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ergic53 antibodies  (Oxford Instruments)


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    Oxford Instruments ergic53 antibodies
    Ergic53 Antibodies, supplied by Oxford Instruments, used in various techniques. Bioz Stars score: 99/100, based on 44185 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ergic53+antibodies/Imaris/pm40593538-582-12-17
    Average 99 stars, based on 44185 article reviews
    ergic53 antibodies - by Bioz Stars, 2026-09
    99/100 stars

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    Related Articles

    Staining:

    Article Title: TUG protein acts through a disordered region to organize the early secretory pathway
    Article Snippet: .. To quantify ERGIC53 surfaces, confocal images of MEFs stained using GM130 and ERGIC53 antibodies were segmented in Imaris after local background subtraction. ..

    Article Title: TUG protein acts through a disordered region to organize the early secretory pathway.
    Article Snippet: .. To quantify ERGIC53 surfaces, confocal images of MEFs stained using GM130 and ERGIC53 antibodies were segmented in Imaris after local background subtraction. ..

    Article Title: TUG protein acts through a disordered region to organize the early secretory pathway
    Article Snippet: .. To quantify ERGIC53 surfaces, confocal images of MEFs stained using GM130 and ERGIC53 antibodies were segmented in Imaris after local background subtraction. ..



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    Image Search Results


    A. Domain structure and O-GlcNAc sites of human Sec24D. B. CRISPR strategy to generate Sec24D knock-in cells. C. PCR genotyping of Sec24D WT , Sec24D T9A , and Sec24D S13A SW1353 single cell-derived clones, using primers depicted in B. D. Myc-6xHis tagged endogenous Sec24D was purified from Sec24D WT , Sec24D T9A , and Sec24D S13A cells by tandem myc IP and denaturing Ni-NTA affinity and analyzed by IB. E. Quantification of experiments depicted in D. Signal from O-GlcNAc blots of purified Sec24D was normalized to myc signal, and intensities relative to Sec24D WT were calculated (n = 3). Data were analyzed by one-way ANOVA with post hoc Tukey test. * p < 0.05; ** p < 0.01; ns: not significant. F. Myc-6xHis tagged endogenous Sec24D was purified from Sec24D WT , Sec24D T9A , and Sec24D S13A cells by tandem myc IP and denaturing Ni-NTA affinity at 0 or 5 minutes after collagen release and analyzed by IB. G. Quantification of experiments depicted in F. Signal from O-GlcNAc blots of purified Sec24D was normalized to myc signal, and intensities relative to time-zero were calculated (n = 8). Data were analyzed by Welch’s t -test. * p < 0.05. H. O-GlcNAcylated Sec24D was visualized by PLA in Sec24D WT , Sec24D T9A , and Sec24D S13A cells at 0 or 5 minutes after collagen release. Scale bars: 10 µm. I. Quantification of experiments depicted in H. Left: Total fluorescence intensity (FI) of PLA signal normalized to per-cell area (n = 3). Right: Total FI, normalized to cell area at time-zero (n = 3). Data were analyzed by two-way ANOVA with post hoc Tukey test. * p < 0.05; ** p < 0.01; **** p < 0.0001; ns: not significant. J. Parental SW1353, Sec24D WT , Sec24D T9A , and Sec24D S13A cells were analyzed by PLA for O-GlcNAcylated Sec24D (myc-MultiMab antibodies), and Sec31A or ERGIC53 was detected by IF. Scale bars: 10 µm. K. Quantification of experiments depicted in J. Mander’s overlap coefficients (MOCs) between PLA signals and Sec31A or ERGIC53 was calculated (N = 3). MOC data with Costes p value < 0.95 were deemed to be statistically indistinguishable from random overlap and are displayed as gray dots. One-way ANOVA with post-hoc Tukey test was conducted as statistical analysis. * p < 0.05; **** p < 0.0001; ns: not significant.

    Journal: bioRxiv

    Article Title: Dynamic regulation of the COPII interactome and collagen trafficking by site-specific glycosylation of Sec24D

    doi: 10.1101/2025.06.13.659590

    Figure Lengend Snippet: A. Domain structure and O-GlcNAc sites of human Sec24D. B. CRISPR strategy to generate Sec24D knock-in cells. C. PCR genotyping of Sec24D WT , Sec24D T9A , and Sec24D S13A SW1353 single cell-derived clones, using primers depicted in B. D. Myc-6xHis tagged endogenous Sec24D was purified from Sec24D WT , Sec24D T9A , and Sec24D S13A cells by tandem myc IP and denaturing Ni-NTA affinity and analyzed by IB. E. Quantification of experiments depicted in D. Signal from O-GlcNAc blots of purified Sec24D was normalized to myc signal, and intensities relative to Sec24D WT were calculated (n = 3). Data were analyzed by one-way ANOVA with post hoc Tukey test. * p < 0.05; ** p < 0.01; ns: not significant. F. Myc-6xHis tagged endogenous Sec24D was purified from Sec24D WT , Sec24D T9A , and Sec24D S13A cells by tandem myc IP and denaturing Ni-NTA affinity at 0 or 5 minutes after collagen release and analyzed by IB. G. Quantification of experiments depicted in F. Signal from O-GlcNAc blots of purified Sec24D was normalized to myc signal, and intensities relative to time-zero were calculated (n = 8). Data were analyzed by Welch’s t -test. * p < 0.05. H. O-GlcNAcylated Sec24D was visualized by PLA in Sec24D WT , Sec24D T9A , and Sec24D S13A cells at 0 or 5 minutes after collagen release. Scale bars: 10 µm. I. Quantification of experiments depicted in H. Left: Total fluorescence intensity (FI) of PLA signal normalized to per-cell area (n = 3). Right: Total FI, normalized to cell area at time-zero (n = 3). Data were analyzed by two-way ANOVA with post hoc Tukey test. * p < 0.05; ** p < 0.01; **** p < 0.0001; ns: not significant. J. Parental SW1353, Sec24D WT , Sec24D T9A , and Sec24D S13A cells were analyzed by PLA for O-GlcNAcylated Sec24D (myc-MultiMab antibodies), and Sec31A or ERGIC53 was detected by IF. Scale bars: 10 µm. K. Quantification of experiments depicted in J. Mander’s overlap coefficients (MOCs) between PLA signals and Sec31A or ERGIC53 was calculated (N = 3). MOC data with Costes p value < 0.95 were deemed to be statistically indistinguishable from random overlap and are displayed as gray dots. One-way ANOVA with post-hoc Tukey test was conducted as statistical analysis. * p < 0.05; **** p < 0.0001; ns: not significant.

    Article Snippet: The following antibodies were used: Rabbit anti-collagen I antiserum (LF-68) was a gift from L. Fisher, National Institute of Dental and Craniofacial Research; Rabbit monoclonal anti-Sec24D (D9M7L, #14687), Rabbit polyclonal anti-Sec23A (#8162), Rabbit MultiMab monoclonal mix anti-O-GlcNAc (#82332), Rabbit monoclonal anti-Calnexin (C5C9, #2679), Rabbit monoclonal anti-CD44 (E7K2Y, #37259), Rabbit monoclonal anti-IRS-1 (59G8, #2390), and Rabbit anti-HA (C29F4, #3724) from Cell Signaling Technology; Mouse anti-c-Myc (9E10, #626802), and Mouse anti-O-GlcNAc (RL2, #677902) from BioLegend; Mouse anti-O-GlcNAc (18B10.C7, #MA1-038) from ThermoFisher Scientific; Mouse anti-α-Tubulin (#T6074), Rabbit polyclonal anti-MIA3 (TANGO1) (#HPA055922), Rabbit polyclonal anti-Sec23IP (#HPA038403), and Rabbit polyclonal anti-SVIL (#HPA020138) from Sigma-Aldrich; Rat monoclonal anti-HA (3F10, #11867423001) from Roche; Rabbit polyclonal anti-Sec16A (#A300-648A), and Goat anti-myc tag antibody (#A190-104A) from Bethyl Laboratories; Mouse anti-Sec31A (32, #612351), and Mouse anti-GM130 (35, #610822) from BD Biosciences; Rabbit polyclonal anti-Sec13 (#A11613) from ABclonal; Rabbit polyclonal anti-Sec23B (#NBP2-20279) from Novus Biologicals; Rabbit monoclonal anti-Sec24D (EPR16089, #ab191566), Chicken anti-GFP (#ab13970), Rabbit monoclonal anti-LMAN1 (ERGIC53) antibody (EPR6979, #ab125006) and Rabbit monoclonal anti-MYOF (EPR18887, #ab178386) from Abcam; Mouse anti-Calnexin (2A2C6, #66903-1-Ig) from Proteintech; mouse anti-O-GlcNAc (CTD110.6, #sc-59623), and mouse anti-ERGIC53 (C-6, #sc-365158) from Santa Cruz Biotechnology; anti-procollagen I (PIP, #42024) from QED Bioscience; Goat horseradish peroxidase (HRP)-conjugated anti-mouse IgG (#1030-05), and Goat HRP-conjugated anti-rabbit IgG (#4030-05) from SouthernBiotech; Goat IRDye 800CW-conjugated anti-mouse IgG (#925-32210), and Goat IRDye 800CW-conjugated anti-rabbit IgG (#925-32211) from LI-COR; Goat Alexa Fluor 488-conjugated anti-mouse IgG (A-11001), Goat Alexa Fluor 488-conjugated anti-rabbit IgG (A-11008), Goat Alexa Fluor 488-conjugated anti-chicken IgY (A-11039), Goat Alexa Fluor 594-conjugated anti-mouse IgG (A-11005), Goat Alexa Fluor 594-conjugated anti-rabbit IgG (A-11012), Goat Alexa Fluor 647-conjugated anti-mouse IgG (A-21235), Goat Alexa Fluor 647-conjugated anti-rabbit IgG (A-32733), Goat Alexa Fluor Plus 647-conjugated anti-mouse IgG highly cross-adsorbed (A32728), Goat Alexa Fluor Plus 594-conjugated anti-rat IgG highly cross-adsorbed (A48264), Donkey Alexa Fluor 488-conjugated anti-mouse IgG (A-21202).

    Techniques: CRISPR, Knock-In, Derivative Assay, Clone Assay, Purification, Fluorescence

    A. Domain structure of MYOF. B. Sec24D WT , Sec24D T9A , and Sec24D S13A cells were analyzed by PLA for Sec24D-MYOF interaction (myc-MYOF antibodies) and Sec31A (left) or ERGIC53 (right) via IF. Scale bars: 10 µm. C. Line plots display the FIs of PLA and Sec31A (top) or ERGIC53 (bottom) signal along the inset arrow paths in B. D. From experiments depicted in B, MOCs between PLA and Sec31A (left) or PLA and ERGIC53 (right) were calculated (n = 3). Data were analyzed by unpaired Student’s or Welch’s t -test. MOC data with Costes p value < 0.95 were deemed to be statistically indistinguishable from random overlap and are displayed as gray dots. **** p < 0.0001. E. Control and MYOF-knockdown SW1353 cells were treated with 50 µg/ml sodium ascorbate for 5 h and then analyzed by IF. Scale bars: 10 µm. F. Quantification of experiments depicted in E. MFI of COL1A1 was measured and normalized to the control sample (n = 3). Data were analyzed by Welch’s t -test. **** p < 0.0001. G. Control and MYOF-knockdown SW1353 cells were incubated at 40 °C for 3 h, shifted to 32 °C plus 50 µg/ml sodium ascorbate and 100 µg/ml cycloheximide for the indicated times, and analyzed by IF. Scale bars: 10 µm. H. Quantification of experiments depicted in G. Percentage of cells with Golgi-localized COL1A1 in each sample was calculated (n = 3). Data were analyzed by two-way ANOVA with post hoc Sidak’s test. **** p < 0.0001. I. Control and MYOF-knockdown SW1353 cells expressing the E-cadherin RUSH system were incubated with 50 µM biotin and 100 µg/ml cycloheximide for the indicated times and analyzed by IF. Scale bars: 10 µm. J. Quantification of experiments depicted in I. Percentage of COL1A1 FI in the Golgi was calculated for each sample (n = 3). Data were analyzed by two-way ANOVA with post hoc Sidak’s test. ns: not significant. K. Quantification of experiments depicted in G at 15 min time-points. Left: Percentage of cells with large COL1A1 puncta (defined as ≥ 0.7 µm 2 size) was calculated for each sample (n = 3). Data were analyzed by unpaired Student’s t -test. Middle: Average size of COL1A1 puncta was calculated (n = 3). Data were analyzed by unpaired Student’s t -test. Right: Number of large COL1A1 puncta was calculated and normalized to cell area (n = 3). Data were analyzed by Welch’s t -test. ** p < 0.01; *** p < 0.001; **** p < 0.0001.

    Journal: bioRxiv

    Article Title: Dynamic regulation of the COPII interactome and collagen trafficking by site-specific glycosylation of Sec24D

    doi: 10.1101/2025.06.13.659590

    Figure Lengend Snippet: A. Domain structure of MYOF. B. Sec24D WT , Sec24D T9A , and Sec24D S13A cells were analyzed by PLA for Sec24D-MYOF interaction (myc-MYOF antibodies) and Sec31A (left) or ERGIC53 (right) via IF. Scale bars: 10 µm. C. Line plots display the FIs of PLA and Sec31A (top) or ERGIC53 (bottom) signal along the inset arrow paths in B. D. From experiments depicted in B, MOCs between PLA and Sec31A (left) or PLA and ERGIC53 (right) were calculated (n = 3). Data were analyzed by unpaired Student’s or Welch’s t -test. MOC data with Costes p value < 0.95 were deemed to be statistically indistinguishable from random overlap and are displayed as gray dots. **** p < 0.0001. E. Control and MYOF-knockdown SW1353 cells were treated with 50 µg/ml sodium ascorbate for 5 h and then analyzed by IF. Scale bars: 10 µm. F. Quantification of experiments depicted in E. MFI of COL1A1 was measured and normalized to the control sample (n = 3). Data were analyzed by Welch’s t -test. **** p < 0.0001. G. Control and MYOF-knockdown SW1353 cells were incubated at 40 °C for 3 h, shifted to 32 °C plus 50 µg/ml sodium ascorbate and 100 µg/ml cycloheximide for the indicated times, and analyzed by IF. Scale bars: 10 µm. H. Quantification of experiments depicted in G. Percentage of cells with Golgi-localized COL1A1 in each sample was calculated (n = 3). Data were analyzed by two-way ANOVA with post hoc Sidak’s test. **** p < 0.0001. I. Control and MYOF-knockdown SW1353 cells expressing the E-cadherin RUSH system were incubated with 50 µM biotin and 100 µg/ml cycloheximide for the indicated times and analyzed by IF. Scale bars: 10 µm. J. Quantification of experiments depicted in I. Percentage of COL1A1 FI in the Golgi was calculated for each sample (n = 3). Data were analyzed by two-way ANOVA with post hoc Sidak’s test. ns: not significant. K. Quantification of experiments depicted in G at 15 min time-points. Left: Percentage of cells with large COL1A1 puncta (defined as ≥ 0.7 µm 2 size) was calculated for each sample (n = 3). Data were analyzed by unpaired Student’s t -test. Middle: Average size of COL1A1 puncta was calculated (n = 3). Data were analyzed by unpaired Student’s t -test. Right: Number of large COL1A1 puncta was calculated and normalized to cell area (n = 3). Data were analyzed by Welch’s t -test. ** p < 0.01; *** p < 0.001; **** p < 0.0001.

    Article Snippet: The following antibodies were used: Rabbit anti-collagen I antiserum (LF-68) was a gift from L. Fisher, National Institute of Dental and Craniofacial Research; Rabbit monoclonal anti-Sec24D (D9M7L, #14687), Rabbit polyclonal anti-Sec23A (#8162), Rabbit MultiMab monoclonal mix anti-O-GlcNAc (#82332), Rabbit monoclonal anti-Calnexin (C5C9, #2679), Rabbit monoclonal anti-CD44 (E7K2Y, #37259), Rabbit monoclonal anti-IRS-1 (59G8, #2390), and Rabbit anti-HA (C29F4, #3724) from Cell Signaling Technology; Mouse anti-c-Myc (9E10, #626802), and Mouse anti-O-GlcNAc (RL2, #677902) from BioLegend; Mouse anti-O-GlcNAc (18B10.C7, #MA1-038) from ThermoFisher Scientific; Mouse anti-α-Tubulin (#T6074), Rabbit polyclonal anti-MIA3 (TANGO1) (#HPA055922), Rabbit polyclonal anti-Sec23IP (#HPA038403), and Rabbit polyclonal anti-SVIL (#HPA020138) from Sigma-Aldrich; Rat monoclonal anti-HA (3F10, #11867423001) from Roche; Rabbit polyclonal anti-Sec16A (#A300-648A), and Goat anti-myc tag antibody (#A190-104A) from Bethyl Laboratories; Mouse anti-Sec31A (32, #612351), and Mouse anti-GM130 (35, #610822) from BD Biosciences; Rabbit polyclonal anti-Sec13 (#A11613) from ABclonal; Rabbit polyclonal anti-Sec23B (#NBP2-20279) from Novus Biologicals; Rabbit monoclonal anti-Sec24D (EPR16089, #ab191566), Chicken anti-GFP (#ab13970), Rabbit monoclonal anti-LMAN1 (ERGIC53) antibody (EPR6979, #ab125006) and Rabbit monoclonal anti-MYOF (EPR18887, #ab178386) from Abcam; Mouse anti-Calnexin (2A2C6, #66903-1-Ig) from Proteintech; mouse anti-O-GlcNAc (CTD110.6, #sc-59623), and mouse anti-ERGIC53 (C-6, #sc-365158) from Santa Cruz Biotechnology; anti-procollagen I (PIP, #42024) from QED Bioscience; Goat horseradish peroxidase (HRP)-conjugated anti-mouse IgG (#1030-05), and Goat HRP-conjugated anti-rabbit IgG (#4030-05) from SouthernBiotech; Goat IRDye 800CW-conjugated anti-mouse IgG (#925-32210), and Goat IRDye 800CW-conjugated anti-rabbit IgG (#925-32211) from LI-COR; Goat Alexa Fluor 488-conjugated anti-mouse IgG (A-11001), Goat Alexa Fluor 488-conjugated anti-rabbit IgG (A-11008), Goat Alexa Fluor 488-conjugated anti-chicken IgY (A-11039), Goat Alexa Fluor 594-conjugated anti-mouse IgG (A-11005), Goat Alexa Fluor 594-conjugated anti-rabbit IgG (A-11012), Goat Alexa Fluor 647-conjugated anti-mouse IgG (A-21235), Goat Alexa Fluor 647-conjugated anti-rabbit IgG (A-32733), Goat Alexa Fluor Plus 647-conjugated anti-mouse IgG highly cross-adsorbed (A32728), Goat Alexa Fluor Plus 594-conjugated anti-rat IgG highly cross-adsorbed (A48264), Donkey Alexa Fluor 488-conjugated anti-mouse IgG (A-21202).

    Techniques: Control, Knockdown, Incubation, Expressing

    A. Control and MYOF-knockdown SW1353 cells were incubated at 40 °C for 3 h, shifted to 32 °C plus 50 µg/ml sodium ascorbate and 100 µg/ml cycloheximide for 15 min, and analyzed by IF. Scale bars: 10 µm. B. Control and MYOF-knockdown SW1353 cells were incubated at 40 °C for 3 h, shifted to 32 °C plus 50 µg/ml sodium ascorbate and 100 µg/ml cycloheximide for 15 min, and analyzed by IF. Scale bars: 10 µm. C. Quantification of experiments depicted in B. Line plots display the FIs of COL1A1 and ERGIC53 signal along the inset arrow paths. Dotted lines represent the remaining noise in the ERGIC53 channel after background subtraction. D. MYOF-knockdown SW1353 cells were transfected with empty vector (EV) or siRNA-resistant expression constructs for full-length (FL) or ΔC2A mutant HA-MYOF. Cells were incubated at 40°C for 3 h, shifted to 32 °C plus 50 µg/ml sodium ascorbate and 100 µg/ml cycloheximide for 15 min, and analyzed by IF. Scale bars: 10 µm. E. Quantification of experiments depicted in D. Percentage of cells with Golgi-localized COL1A1 was calculated for each sample (n = 5). Data were analyzed by one-way ANOVA with post hoc Tukey test. * p < 0.05; ns: not significant. F. Quantification of experiments depicted in D. Percentage of cells with large COL1A1 puncta was calculated for each sample (n = 5). Data were analyzed by one-way ANOVA with post hoc Tukey test. * p < 0.05; *** p < 0.001; ns: not significant.

    Journal: bioRxiv

    Article Title: Dynamic regulation of the COPII interactome and collagen trafficking by site-specific glycosylation of Sec24D

    doi: 10.1101/2025.06.13.659590

    Figure Lengend Snippet: A. Control and MYOF-knockdown SW1353 cells were incubated at 40 °C for 3 h, shifted to 32 °C plus 50 µg/ml sodium ascorbate and 100 µg/ml cycloheximide for 15 min, and analyzed by IF. Scale bars: 10 µm. B. Control and MYOF-knockdown SW1353 cells were incubated at 40 °C for 3 h, shifted to 32 °C plus 50 µg/ml sodium ascorbate and 100 µg/ml cycloheximide for 15 min, and analyzed by IF. Scale bars: 10 µm. C. Quantification of experiments depicted in B. Line plots display the FIs of COL1A1 and ERGIC53 signal along the inset arrow paths. Dotted lines represent the remaining noise in the ERGIC53 channel after background subtraction. D. MYOF-knockdown SW1353 cells were transfected with empty vector (EV) or siRNA-resistant expression constructs for full-length (FL) or ΔC2A mutant HA-MYOF. Cells were incubated at 40°C for 3 h, shifted to 32 °C plus 50 µg/ml sodium ascorbate and 100 µg/ml cycloheximide for 15 min, and analyzed by IF. Scale bars: 10 µm. E. Quantification of experiments depicted in D. Percentage of cells with Golgi-localized COL1A1 was calculated for each sample (n = 5). Data were analyzed by one-way ANOVA with post hoc Tukey test. * p < 0.05; ns: not significant. F. Quantification of experiments depicted in D. Percentage of cells with large COL1A1 puncta was calculated for each sample (n = 5). Data were analyzed by one-way ANOVA with post hoc Tukey test. * p < 0.05; *** p < 0.001; ns: not significant.

    Article Snippet: The following antibodies were used: Rabbit anti-collagen I antiserum (LF-68) was a gift from L. Fisher, National Institute of Dental and Craniofacial Research; Rabbit monoclonal anti-Sec24D (D9M7L, #14687), Rabbit polyclonal anti-Sec23A (#8162), Rabbit MultiMab monoclonal mix anti-O-GlcNAc (#82332), Rabbit monoclonal anti-Calnexin (C5C9, #2679), Rabbit monoclonal anti-CD44 (E7K2Y, #37259), Rabbit monoclonal anti-IRS-1 (59G8, #2390), and Rabbit anti-HA (C29F4, #3724) from Cell Signaling Technology; Mouse anti-c-Myc (9E10, #626802), and Mouse anti-O-GlcNAc (RL2, #677902) from BioLegend; Mouse anti-O-GlcNAc (18B10.C7, #MA1-038) from ThermoFisher Scientific; Mouse anti-α-Tubulin (#T6074), Rabbit polyclonal anti-MIA3 (TANGO1) (#HPA055922), Rabbit polyclonal anti-Sec23IP (#HPA038403), and Rabbit polyclonal anti-SVIL (#HPA020138) from Sigma-Aldrich; Rat monoclonal anti-HA (3F10, #11867423001) from Roche; Rabbit polyclonal anti-Sec16A (#A300-648A), and Goat anti-myc tag antibody (#A190-104A) from Bethyl Laboratories; Mouse anti-Sec31A (32, #612351), and Mouse anti-GM130 (35, #610822) from BD Biosciences; Rabbit polyclonal anti-Sec13 (#A11613) from ABclonal; Rabbit polyclonal anti-Sec23B (#NBP2-20279) from Novus Biologicals; Rabbit monoclonal anti-Sec24D (EPR16089, #ab191566), Chicken anti-GFP (#ab13970), Rabbit monoclonal anti-LMAN1 (ERGIC53) antibody (EPR6979, #ab125006) and Rabbit monoclonal anti-MYOF (EPR18887, #ab178386) from Abcam; Mouse anti-Calnexin (2A2C6, #66903-1-Ig) from Proteintech; mouse anti-O-GlcNAc (CTD110.6, #sc-59623), and mouse anti-ERGIC53 (C-6, #sc-365158) from Santa Cruz Biotechnology; anti-procollagen I (PIP, #42024) from QED Bioscience; Goat horseradish peroxidase (HRP)-conjugated anti-mouse IgG (#1030-05), and Goat HRP-conjugated anti-rabbit IgG (#4030-05) from SouthernBiotech; Goat IRDye 800CW-conjugated anti-mouse IgG (#925-32210), and Goat IRDye 800CW-conjugated anti-rabbit IgG (#925-32211) from LI-COR; Goat Alexa Fluor 488-conjugated anti-mouse IgG (A-11001), Goat Alexa Fluor 488-conjugated anti-rabbit IgG (A-11008), Goat Alexa Fluor 488-conjugated anti-chicken IgY (A-11039), Goat Alexa Fluor 594-conjugated anti-mouse IgG (A-11005), Goat Alexa Fluor 594-conjugated anti-rabbit IgG (A-11012), Goat Alexa Fluor 647-conjugated anti-mouse IgG (A-21235), Goat Alexa Fluor 647-conjugated anti-rabbit IgG (A-32733), Goat Alexa Fluor Plus 647-conjugated anti-mouse IgG highly cross-adsorbed (A32728), Goat Alexa Fluor Plus 594-conjugated anti-rat IgG highly cross-adsorbed (A48264), Donkey Alexa Fluor 488-conjugated anti-mouse IgG (A-21202).

    Techniques: Control, Knockdown, Incubation, Transfection, Plasmid Preparation, Expressing, Construct, Mutagenesis