5 ml packed affigel-10 agarose resin Search Results


affigel 10  (Bio-Rad)
99
Bio-Rad affigel 10
Affigel 10, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/5+ml+packed+affigel-10+agarose+resin/Affi-Gel+10+Gel/pmc03024902-34-10-12
Average 99 stars, based on 1 article reviews
affigel 10 - by Bioz Stars, 2026-10
99/100 stars
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anti tnp conjugated affigel 10  (Bio-Rad)
94
Bio-Rad anti tnp conjugated affigel 10
Anti Tnp Conjugated Affigel 10, supplied by Bio-Rad, 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/5+ml+packed+affigel-10+agarose+resin/Rabbit+anti+Mouse+IgG/pm10694273-34-12-19
Average 94 stars, based on 1 article reviews
anti tnp conjugated affigel 10 - by Bioz Stars, 2026-10
94/100 stars
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anti human β 2 gpi igg  (Bio-Rad)
96
Bio-Rad anti human β 2 gpi igg
Anti Human β 2 Gpi Igg, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/5+ml+packed+affigel-10+agarose+resin/Human+anti+Human+IgG/pmc02965030-74-4-13
Average 96 stars, based on 1 article reviews
anti human β 2 gpi igg - by Bioz Stars, 2026-10
96/100 stars
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bovine serum albumin bsa  (Bio-Rad)
96
Bio-Rad bovine serum albumin bsa
Protein-affinity chromatography was performed using microcolumns containing immobilized <t>RNAPII,</t> <t>RAP74,</t> RAP30, TFIIE56, TFIIE34, TFIIB, TBP, and <t>BSA.</t> A volume of 50 μl of nTFIIA (100 ng of α) was chromatographed through each column. The flowthrough was collected in each case. The columns were eluted with 50 μl of buffer containing increasing amounts of NaCl (e.g. 0.1, 0.3, and 0.5 M). The fractions were analyzed using SDS-PAGE and compared with the input (I). The positions of the nTFIIA subunits and a contaminant polypeptide of the TFIIA preparation that served as negative control are indicated. In each case, a diagram showing the relative intensities of both TFIIAα and a contaminant band (negative control) in the various fractions is shown.
Bovine Serum Albumin Bsa, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/5+ml+packed+affigel-10+agarose+resin/Quick+Start+Bovine+Serum+Albumin+Standard/pmc04492724-63-12-21
Average 96 stars, based on 1 article reviews
bovine serum albumin bsa - by Bioz Stars, 2026-10
96/100 stars
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Image Search Results


Protein-affinity chromatography was performed using microcolumns containing immobilized RNAPII, RAP74, RAP30, TFIIE56, TFIIE34, TFIIB, TBP, and BSA. A volume of 50 μl of nTFIIA (100 ng of α) was chromatographed through each column. The flowthrough was collected in each case. The columns were eluted with 50 μl of buffer containing increasing amounts of NaCl (e.g. 0.1, 0.3, and 0.5 M). The fractions were analyzed using SDS-PAGE and compared with the input (I). The positions of the nTFIIA subunits and a contaminant polypeptide of the TFIIA preparation that served as negative control are indicated. In each case, a diagram showing the relative intensities of both TFIIAα and a contaminant band (negative control) in the various fractions is shown.

Journal: The Journal of biological chemistry

Article Title: Structural and Functional Interactions of Transcription Factor (TF) IIA with TFIIE and TFIIF in Transcription Initiation by RNA Polymerase II *

doi: 10.1074/jbc.M106422200

Figure Lengend Snippet: Protein-affinity chromatography was performed using microcolumns containing immobilized RNAPII, RAP74, RAP30, TFIIE56, TFIIE34, TFIIB, TBP, and BSA. A volume of 50 μl of nTFIIA (100 ng of α) was chromatographed through each column. The flowthrough was collected in each case. The columns were eluted with 50 μl of buffer containing increasing amounts of NaCl (e.g. 0.1, 0.3, and 0.5 M). The fractions were analyzed using SDS-PAGE and compared with the input (I). The positions of the nTFIIA subunits and a contaminant polypeptide of the TFIIA preparation that served as negative control are indicated. In each case, a diagram showing the relative intensities of both TFIIAα and a contaminant band (negative control) in the various fractions is shown.

Article Snippet: RAP74 wt, RAP74 deletion mutants, RAP30, TFIIE34, TFIIE56, RNAPII, TFIIB, TBP, and bovine serum albumin (BSA) were immobilized on Affigel 10 (Bio-Rad) at a concentration of 1 to 5 mg/ml resin.

Techniques: Affinity Chromatography, SDS Page, Negative Control

Protein-affinity chromatography was performed using microcolumns containing immobilized RAP74, TFIIE34, and TFIIE56. A volume of 50 μl containing 200 ng of TFIIAα/β and TFIIAγ was chromatographed through each column. Fractions were collected and analyzed as in Fig. 2. The positions of α/β, γ, and BSA (as an internal negative control) are indicated.

Journal: The Journal of biological chemistry

Article Title: Structural and Functional Interactions of Transcription Factor (TF) IIA with TFIIE and TFIIF in Transcription Initiation by RNA Polymerase II *

doi: 10.1074/jbc.M106422200

Figure Lengend Snippet: Protein-affinity chromatography was performed using microcolumns containing immobilized RAP74, TFIIE34, and TFIIE56. A volume of 50 μl containing 200 ng of TFIIAα/β and TFIIAγ was chromatographed through each column. Fractions were collected and analyzed as in Fig. 2. The positions of α/β, γ, and BSA (as an internal negative control) are indicated.

Article Snippet: RAP74 wt, RAP74 deletion mutants, RAP30, TFIIE34, TFIIE56, RNAPII, TFIIB, TBP, and bovine serum albumin (BSA) were immobilized on Affigel 10 (Bio-Rad) at a concentration of 1 to 5 mg/ml resin.

Techniques: Affinity Chromatography, Negative Control

A, protein affinity chromatography was performed using columns containing immobilized RAP74 fragments (wild type or deletions mutants). A volume of 50 μl containing 200 ng of TFIIAα/β was chromatographed through each column. Fractions were collected and analyzed as in Fig. 2. The positions of TFIIAα/β and BSA (as an internal negative control) are indicated. B, summary of the interactions between the RAP74 deletion mutants and TFIIA. The various domains of RAP74 are indicated in the top part. The two TFIIA-binding domains of RAP74 are deduced from our analysis.

Journal: The Journal of biological chemistry

Article Title: Structural and Functional Interactions of Transcription Factor (TF) IIA with TFIIE and TFIIF in Transcription Initiation by RNA Polymerase II *

doi: 10.1074/jbc.M106422200

Figure Lengend Snippet: A, protein affinity chromatography was performed using columns containing immobilized RAP74 fragments (wild type or deletions mutants). A volume of 50 μl containing 200 ng of TFIIAα/β was chromatographed through each column. Fractions were collected and analyzed as in Fig. 2. The positions of TFIIAα/β and BSA (as an internal negative control) are indicated. B, summary of the interactions between the RAP74 deletion mutants and TFIIA. The various domains of RAP74 are indicated in the top part. The two TFIIA-binding domains of RAP74 are deduced from our analysis.

Article Snippet: RAP74 wt, RAP74 deletion mutants, RAP30, TFIIE34, TFIIE56, RNAPII, TFIIB, TBP, and bovine serum albumin (BSA) were immobilized on Affigel 10 (Bio-Rad) at a concentration of 1 to 5 mg/ml resin.

Techniques: Affinity Chromatography, Negative Control, Binding Assay