface property analysis shows that, when aligned with HDAC1 and HDAC3 in the closed TRiC chamber, the putative TRiC-interaction surface of HDAC8 is predominantly positively charged, opposite to those of HDAC1 and HDAC3, disfavoring TRiC binding.

Journal: Science Advances

Article Title: TRiC-assisted folding of class I HDAC family proteins regulated by distinct co-chaperone and cofactor networks

doi: 10.1126/sciadv.aef3048

Figure Lengend Snippet: ( A ) Sequence identities among HDAC1, HDAC2, HDAC3, and HDAC8. AlphaFold2- predicted HDAC3 model was aligned with HDAC1 and HDAC8, respectively. ( B ) Co-immunoprecipitation (co-IP) assays show that TRiC (monitored by CCT8) interacts with Flag-tagged HDAC1 and HDAC3, but displays no detectable binding to HDAC8. mNG2 serves as a negative control. ( C ) Top and side views of the closed-state TRiC-HDAC1-S1 cryo-EM map, exhibiting extra densities (medium violet red) within TRiC chamber. ( D ) The extra chamber density matches the HDAC1 model, with the N terminus less well ordered. ( E ) Comparison of substrate positions in TRiC-HDAC1-S1 and TRiC-HDAC3-S2, with their structures superimposed (HDAC3 density transparent seagrass green, HDAC1 violet red). ( F ) XL-MS analysis of the TRiC-HDAC1 complex, showing cross-links between HDAC1 and TRiC, between HDAC1 and PFD, and between PFD and TRiC. ( G ) HDAC8 refolding assay. HDAC8 was denatured in 6 M guanidine hydrochloride and dialyzed to remove the denaturant, with activity recovery monitored during dialysis. The schematic at left outlines the unfolding/refolding protocol; the bar graph at right quantifies HDAC8 activity relative to native protein (100%) at refold1–3 stages. “Unfolded” denotes activity in denaturant-containing buffer. Data are mean ± SEM ( n = 3). Statistical significance was assessed by one-way ANOVA: * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. Analyzed with GraphPad Prism. ( H ) Electrostatic surface property analysis shows that, when aligned with HDAC1 and HDAC3 in the closed TRiC chamber, the putative TRiC-interaction surface of HDAC8 is predominantly positively charged, opposite to those of HDAC1 and HDAC3, disfavoring TRiC binding.

Article Snippet: Antibody dilution was 1:2000 for the following immunoblots: HDAC3 (ABclonal A28114), HDAC1 (ABclonal A26492), HSPA1B (ABclonal A23457), PDCD5 (Proteintech 12456–1-AP), CCT2 (ABclonal A6546), CCT8 (ABclonal A4449), Flag (Sigma F1804), strep (Sigma SAB2702216), Goat Anti-Rabbit IgG H&L (HRP) (Abcam ab97051), HRP-conjugated Goat Anti-Mouse IgG (Proteintech SA00001–1-A).

Techniques: Sequencing, Immunoprecipitation, Co-Immunoprecipitation Assay, Binding Assay, Negative Control, Cryo-EM Sample Prep, Comparison, Structural Proteomics, Activity Assay