2c1 against human aat polymers  (Hycult Biotech)


Bioz Verified Symbol Hycult Biotech is a verified supplier
Bioz Manufacturer Symbol Hycult Biotech manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 93
      Buy from Supplier

    Structured Review

    Hycult Biotech 2c1 against human aat polymers
    Interaction of ERdj3 with ZAAT. (A) ZAAT co‐immunoprecipitated with ERdj3 with and without cross‐linker. <t>AAT</t> KO Huh 7.5 cells were transfected with NT siRNA or siERdj3. Then, 24 h post silencing, cells were transfected with ZAAT plasmid. AAT was pulled down, and ERdj3 bound to ZAAT was determined by Western blot. (B) ERdj3 co‐localizes with ZAAT polymers. ZAAT transiently transfected cells were immunostained using <t>2C1</t> antibody (Alexa 594; red) and anti‐ERdj3 (Alexa 488; green), and nuclei were stained using DAPI (blue). (C) Erdj3 overexpression increases ZAAT polymer formation. MAAT and ZAAT transiently transfected cells were transfected with control (CO) or ERdj3 plasmids 24 h after the first transfection. Then, 48 h post transfection, lysates were incubated for 1 h at 37°C or 60°C to form polymers. Lysates were loaded on non‐denaturing native gel.
    2c1 Against Human Aat Polymers, supplied by Hycult Biotech, 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/2c1 against human aat polymers/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    2c1 against human aat polymers - by Bioz Stars, 2023-06
    93/100 stars

    Images

    1) Product Images from "Erdj3 Has an Essential Role for Z Variant Alpha‐1‐Antitrypsin Degradation"

    Article Title: Erdj3 Has an Essential Role for Z Variant Alpha‐1‐Antitrypsin Degradation

    Journal: Journal of Cellular Biochemistry

    doi: 10.1002/jcb.26069

    Interaction of ERdj3 with ZAAT. (A) ZAAT co‐immunoprecipitated with ERdj3 with and without cross‐linker. AAT KO Huh 7.5 cells were transfected with NT siRNA or siERdj3. Then, 24 h post silencing, cells were transfected with ZAAT plasmid. AAT was pulled down, and ERdj3 bound to ZAAT was determined by Western blot. (B) ERdj3 co‐localizes with ZAAT polymers. ZAAT transiently transfected cells were immunostained using 2C1 antibody (Alexa 594; red) and anti‐ERdj3 (Alexa 488; green), and nuclei were stained using DAPI (blue). (C) Erdj3 overexpression increases ZAAT polymer formation. MAAT and ZAAT transiently transfected cells were transfected with control (CO) or ERdj3 plasmids 24 h after the first transfection. Then, 48 h post transfection, lysates were incubated for 1 h at 37°C or 60°C to form polymers. Lysates were loaded on non‐denaturing native gel.
    Figure Legend Snippet: Interaction of ERdj3 with ZAAT. (A) ZAAT co‐immunoprecipitated with ERdj3 with and without cross‐linker. AAT KO Huh 7.5 cells were transfected with NT siRNA or siERdj3. Then, 24 h post silencing, cells were transfected with ZAAT plasmid. AAT was pulled down, and ERdj3 bound to ZAAT was determined by Western blot. (B) ERdj3 co‐localizes with ZAAT polymers. ZAAT transiently transfected cells were immunostained using 2C1 antibody (Alexa 594; red) and anti‐ERdj3 (Alexa 488; green), and nuclei were stained using DAPI (blue). (C) Erdj3 overexpression increases ZAAT polymer formation. MAAT and ZAAT transiently transfected cells were transfected with control (CO) or ERdj3 plasmids 24 h after the first transfection. Then, 48 h post transfection, lysates were incubated for 1 h at 37°C or 60°C to form polymers. Lysates were loaded on non‐denaturing native gel.

    Techniques Used: Immunoprecipitation, Transfection, Plasmid Preparation, Western Blot, Staining, Over Expression, Incubation

    The effect of siERdj3 on ZAAT degradation. (A) siERdj3 increases ZAAT degradation. NT siRNA or siERdj3 (20 or 40 µM) were introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. The level of ZAAT inside the cells (IC) and in the media (EC) and the level of ERdj3 were measured by Western blot. GAPDH was used as loading control. (B) siERdj3 does not affect ZAAT secretion. By ELISA, total AAT was measured in the media from the same samples as in panel A experiment. Total AAT was shown in picomolar concentration. (C) siERdj3 accelerates ZAAT clearance from the ER of hepatocytes. NT siRNA or 20 nM of siERdj3 was introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. IC ZAAT and EC ZAAT from NT siRNA and siERdj3‐treated samples were shown after pulse‐chase radiolabeling. (D) ZAAT polymers are reduced following siERdj3 treatment. NT siRNA or 20 µM of siERdj3 were introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. ZAAT polymers were immunostained with 2C1 antibody (Alexa 594; red). (E) Integrated density of red fluorescent measurement from four images per sample.
    Figure Legend Snippet: The effect of siERdj3 on ZAAT degradation. (A) siERdj3 increases ZAAT degradation. NT siRNA or siERdj3 (20 or 40 µM) were introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. The level of ZAAT inside the cells (IC) and in the media (EC) and the level of ERdj3 were measured by Western blot. GAPDH was used as loading control. (B) siERdj3 does not affect ZAAT secretion. By ELISA, total AAT was measured in the media from the same samples as in panel A experiment. Total AAT was shown in picomolar concentration. (C) siERdj3 accelerates ZAAT clearance from the ER of hepatocytes. NT siRNA or 20 nM of siERdj3 was introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. IC ZAAT and EC ZAAT from NT siRNA and siERdj3‐treated samples were shown after pulse‐chase radiolabeling. (D) ZAAT polymers are reduced following siERdj3 treatment. NT siRNA or 20 µM of siERdj3 were introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. ZAAT polymers were immunostained with 2C1 antibody (Alexa 594; red). (E) Integrated density of red fluorescent measurement from four images per sample.

    Techniques Used: Transfection, Western Blot, Enzyme-linked Immunosorbent Assay, Concentration Assay, Pulse Chase, Radioactivity

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 2c1 against human aat polymers  (Hycult Biotech)
    93
    Hycult Biotech 2c1 against human aat polymers
    Interaction of ERdj3 with ZAAT. (A) ZAAT co‐immunoprecipitated with ERdj3 with and without cross‐linker. <t>AAT</t> KO Huh 7.5 cells were transfected with NT siRNA or siERdj3. Then, 24 h post silencing, cells were transfected with ZAAT plasmid. AAT was pulled down, and ERdj3 bound to ZAAT was determined by Western blot. (B) ERdj3 co‐localizes with ZAAT polymers. ZAAT transiently transfected cells were immunostained using <t>2C1</t> antibody (Alexa 594; red) and anti‐ERdj3 (Alexa 488; green), and nuclei were stained using DAPI (blue). (C) Erdj3 overexpression increases ZAAT polymer formation. MAAT and ZAAT transiently transfected cells were transfected with control (CO) or ERdj3 plasmids 24 h after the first transfection. Then, 48 h post transfection, lysates were incubated for 1 h at 37°C or 60°C to form polymers. Lysates were loaded on non‐denaturing native gel.
    2c1 Against Human Aat Polymers, supplied by Hycult Biotech, 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/2c1 against human aat polymers/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    2c1 against human aat polymers - by Bioz Stars, 2023-06
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Interaction of ERdj3 with ZAAT. (A) ZAAT co‐immunoprecipitated with ERdj3 with and without cross‐linker. AAT KO Huh 7.5 cells were transfected with NT siRNA or siERdj3. Then, 24 h post silencing, cells were transfected with ZAAT plasmid. AAT was pulled down, and ERdj3 bound to ZAAT was determined by Western blot. (B) ERdj3 co‐localizes with ZAAT polymers. ZAAT transiently transfected cells were immunostained using 2C1 antibody (Alexa 594; red) and anti‐ERdj3 (Alexa 488; green), and nuclei were stained using DAPI (blue). (C) Erdj3 overexpression increases ZAAT polymer formation. MAAT and ZAAT transiently transfected cells were transfected with control (CO) or ERdj3 plasmids 24 h after the first transfection. Then, 48 h post transfection, lysates were incubated for 1 h at 37°C or 60°C to form polymers. Lysates were loaded on non‐denaturing native gel.

    Journal: Journal of Cellular Biochemistry

    Article Title: Erdj3 Has an Essential Role for Z Variant Alpha‐1‐Antitrypsin Degradation

    doi: 10.1002/jcb.26069

    Figure Lengend Snippet: Interaction of ERdj3 with ZAAT. (A) ZAAT co‐immunoprecipitated with ERdj3 with and without cross‐linker. AAT KO Huh 7.5 cells were transfected with NT siRNA or siERdj3. Then, 24 h post silencing, cells were transfected with ZAAT plasmid. AAT was pulled down, and ERdj3 bound to ZAAT was determined by Western blot. (B) ERdj3 co‐localizes with ZAAT polymers. ZAAT transiently transfected cells were immunostained using 2C1 antibody (Alexa 594; red) and anti‐ERdj3 (Alexa 488; green), and nuclei were stained using DAPI (blue). (C) Erdj3 overexpression increases ZAAT polymer formation. MAAT and ZAAT transiently transfected cells were transfected with control (CO) or ERdj3 plasmids 24 h after the first transfection. Then, 48 h post transfection, lysates were incubated for 1 h at 37°C or 60°C to form polymers. Lysates were loaded on non‐denaturing native gel.

    Article Snippet: Bafilomycin A1, MG132, Brefeldin A, and mouse monoclonal anti‐β‐actin were purchased from Sigma (St. Louis, MO), and 2C1 against human AAT polymers was purchased from Hycult biotech (Netherlands).

    Techniques: Immunoprecipitation, Transfection, Plasmid Preparation, Western Blot, Staining, Over Expression, Incubation

    The effect of siERdj3 on ZAAT degradation. (A) siERdj3 increases ZAAT degradation. NT siRNA or siERdj3 (20 or 40 µM) were introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. The level of ZAAT inside the cells (IC) and in the media (EC) and the level of ERdj3 were measured by Western blot. GAPDH was used as loading control. (B) siERdj3 does not affect ZAAT secretion. By ELISA, total AAT was measured in the media from the same samples as in panel A experiment. Total AAT was shown in picomolar concentration. (C) siERdj3 accelerates ZAAT clearance from the ER of hepatocytes. NT siRNA or 20 nM of siERdj3 was introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. IC ZAAT and EC ZAAT from NT siRNA and siERdj3‐treated samples were shown after pulse‐chase radiolabeling. (D) ZAAT polymers are reduced following siERdj3 treatment. NT siRNA or 20 µM of siERdj3 were introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. ZAAT polymers were immunostained with 2C1 antibody (Alexa 594; red). (E) Integrated density of red fluorescent measurement from four images per sample.

    Journal: Journal of Cellular Biochemistry

    Article Title: Erdj3 Has an Essential Role for Z Variant Alpha‐1‐Antitrypsin Degradation

    doi: 10.1002/jcb.26069

    Figure Lengend Snippet: The effect of siERdj3 on ZAAT degradation. (A) siERdj3 increases ZAAT degradation. NT siRNA or siERdj3 (20 or 40 µM) were introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. The level of ZAAT inside the cells (IC) and in the media (EC) and the level of ERdj3 were measured by Western blot. GAPDH was used as loading control. (B) siERdj3 does not affect ZAAT secretion. By ELISA, total AAT was measured in the media from the same samples as in panel A experiment. Total AAT was shown in picomolar concentration. (C) siERdj3 accelerates ZAAT clearance from the ER of hepatocytes. NT siRNA or 20 nM of siERdj3 was introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. IC ZAAT and EC ZAAT from NT siRNA and siERdj3‐treated samples were shown after pulse‐chase radiolabeling. (D) ZAAT polymers are reduced following siERdj3 treatment. NT siRNA or 20 µM of siERdj3 were introduced 24 h post ZAAT transfection to AAT KO Huh 7.5 cells. ZAAT polymers were immunostained with 2C1 antibody (Alexa 594; red). (E) Integrated density of red fluorescent measurement from four images per sample.

    Article Snippet: Bafilomycin A1, MG132, Brefeldin A, and mouse monoclonal anti‐β‐actin were purchased from Sigma (St. Louis, MO), and 2C1 against human AAT polymers was purchased from Hycult biotech (Netherlands).

    Techniques: Transfection, Western Blot, Enzyme-linked Immunosorbent Assay, Concentration Assay, Pulse Chase, Radioactivity