anti tcp1 Search Results


rabbit anti tcp1 polyclonal affinity purified  (Innovative Research Inc)
N/A
Rabbit Anti TCP1 Polyclonal Affinity Purified (PBS with 0.02% sodium azide, 50% glycerol, pH7.3) (Immunofluorescence) from Innovative Research is a polyclonal antibody in a liquid format, buffered in PBS with 0.02% sodium azide, 50% glycerol,
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anti-tcp1 (#r27336)  (ZenBio)
90
ZenBio anti-tcp1 (#r27336)
Anti Tcp1 (#R27336), 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/anti+tcp1/anti+tcp1+++r27336+/ppr0694988-56-2-10
Average 90 stars, based on 1 article reviews
anti-tcp1 (#r27336) - by Bioz Stars, 2026-09
90/100 stars
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anti-tcp1 91a  (Assay Designs Inc)
90
Assay Designs Inc anti-tcp1 91a
Anti Tcp1 91a, supplied by Assay Designs Inc, 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/anti+tcp1/anti+tcp1+91a/pmc02808216-234-41-43
Average 90 stars, based on 1 article reviews
anti-tcp1 91a - by Bioz Stars, 2026-09
90/100 stars
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primary antibodies for vp1 i58  (Stressgen Biotechnologies)
86
Stressgen Biotechnologies primary antibodies for vp1 i58
E. coli chaperones interact with the C-terminal domain of the polyomavirus capsid protein <t>VP1.</t> (A) Recombinant <t>VP1</t> and a GST-VP3 fusion protein were coexpressed in E. coli and were purified by using glutathione Sepharose chromatography, followed by thrombin cleavage as described (15). Eluates were analyzed by SDS/PAGE and Coomassie blue staining. Lane 1, full-length VP1 (flVP1) coexpressed with full-length VP3 (flVP3); lane 2, residues 32-316 of VP1 (tVP1) coexpressed with the C-terminal 105 residues of VP3 (tVP3); lane 3, flVP1 coexpressed with tVP3; and lane 4, tVP1 coexpressed with flVP3. (B) Immunoblots of VP1 + VP3 pentamers purified by glutathione affinity, ion exchange, and gel filtration chromatography (VP1 + VP3), or only glutathione affinity and gel filtration chromatography (VP1 + VP3 + copurified chaperones).
Primary Antibodies For Vp1 I58, supplied by Stressgen Biotechnologies, 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/anti+tcp1/1+anti+tcp/pmc00193586-47-6-33
Average 86 stars, based on 1 article reviews
primary antibodies for vp1 i58 - by Bioz Stars, 2026-09
86/100 stars
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resource source identifier antibodies mouse monoclonal anti cct1 boster  (Boster Bio)
92
Boster Bio resource source identifier antibodies mouse monoclonal anti cct1 boster
E. coli chaperones interact with the C-terminal domain of the polyomavirus capsid protein <t>VP1.</t> (A) Recombinant <t>VP1</t> and a GST-VP3 fusion protein were coexpressed in E. coli and were purified by using glutathione Sepharose chromatography, followed by thrombin cleavage as described (15). Eluates were analyzed by SDS/PAGE and Coomassie blue staining. Lane 1, full-length VP1 (flVP1) coexpressed with full-length VP3 (flVP3); lane 2, residues 32-316 of VP1 (tVP1) coexpressed with the C-terminal 105 residues of VP3 (tVP3); lane 3, flVP1 coexpressed with tVP3; and lane 4, tVP1 coexpressed with flVP3. (B) Immunoblots of VP1 + VP3 pentamers purified by glutathione affinity, ion exchange, and gel filtration chromatography (VP1 + VP3), or only glutathione affinity and gel filtration chromatography (VP1 + VP3 + copurified chaperones).
Resource Source Identifier Antibodies Mouse Monoclonal Anti Cct1 Boster, supplied by Boster Bio, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+tcp1/Anti-TCP1+alpha+Antibody+Picoband/pm35366418-688-2-9
Average 92 stars, based on 1 article reviews
resource source identifier antibodies mouse monoclonal anti cct1 boster - by Bioz Stars, 2026-09
92/100 stars
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a6546  (Boster Bio)
92
Boster Bio a6546
E. coli chaperones interact with the C-terminal domain of the polyomavirus capsid protein <t>VP1.</t> (A) Recombinant <t>VP1</t> and a GST-VP3 fusion protein were coexpressed in E. coli and were purified by using glutathione Sepharose chromatography, followed by thrombin cleavage as described (15). Eluates were analyzed by SDS/PAGE and Coomassie blue staining. Lane 1, full-length VP1 (flVP1) coexpressed with full-length VP3 (flVP3); lane 2, residues 32-316 of VP1 (tVP1) coexpressed with the C-terminal 105 residues of VP3 (tVP3); lane 3, flVP1 coexpressed with tVP3; and lane 4, tVP1 coexpressed with flVP3. (B) Immunoblots of VP1 + VP3 pentamers purified by glutathione affinity, ion exchange, and gel filtration chromatography (VP1 + VP3), or only glutathione affinity and gel filtration chromatography (VP1 + VP3 + copurified chaperones).
A6546, supplied by Boster Bio, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+tcp1/Anti-CCT3+Antibody+Picoband/pm35366418-688-17-22
Average 92 stars, based on 1 article reviews
a6546 - by Bioz Stars, 2026-09
92/100 stars
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custom-made rabbit antibody: anti-tcp1, 292-305:c-skggirkrarpgss  (BioGenes GmbH)
90
BioGenes GmbH custom-made rabbit antibody: anti-tcp1, 292-305:c-skggirkrarpgss
E. coli chaperones interact with the C-terminal domain of the polyomavirus capsid protein <t>VP1.</t> (A) Recombinant <t>VP1</t> and a GST-VP3 fusion protein were coexpressed in E. coli and were purified by using glutathione Sepharose chromatography, followed by thrombin cleavage as described (15). Eluates were analyzed by SDS/PAGE and Coomassie blue staining. Lane 1, full-length VP1 (flVP1) coexpressed with full-length VP3 (flVP3); lane 2, residues 32-316 of VP1 (tVP1) coexpressed with the C-terminal 105 residues of VP3 (tVP3); lane 3, flVP1 coexpressed with tVP3; and lane 4, tVP1 coexpressed with flVP3. (B) Immunoblots of VP1 + VP3 pentamers purified by glutathione affinity, ion exchange, and gel filtration chromatography (VP1 + VP3), or only glutathione affinity and gel filtration chromatography (VP1 + VP3 + copurified chaperones).
Custom Made Rabbit Antibody: Anti Tcp1, 292 305:C Skggirkrarpgss, supplied by BioGenes GmbH, 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/anti+tcp1/custom+made+rabbit+antibody++anti+tcp1++292+305+c+skggirkrarpgss/pm32895530-818-40-42
Average 90 stars, based on 1 article reviews
custom-made rabbit antibody: anti-tcp1, 292-305:c-skggirkrarpgss - by Bioz Stars, 2026-09
90/100 stars
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anti-tcp1 delta/cct4 antibody picoband  (Boster Bio)
90
Boster Bio anti-tcp1 delta/cct4 antibody picoband
E. coli chaperones interact with the C-terminal domain of the polyomavirus capsid protein <t>VP1.</t> (A) Recombinant <t>VP1</t> and a GST-VP3 fusion protein were coexpressed in E. coli and were purified by using glutathione Sepharose chromatography, followed by thrombin cleavage as described (15). Eluates were analyzed by SDS/PAGE and Coomassie blue staining. Lane 1, full-length VP1 (flVP1) coexpressed with full-length VP3 (flVP3); lane 2, residues 32-316 of VP1 (tVP1) coexpressed with the C-terminal 105 residues of VP3 (tVP3); lane 3, flVP1 coexpressed with tVP3; and lane 4, tVP1 coexpressed with flVP3. (B) Immunoblots of VP1 + VP3 pentamers purified by glutathione affinity, ion exchange, and gel filtration chromatography (VP1 + VP3), or only glutathione affinity and gel filtration chromatography (VP1 + VP3 + copurified chaperones).
Anti Tcp1 Delta/Cct4 Antibody Picoband, supplied by Boster Bio, 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/anti+tcp1/Anti-TCP1+delta%2FCCT4+Antibody+Picoband/boster+bio___pb9927
Average 90 stars, based on 1 article reviews
anti-tcp1 delta/cct4 antibody picoband - by Bioz Stars, 2026-09
90/100 stars
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anti-tcp1 (full length) polyclonal antibody  (Creative BioMart)
N/A
The protein encoded by this gene is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical
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rabbit anti-human tcp1 beta / cct2  (RayBiotech)
N/A
TCP1 Beta / CCT2 Rabbit anti-Human Polyclonal (Unconjugated) Antibody, (50 µl)
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mouse anti-human cct5 / tcp1 epsilon  (RayBiotech)
N/A
CCT5 / TCP1 Epsilon Mouse anti-Human Monoclonal (Unconjugated) (4E5-4B1) Antibody, (50 µg)
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anti tcp1 beta picoband antibody  (Abcepta)
N/A
Rabbit IgG polyclonal antibody for T complex protein 1 subunit beta CCT2 detection Tested with WB IHC P in Human Mouse Rat
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Image Search Results


E. coli chaperones interact with the C-terminal domain of the polyomavirus capsid protein VP1. (A) Recombinant VP1 and a GST-VP3 fusion protein were coexpressed in E. coli and were purified by using glutathione Sepharose chromatography, followed by thrombin cleavage as described (15). Eluates were analyzed by SDS/PAGE and Coomassie blue staining. Lane 1, full-length VP1 (flVP1) coexpressed with full-length VP3 (flVP3); lane 2, residues 32-316 of VP1 (tVP1) coexpressed with the C-terminal 105 residues of VP3 (tVP3); lane 3, flVP1 coexpressed with tVP3; and lane 4, tVP1 coexpressed with flVP3. (B) Immunoblots of VP1 + VP3 pentamers purified by glutathione affinity, ion exchange, and gel filtration chromatography (VP1 + VP3), or only glutathione affinity and gel filtration chromatography (VP1 + VP3 + copurified chaperones).

Journal:

Article Title: Chaperone-mediated in vitro assembly of Polyomavirus capsids

doi: 10.1073/pnas.1832245100

Figure Lengend Snippet: E. coli chaperones interact with the C-terminal domain of the polyomavirus capsid protein VP1. (A) Recombinant VP1 and a GST-VP3 fusion protein were coexpressed in E. coli and were purified by using glutathione Sepharose chromatography, followed by thrombin cleavage as described (15). Eluates were analyzed by SDS/PAGE and Coomassie blue staining. Lane 1, full-length VP1 (flVP1) coexpressed with full-length VP3 (flVP3); lane 2, residues 32-316 of VP1 (tVP1) coexpressed with the C-terminal 105 residues of VP3 (tVP3); lane 3, flVP1 coexpressed with tVP3; and lane 4, tVP1 coexpressed with flVP3. (B) Immunoblots of VP1 + VP3 pentamers purified by glutathione affinity, ion exchange, and gel filtration chromatography (VP1 + VP3), or only glutathione affinity and gel filtration chromatography (VP1 + VP3 + copurified chaperones).

Article Snippet: The membranes were blotted by using primary antibodies for VP1 (I58) ( 7 , 22 ), VP3 (482) ( 7 , 22 ), DnaK (AXL623, Accurate Chemical and Scientific, Westbury, NY), DnaJ (SPA-410, StressGen Biotechnologies), GrpE (SPA-240, StressGen Biotechnologies), and GroEL (SPA-870, StressGen Biotechnologies) at 1:1,000 dilution, and secondary anti-rabbit or anti-mouse alkaline phosphatase conjugates (S373B or S372B, Promega) at 1:5,000 dilution.

Techniques: Recombinant, Purification, Chromatography, SDS Page, Staining, Western Blot, Filtration

A stable interaction between E. coli chaperones and VP1 inhibits calcium-mediated assembly. (A) Purified proteins YDJ-1, DnaK, and VP1 + VP3 analyzed by SDS/PAGE and Coomassie blue staining. (B) Anti-VP1 (I58) (7, 22) coimmunoprecipitation of purified proteins (YDJ-1 at 0.5× molar concentration, DnaK at 4× molar concentration, and VP1 + VP3 at 1× molar concentration) incubated without treatment (No trt), which is incubated briefly in ATP, followed by either ATP, excess ADP, or apyrase; or incubation of YDJ-1 and DnaK in the absence of VP1 + VP3 (No VP1 + VP3). (C-G) Purified pentamers of recombinant VP1 + VP3 without chaperones (C) or with copurified E. coli chaperones (G), in dissociating buffer visualized by negative stain and TEM. (D-F and H-J) In vitro assembly reactions of VP1 + VP3 pentamers without (D-F) or with (H-J) copurified chaperones, after dialysis into indicated calcium buffers, and visualized by negative stain and TEM. (Scale bar, 50 nm.) (K) Quantitation of the mean number of 50-nm particles per grid square (±SEM, n = 3) from the in vitro assembly reactions shown in C-J.

Journal:

Article Title: Chaperone-mediated in vitro assembly of Polyomavirus capsids

doi: 10.1073/pnas.1832245100

Figure Lengend Snippet: A stable interaction between E. coli chaperones and VP1 inhibits calcium-mediated assembly. (A) Purified proteins YDJ-1, DnaK, and VP1 + VP3 analyzed by SDS/PAGE and Coomassie blue staining. (B) Anti-VP1 (I58) (7, 22) coimmunoprecipitation of purified proteins (YDJ-1 at 0.5× molar concentration, DnaK at 4× molar concentration, and VP1 + VP3 at 1× molar concentration) incubated without treatment (No trt), which is incubated briefly in ATP, followed by either ATP, excess ADP, or apyrase; or incubation of YDJ-1 and DnaK in the absence of VP1 + VP3 (No VP1 + VP3). (C-G) Purified pentamers of recombinant VP1 + VP3 without chaperones (C) or with copurified E. coli chaperones (G), in dissociating buffer visualized by negative stain and TEM. (D-F and H-J) In vitro assembly reactions of VP1 + VP3 pentamers without (D-F) or with (H-J) copurified chaperones, after dialysis into indicated calcium buffers, and visualized by negative stain and TEM. (Scale bar, 50 nm.) (K) Quantitation of the mean number of 50-nm particles per grid square (±SEM, n = 3) from the in vitro assembly reactions shown in C-J.

Article Snippet: The membranes were blotted by using primary antibodies for VP1 (I58) ( 7 , 22 ), VP3 (482) ( 7 , 22 ), DnaK (AXL623, Accurate Chemical and Scientific, Westbury, NY), DnaJ (SPA-410, StressGen Biotechnologies), GrpE (SPA-240, StressGen Biotechnologies), and GroEL (SPA-870, StressGen Biotechnologies) at 1:1,000 dilution, and secondary anti-rabbit or anti-mouse alkaline phosphatase conjugates (S373B or S372B, Promega) at 1:5,000 dilution.

Techniques: Purification, SDS Page, Staining, Concentration Assay, Incubation, Recombinant, In Vitro, Quantitation Assay

E. coli chaperones DnaK, DnaJ, and GrpE assemble capsid proteins in vitro. (A-H) In vitro assembly reactions of VP1 + VP3 pentamers without (A-D) or with (E-H) copurified chaperones dialyzed into indicated dissociation buffers and visualized by negative stain and TEM. (I-K) In vitro assembly reactions of VP1 + VP3 pentamers at 1× molar concentration in dissociating buffer with ATP, using no chaperones (I), a reconstituted chaperone system with purified DnaK (0.5×), DnaJ (0.05×), and GrpE (0.05×)(J), or a reconstituted chaperone system with purified DnaK (0.5×), DnaJ (0.05×), GrpE (0.05×), and GroELS (1×) visualized by negative stain and TEM. (Scale bar, 50 nm.) (L) Quantitation of the mean number of 55-nm particles per grid square (±SEM, n = 3) from the in vitro assembly reactions shown in A-K.

Journal:

Article Title: Chaperone-mediated in vitro assembly of Polyomavirus capsids

doi: 10.1073/pnas.1832245100

Figure Lengend Snippet: E. coli chaperones DnaK, DnaJ, and GrpE assemble capsid proteins in vitro. (A-H) In vitro assembly reactions of VP1 + VP3 pentamers without (A-D) or with (E-H) copurified chaperones dialyzed into indicated dissociation buffers and visualized by negative stain and TEM. (I-K) In vitro assembly reactions of VP1 + VP3 pentamers at 1× molar concentration in dissociating buffer with ATP, using no chaperones (I), a reconstituted chaperone system with purified DnaK (0.5×), DnaJ (0.05×), and GrpE (0.05×)(J), or a reconstituted chaperone system with purified DnaK (0.5×), DnaJ (0.05×), GrpE (0.05×), and GroELS (1×) visualized by negative stain and TEM. (Scale bar, 50 nm.) (L) Quantitation of the mean number of 55-nm particles per grid square (±SEM, n = 3) from the in vitro assembly reactions shown in A-K.

Article Snippet: The membranes were blotted by using primary antibodies for VP1 (I58) ( 7 , 22 ), VP3 (482) ( 7 , 22 ), DnaK (AXL623, Accurate Chemical and Scientific, Westbury, NY), DnaJ (SPA-410, StressGen Biotechnologies), GrpE (SPA-240, StressGen Biotechnologies), and GroEL (SPA-870, StressGen Biotechnologies) at 1:1,000 dilution, and secondary anti-rabbit or anti-mouse alkaline phosphatase conjugates (S373B or S372B, Promega) at 1:5,000 dilution.

Techniques: In Vitro, Staining, Concentration Assay, Purification, Quantitation Assay

Capsids assembled by chaperones in vitro are uniform. (A-D) Negative stain and TEM of calcium assembly reaction (A), chaperone assembly reaction (B), VP1 VLPs (C), and polyoma virions (D). (Scale bar, 50 nm.) (E) Size polymorphism, based on 50 random assembled particles for the reactions shown in A-D.

Journal:

Article Title: Chaperone-mediated in vitro assembly of Polyomavirus capsids

doi: 10.1073/pnas.1832245100

Figure Lengend Snippet: Capsids assembled by chaperones in vitro are uniform. (A-D) Negative stain and TEM of calcium assembly reaction (A), chaperone assembly reaction (B), VP1 VLPs (C), and polyoma virions (D). (Scale bar, 50 nm.) (E) Size polymorphism, based on 50 random assembled particles for the reactions shown in A-D.

Article Snippet: The membranes were blotted by using primary antibodies for VP1 (I58) ( 7 , 22 ), VP3 (482) ( 7 , 22 ), DnaK (AXL623, Accurate Chemical and Scientific, Westbury, NY), DnaJ (SPA-410, StressGen Biotechnologies), GrpE (SPA-240, StressGen Biotechnologies), and GroEL (SPA-870, StressGen Biotechnologies) at 1:1,000 dilution, and secondary anti-rabbit or anti-mouse alkaline phosphatase conjugates (S373B or S372B, Promega) at 1:5,000 dilution.

Techniques: In Vitro, Staining

Mammalian hsc70 requires the J-domain of large T antigen to assemble capsid proteins in vitro.(A-C) In vitro assembly reactions of purified recombinant SV40 capsid proteins VP1 + VP3 at 1× molar concentration with mammalian hsc70 (1×) (A), mammalian hsc70 (1×) + LgT (at 0.1× for the J-domain) (B), or mammalian hsc70 (1×) + LgT D44N, a J-domain mutant (0.1×)(C), visualized by negative stain and TEM. (Scale bar, 50 nm.) (D) Quantitation of the mean number of 50-nm particles per grid square (±SEM, n = 10) from the in vitro assembly reactions shown in A-C.

Journal:

Article Title: Chaperone-mediated in vitro assembly of Polyomavirus capsids

doi: 10.1073/pnas.1832245100

Figure Lengend Snippet: Mammalian hsc70 requires the J-domain of large T antigen to assemble capsid proteins in vitro.(A-C) In vitro assembly reactions of purified recombinant SV40 capsid proteins VP1 + VP3 at 1× molar concentration with mammalian hsc70 (1×) (A), mammalian hsc70 (1×) + LgT (at 0.1× for the J-domain) (B), or mammalian hsc70 (1×) + LgT D44N, a J-domain mutant (0.1×)(C), visualized by negative stain and TEM. (Scale bar, 50 nm.) (D) Quantitation of the mean number of 50-nm particles per grid square (±SEM, n = 10) from the in vitro assembly reactions shown in A-C.

Article Snippet: The membranes were blotted by using primary antibodies for VP1 (I58) ( 7 , 22 ), VP3 (482) ( 7 , 22 ), DnaK (AXL623, Accurate Chemical and Scientific, Westbury, NY), DnaJ (SPA-410, StressGen Biotechnologies), GrpE (SPA-240, StressGen Biotechnologies), and GroEL (SPA-870, StressGen Biotechnologies) at 1:1,000 dilution, and secondary anti-rabbit or anti-mouse alkaline phosphatase conjugates (S373B or S372B, Promega) at 1:5,000 dilution.

Techniques: In Vitro, Purification, Recombinant, Concentration Assay, Mutagenesis, Staining, Quantitation Assay