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anti α1 antitrypsin  (Valiant Co Ltd)
86
Valiant Co Ltd anti α1 antitrypsin
NS1 κ LC expressed in P3U.1 cells (A), RE61 λ LC and BiP (C) or HA-γ V-CH1 (E) were transiently co-expressed with or without Herp-FLAG in 293T cells. At 24 hr post-transfection, cell extracts were prepared from cells treated with or without lactacystin and immunoprecipitated with anti-κ LC antiserum (A), anti-λ LC antiserum (C) or anti-HA antibody (E). Cell extracts and precipitated samples were subjected to immunoblot analyses as indicated. Non-secreted λ LC RE61 (B) or HA-γ V-CH1 (D) were transiently expressed in 293T cells. At 24 hr post-transfection, cells were labeled with 35S-methionine/cysteine for 15 min and chased for the indicated times in the presence or absence of lactacystin. Immunoprecipitated samples from cell extracts were subjected to SDS-PAGE, followed by autoradiography. The signals for λ LC RE61 (B) or HA-γ V-CH1 (D) were quantified as expressed as a percent of that present at t=0. The values are shown at the bottom of each lane. The <t>α1-antitrypsin</t> (AAT) NHK variant (F) or Z variant (G) was transiently co-expressed with or without Herp-FLAG in 293T cells. At 24 hr post-transfection, cell extracts were prepared after treatment with or without tunicamycin for 3 hr and subjected to immunoprecipitation with anti-α1-antitrypsin antiserum. Cell extracts and precipitated samples were subjected to immunoblot analysis as indicated.
Anti α1 Antitrypsin, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti α1 antitrypsin - by Bioz Stars, 2026-02
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NS1 κ LC expressed in P3U.1 cells (A), RE61 λ LC and BiP (C) or HA-γ V-CH1 (E) were transiently co-expressed with or without Herp-FLAG in 293T cells. At 24 hr post-transfection, cell extracts were prepared from cells treated with or without lactacystin and immunoprecipitated with anti-κ LC antiserum (A), anti-λ LC antiserum (C) or anti-HA antibody (E). Cell extracts and precipitated samples were subjected to immunoblot analyses as indicated. Non-secreted λ LC RE61 (B) or HA-γ V-CH1 (D) were transiently expressed in 293T cells. At 24 hr post-transfection, cells were labeled with 35S-methionine/cysteine for 15 min and chased for the indicated times in the presence or absence of lactacystin. Immunoprecipitated samples from cell extracts were subjected to SDS-PAGE, followed by autoradiography. The signals for λ LC RE61 (B) or HA-γ V-CH1 (D) were quantified as expressed as a percent of that present at t=0. The values are shown at the bottom of each lane. The α1-antitrypsin (AAT) NHK variant (F) or Z variant (G) was transiently co-expressed with or without Herp-FLAG in 293T cells. At 24 hr post-transfection, cell extracts were prepared after treatment with or without tunicamycin for 3 hr and subjected to immunoprecipitation with anti-α1-antitrypsin antiserum. Cell extracts and precipitated samples were subjected to immunoblot analysis as indicated.

Journal:

Article Title: Characterization of an ERAD pathway for non-glycosylated BiP substrates which requires Herp

doi: 10.1016/j.molcel.2007.09.012

Figure Lengend Snippet: NS1 κ LC expressed in P3U.1 cells (A), RE61 λ LC and BiP (C) or HA-γ V-CH1 (E) were transiently co-expressed with or without Herp-FLAG in 293T cells. At 24 hr post-transfection, cell extracts were prepared from cells treated with or without lactacystin and immunoprecipitated with anti-κ LC antiserum (A), anti-λ LC antiserum (C) or anti-HA antibody (E). Cell extracts and precipitated samples were subjected to immunoblot analyses as indicated. Non-secreted λ LC RE61 (B) or HA-γ V-CH1 (D) were transiently expressed in 293T cells. At 24 hr post-transfection, cells were labeled with 35S-methionine/cysteine for 15 min and chased for the indicated times in the presence or absence of lactacystin. Immunoprecipitated samples from cell extracts were subjected to SDS-PAGE, followed by autoradiography. The signals for λ LC RE61 (B) or HA-γ V-CH1 (D) were quantified as expressed as a percent of that present at t=0. The values are shown at the bottom of each lane. The α1-antitrypsin (AAT) NHK variant (F) or Z variant (G) was transiently co-expressed with or without Herp-FLAG in 293T cells. At 24 hr post-transfection, cell extracts were prepared after treatment with or without tunicamycin for 3 hr and subjected to immunoprecipitation with anti-α1-antitrypsin antiserum. Cell extracts and precipitated samples were subjected to immunoblot analysis as indicated.

Article Snippet: All other antibodies were purchased from companies; anti-mouse IgG (Igγ and κ) and anti-mouse IgM (Igμ and λ) (Southern Biotech), anti-actin, anti-Hsc70, and anti-FLAG D-8 (Santa Cruz), anti-ubiquitinated proteins FK2, anti-HC8, and anti-S1 (BIOMOL), and anti-α1 antitrypsin (MP Biomedicals).

Techniques: Transfection, Immunoprecipitation, Western Blot, Labeling, SDS Page, Autoradiography, Variant Assay