mouse anti v5 Search Results


mouse anti v5  (Sino Biological)
94
Sino Biological mouse anti v5
Mouse Anti V5, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti v5 - by Bioz Stars, 2026-03
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anti v5 antibody  (Bio-Rad)
96
Bio-Rad anti v5 antibody
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Anti V5 Antibody, 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
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Average 96 stars, based on 1 article reviews
anti v5 antibody - by Bioz Stars, 2026-03
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mouse anti v5 tag antibody  (Cusabio)
92
Cusabio mouse anti v5 tag antibody
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Mouse Anti V5 Tag Antibody, supplied by Cusabio, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 1 article reviews
mouse anti v5 tag antibody - by Bioz Stars, 2026-03
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anti mouse antibodies  (Boster Bio)
92
Boster Bio anti mouse antibodies
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Anti Mouse Antibodies, 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
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Average 92 stars, based on 1 article reviews
anti mouse antibodies - by Bioz Stars, 2026-03
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agarose-conjugated anti-v5-tag beads  (FUJIFILM)
90
FUJIFILM agarose-conjugated anti-v5-tag beads
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Agarose Conjugated Anti V5 Tag Beads, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti-v5 monoclonal antibody  (ICN Pharmaceuticals)
90
ICN Pharmaceuticals mouse anti-v5 monoclonal antibody
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Mouse Anti V5 Monoclonal Antibody, supplied by ICN Pharmaceuticals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
mouse anti-v5 monoclonal antibody - by Bioz Stars, 2026-03
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hrp-labeled mouse anti-v5 tag  (Nacalai)
90
Nacalai hrp-labeled mouse anti-v5 tag
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Hrp Labeled Mouse Anti V5 Tag, supplied by Nacalai, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti-v5-tag mab mouse antibody  (LabForce AG)
90
LabForce AG anti-v5-tag mab mouse antibody
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Anti V5 Tag Mab Mouse Antibody, supplied by LabForce AG, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rabbit anti-v5  (Huabio Inc)
90
Huabio Inc rabbit anti-v5
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Rabbit Anti V5, supplied by Huabio Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti-v5  (Abnova)
90
Abnova mouse anti-v5
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Mouse Anti V5, supplied by Abnova, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti-v5 tag mouse monoclonal antibody abt2170  (Abbkine Inc)
90
Abbkine Inc anti-v5 tag mouse monoclonal antibody abt2170
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Anti V5 Tag Mouse Monoclonal Antibody Abt2170, supplied by Abbkine Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti-v5 asj-10004-100  (Nordic BioSite)
90
Nordic BioSite mouse anti-v5 asj-10004-100
Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by <t>Brn1-V5.</t> All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.
Mouse Anti V5 Asj 10004 100, supplied by Nordic BioSite, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by Brn1-V5. All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.

Journal: bioRxiv

Article Title: Condensin chromatin association is regulated by SMC head and hinge engagement and phosphorylation

doi: 10.1101/2025.11.17.688780

Figure Lengend Snippet: Expression of inducible Smc2 mutants created by conditional protein exchange. A) Schematic view of budding yeast condensin, illustrating the relative locations of each Smc2 mutation. Engagement of ATP-bound head domains triggers ATP hydrolysis, leading to their disengagement. The K38I and D1112A mutations are predicted to block binding of ATP to their respective pockets. The E113Q mutation is predicted to slow down the rate of ATP hydrolysis, while R58A is predicted to disrupt DNA dependent ATP hydrolysis. The S1085R mutation is predicted to disrupt head-head interactions. B) Within the hinge region of Smc2, we designed two mutations to specifically disrupt either of the two interfaces made with Smc4: hinge interface 1, L665R; hinge interface 2, L567K. Inset panels show additional details for how each single point mutant is predicted to generate a series of steric clashes (red circles) incompatible with hetero-dimerization of the hinge. Key amino acids of Smc2 and Smc4 are labelled in plain and italic text respectively. Figures were generated using MacPyMOL. C) Conditional protein exchange system for smc2 mutations. Under the permissive conditions (2% raffinose, 25°C) functional degron and HA tagged protein is expressed. Under the restrictive conditions (+2% galactose, + doxycycline 37°C), the functional degron protein is degraded and the exogenous HA tagged protein is expressed from a GAL1 promoter. D) Spot test of viability following conditional protein exchange for the different smc2 mutants. E) Condensin complexes generated following expression of different smc2 mutants. Following conditional protein exchange, in vivo condensin complexes were immuno-precipitated and the isolated complexes analyzed by MS/MS as described in the Methods. The signal from several peptides derived from each protein was quantitated by MS/MS and then normalized to the quantity of peptides from the Brn1 subunit. This provides a measure of the relative quantity of each subunit immuno-precipitated by Brn1-V5. All experiments are the average of two independent experiments and the standard deviation of the experiment shown by the error bar.

Article Snippet: Anti-V5 antibody (mouse monoclonal MCA1360, abD Serotec) used at 1:1000 Concentration in Western.

Techniques: Expressing, Mutagenesis, Blocking Assay, Binding Assay, Generated, Functional Assay, Spot Test, In Vivo, Isolation, Tandem Mass Spectroscopy, Derivative Assay, Standard Deviation

Chromatin association of condensin following expression of smc2 enzymatic mutations. Conditional expression depletion strains were arrested in G1 and endogenous Smc2 degraded and the indicated version of exogenous Smc2 expressed. Cells were then released from G1 into restrictive medium containing nocodazole. After 2 h, cells were harvested, and Brn1-V5 levels at the indicated sites analyzed by ChIP-qPCR. The average of at least three experimental repeats (qPCR performed in triplicate in each case) is shown with error bars. Enrichments are grouped according to function,

Journal: bioRxiv

Article Title: Condensin chromatin association is regulated by SMC head and hinge engagement and phosphorylation

doi: 10.1101/2025.11.17.688780

Figure Lengend Snippet: Chromatin association of condensin following expression of smc2 enzymatic mutations. Conditional expression depletion strains were arrested in G1 and endogenous Smc2 degraded and the indicated version of exogenous Smc2 expressed. Cells were then released from G1 into restrictive medium containing nocodazole. After 2 h, cells were harvested, and Brn1-V5 levels at the indicated sites analyzed by ChIP-qPCR. The average of at least three experimental repeats (qPCR performed in triplicate in each case) is shown with error bars. Enrichments are grouped according to function,

Article Snippet: Anti-V5 antibody (mouse monoclonal MCA1360, abD Serotec) used at 1:1000 Concentration in Western.

Techniques: Expressing, ChIP-qPCR

Effects of phosphorylation defective condensin subunits on chromatin association. Strains expressing the defined phosphorylation mutants of A) Smc4- smc4-10A , B) Brn1- brn1-570 , C) Ycs4 – ycs4-543 D) Ycg1, ycg1-521 were released from G1 into medium containing nocodazole at 37°C. After 2 h, cells were harvested, and Brn1-V5 levels at the indicated sites analyzed by ChIP-qPCR. The average of at least three experimental repeats (qPCR performed in triplicate in each case) is shown with error bars.

Journal: bioRxiv

Article Title: Condensin chromatin association is regulated by SMC head and hinge engagement and phosphorylation

doi: 10.1101/2025.11.17.688780

Figure Lengend Snippet: Effects of phosphorylation defective condensin subunits on chromatin association. Strains expressing the defined phosphorylation mutants of A) Smc4- smc4-10A , B) Brn1- brn1-570 , C) Ycs4 – ycs4-543 D) Ycg1, ycg1-521 were released from G1 into medium containing nocodazole at 37°C. After 2 h, cells were harvested, and Brn1-V5 levels at the indicated sites analyzed by ChIP-qPCR. The average of at least three experimental repeats (qPCR performed in triplicate in each case) is shown with error bars.

Article Snippet: Anti-V5 antibody (mouse monoclonal MCA1360, abD Serotec) used at 1:1000 Concentration in Western.

Techniques: Phospho-proteomics, Expressing, ChIP-qPCR

Requirement for Ipl1 and Cdc5 for condensin chromatin association and complex stability. Either A) ipl1-321 , B) cdc5-10 C) cdc5-99 cells were released from G1 into medium containing nocodazole at 37°C. After 2 h, cells were harvested, and Brn1-V5 levels at the indicated sites analyzed by ChIP-qPCR. The average of at least three experimental repeats (qPCR performed in triplicate in each case) is shown with error bars.

Journal: bioRxiv

Article Title: Condensin chromatin association is regulated by SMC head and hinge engagement and phosphorylation

doi: 10.1101/2025.11.17.688780

Figure Lengend Snippet: Requirement for Ipl1 and Cdc5 for condensin chromatin association and complex stability. Either A) ipl1-321 , B) cdc5-10 C) cdc5-99 cells were released from G1 into medium containing nocodazole at 37°C. After 2 h, cells were harvested, and Brn1-V5 levels at the indicated sites analyzed by ChIP-qPCR. The average of at least three experimental repeats (qPCR performed in triplicate in each case) is shown with error bars.

Article Snippet: Anti-V5 antibody (mouse monoclonal MCA1360, abD Serotec) used at 1:1000 Concentration in Western.

Techniques: ChIP-qPCR