nb100-1799 Search Results


93
Novus Biologicals sec16a
A-B. Permeabilized HeLa cells were either pre-incubated in a reaction buffer lacking nucleotides, cytosol or SAR1 proteins for 15 min at 32°C (rundown) or not (control). Subsequently, a full transport cocktail containing rat liver cytosol (RLC) and SAR1-GTP (hamster SAR1a-H79G, 5μg/220μL) were added as indicated. The reaction was carried out for 15 minutes at 32 ° C, the cells were washed, fixed and analyzed for Sec31(using a polyclonal anti Sec31A antibody, A .) or Sec24C ( B. ) at ERES as we described C. The intensity of Sec31A or Sec24C was quantified from 9 fields of cells (20-60 cells per field, each field represented by a circle) derived from 3 to 4 independent experiments. Controls were defined as 100 percent and results analyzed using two-tailed t-test. D. Control and rundown reactions were as described in A in the presence of SAR1-GTP and RLC. Fixed cells were processed for IF using anti Sec24C and Sec31A (monoclonal) antibodies as indicated. E. Permeabilized cells expressing Tac-gp25l (ER marker) were incubated under control or rundown conditions (as in A) with SAR1-GTP and RLC, fixed and stained for Sec13 (red) and Tac (green). F. Analysis of Sec31A recruitment to ERES (marked with anti <t>Sec16A</t> antibody) in permeabilized control or Sec16A-KD cells (staining control) supplemented with Sar1-GTP and RLC as in A was analyzed from 6 fields of cells per condition (circles) from two independent experiments using Pearson Correlation Coefficient (PCC) (shown with two tailed t-test) G. Cells expressing GFP-tagged Sec16A were permeabilized and incubated as in A with RLC and Sar1-GTP, fixed and stained for Sec24C (red). Arrows in inserts indicate juxtapose labeling of recruited Sec24C with ERES markers in control and rundown conditions . H. Reconstitution of COPII recruitment was conducted as described in A. The cells were fixed and labeled with antibodies to Sec31 (polyclonal) and Sec24C, further fixed and processed for EM ( , ). Bars are 5μm in A and 200nm in E. Arrows in E point to gold labeling of Sec24C or Sec31 at ERES as indicated.
Sec16a, supplied by Novus Biologicals, 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/result/sec16a/product/Novus Biologicals
Average 93 stars, based on 1 article reviews
sec16a - by Bioz Stars, 2026-06
93/100 stars
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90
Novus Biologicals rabbit anti sec16a
(A) NRK cells transfected with the indicated siRNA were labeled with anti-ALG-2, anti-sec31A, or <t>anti-sec16A</t> antibodies, a cy3-conjugated secondary antibody, and dapi. Maximum intensity projections from deconvolved widefield z-stacks of the ERES proteins are displayed in grayscale merged with the corresponding dapi panel. (B) Quantitation of 4–5 fields of ~10 random cells per field, for each condition. A consistent intensity threshold was used to automatically capture and count bright cytoplasmic objects. A T-test between the siControl and siPeflin group was performed for each labeled protein: ALG-2, N = 85, p = 0.0003; Sec31A, N = 79, p = 0.0001; Sec16A, N = 100, p = 0.866.
Rabbit Anti Sec16a, supplied by Novus Biologicals, 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/result/rabbit anti sec16a/product/Novus Biologicals
Average 90 stars, based on 1 article reviews
rabbit anti sec16a - by Bioz Stars, 2026-06
90/100 stars
  Buy from Supplier

Image Search Results


A-B. Permeabilized HeLa cells were either pre-incubated in a reaction buffer lacking nucleotides, cytosol or SAR1 proteins for 15 min at 32°C (rundown) or not (control). Subsequently, a full transport cocktail containing rat liver cytosol (RLC) and SAR1-GTP (hamster SAR1a-H79G, 5μg/220μL) were added as indicated. The reaction was carried out for 15 minutes at 32 ° C, the cells were washed, fixed and analyzed for Sec31(using a polyclonal anti Sec31A antibody, A .) or Sec24C ( B. ) at ERES as we described C. The intensity of Sec31A or Sec24C was quantified from 9 fields of cells (20-60 cells per field, each field represented by a circle) derived from 3 to 4 independent experiments. Controls were defined as 100 percent and results analyzed using two-tailed t-test. D. Control and rundown reactions were as described in A in the presence of SAR1-GTP and RLC. Fixed cells were processed for IF using anti Sec24C and Sec31A (monoclonal) antibodies as indicated. E. Permeabilized cells expressing Tac-gp25l (ER marker) were incubated under control or rundown conditions (as in A) with SAR1-GTP and RLC, fixed and stained for Sec13 (red) and Tac (green). F. Analysis of Sec31A recruitment to ERES (marked with anti Sec16A antibody) in permeabilized control or Sec16A-KD cells (staining control) supplemented with Sar1-GTP and RLC as in A was analyzed from 6 fields of cells per condition (circles) from two independent experiments using Pearson Correlation Coefficient (PCC) (shown with two tailed t-test) G. Cells expressing GFP-tagged Sec16A were permeabilized and incubated as in A with RLC and Sar1-GTP, fixed and stained for Sec24C (red). Arrows in inserts indicate juxtapose labeling of recruited Sec24C with ERES markers in control and rundown conditions . H. Reconstitution of COPII recruitment was conducted as described in A. The cells were fixed and labeled with antibodies to Sec31 (polyclonal) and Sec24C, further fixed and processed for EM ( , ). Bars are 5μm in A and 200nm in E. Arrows in E point to gold labeling of Sec24C or Sec31 at ERES as indicated.

Journal: bioRxiv

Article Title: p125A (Sec23ip) couples COPII coat assembly with donor-acceptor membrane organization to facilitate tunnel-based traffic

doi: 10.1101/2025.05.07.652703

Figure Lengend Snippet: A-B. Permeabilized HeLa cells were either pre-incubated in a reaction buffer lacking nucleotides, cytosol or SAR1 proteins for 15 min at 32°C (rundown) or not (control). Subsequently, a full transport cocktail containing rat liver cytosol (RLC) and SAR1-GTP (hamster SAR1a-H79G, 5μg/220μL) were added as indicated. The reaction was carried out for 15 minutes at 32 ° C, the cells were washed, fixed and analyzed for Sec31(using a polyclonal anti Sec31A antibody, A .) or Sec24C ( B. ) at ERES as we described C. The intensity of Sec31A or Sec24C was quantified from 9 fields of cells (20-60 cells per field, each field represented by a circle) derived from 3 to 4 independent experiments. Controls were defined as 100 percent and results analyzed using two-tailed t-test. D. Control and rundown reactions were as described in A in the presence of SAR1-GTP and RLC. Fixed cells were processed for IF using anti Sec24C and Sec31A (monoclonal) antibodies as indicated. E. Permeabilized cells expressing Tac-gp25l (ER marker) were incubated under control or rundown conditions (as in A) with SAR1-GTP and RLC, fixed and stained for Sec13 (red) and Tac (green). F. Analysis of Sec31A recruitment to ERES (marked with anti Sec16A antibody) in permeabilized control or Sec16A-KD cells (staining control) supplemented with Sar1-GTP and RLC as in A was analyzed from 6 fields of cells per condition (circles) from two independent experiments using Pearson Correlation Coefficient (PCC) (shown with two tailed t-test) G. Cells expressing GFP-tagged Sec16A were permeabilized and incubated as in A with RLC and Sar1-GTP, fixed and stained for Sec24C (red). Arrows in inserts indicate juxtapose labeling of recruited Sec24C with ERES markers in control and rundown conditions . H. Reconstitution of COPII recruitment was conducted as described in A. The cells were fixed and labeled with antibodies to Sec31 (polyclonal) and Sec24C, further fixed and processed for EM ( , ). Bars are 5μm in A and 200nm in E. Arrows in E point to gold labeling of Sec24C or Sec31 at ERES as indicated.

Article Snippet: Anti FLAG antibodies (M2, F1804 Sigma), antibodies to Sec16A, Novus Biologicals (NB100-1799), antibodies to p97/VCP, RDI research diagnostics (RDI PR065278), antibodies to GFP, Polysciences Inc. (24240) and Proteintech (66002-1-ig).

Techniques: Incubation, Control, Derivative Assay, Two Tailed Test, Bioprocessing, Expressing, Marker, Staining, Labeling

Active Rab1 or Sec16A depletion do not rescue the linkage between COPII inner and outer layers. A. Cells were transfected with construct expressing Flag-Rab1a-GTP(Q70L), permeabilized and subjected to rundown and COPII recruitment as in , monitoring Sec13 (red) and Rab1-GTP (anti Flag, green). Note that Rab1a-GTP is retained in cells and occasionally preserves Sec13 at the sites. B. Sec16A was depleted using siRNA and analyzed by western blot with Sec31A serving as a control as indicated (triplicates of control or KD samples are shown in the left panel). Depleted cells were permeabilized and subjected to rundown pre-incubation. Subsequently, control or Sec16A depleted cells were supplemented with RLC and SAR1-GTP (as in ). The recruitment of the coat outer layer (Sec31A, monoclonal antibody) and Sec16A localization was determined by IF. Bars are 5 μm.

Journal: bioRxiv

Article Title: p125A (Sec23ip) couples COPII coat assembly with donor-acceptor membrane organization to facilitate tunnel-based traffic

doi: 10.1101/2025.05.07.652703

Figure Lengend Snippet: Active Rab1 or Sec16A depletion do not rescue the linkage between COPII inner and outer layers. A. Cells were transfected with construct expressing Flag-Rab1a-GTP(Q70L), permeabilized and subjected to rundown and COPII recruitment as in , monitoring Sec13 (red) and Rab1-GTP (anti Flag, green). Note that Rab1a-GTP is retained in cells and occasionally preserves Sec13 at the sites. B. Sec16A was depleted using siRNA and analyzed by western blot with Sec31A serving as a control as indicated (triplicates of control or KD samples are shown in the left panel). Depleted cells were permeabilized and subjected to rundown pre-incubation. Subsequently, control or Sec16A depleted cells were supplemented with RLC and SAR1-GTP (as in ). The recruitment of the coat outer layer (Sec31A, monoclonal antibody) and Sec16A localization was determined by IF. Bars are 5 μm.

Article Snippet: Anti FLAG antibodies (M2, F1804 Sigma), antibodies to Sec16A, Novus Biologicals (NB100-1799), antibodies to p97/VCP, RDI research diagnostics (RDI PR065278), antibodies to GFP, Polysciences Inc. (24240) and Proteintech (66002-1-ig).

Techniques: Transfection, Construct, Expressing, Western Blot, Control, Incubation

(A) NRK cells transfected with the indicated siRNA were labeled with anti-ALG-2, anti-sec31A, or anti-sec16A antibodies, a cy3-conjugated secondary antibody, and dapi. Maximum intensity projections from deconvolved widefield z-stacks of the ERES proteins are displayed in grayscale merged with the corresponding dapi panel. (B) Quantitation of 4–5 fields of ~10 random cells per field, for each condition. A consistent intensity threshold was used to automatically capture and count bright cytoplasmic objects. A T-test between the siControl and siPeflin group was performed for each labeled protein: ALG-2, N = 85, p = 0.0003; Sec31A, N = 79, p = 0.0001; Sec16A, N = 100, p = 0.866.

Journal: PLoS ONE

Article Title: Penta-EF-Hand Protein Peflin Is a Negative Regulator of ER-To-Golgi Transport

doi: 10.1371/journal.pone.0157227

Figure Lengend Snippet: (A) NRK cells transfected with the indicated siRNA were labeled with anti-ALG-2, anti-sec31A, or anti-sec16A antibodies, a cy3-conjugated secondary antibody, and dapi. Maximum intensity projections from deconvolved widefield z-stacks of the ERES proteins are displayed in grayscale merged with the corresponding dapi panel. (B) Quantitation of 4–5 fields of ~10 random cells per field, for each condition. A consistent intensity threshold was used to automatically capture and count bright cytoplasmic objects. A T-test between the siControl and siPeflin group was performed for each labeled protein: ALG-2, N = 85, p = 0.0003; Sec31A, N = 79, p = 0.0001; Sec16A, N = 100, p = 0.866.

Article Snippet: Rabbit anti-sec16A (product NB100-1799) was from Novus Biologicals.

Techniques: Transfection, Labeling, Quantitation Assay