SEC16A Antibody

Western Blot: SEC16A Antibody [NB100-1799]

Western Blot: SEC16A Antibody [NB100-1799] - Detection of Human KIAA0310 on HeLa whole cell lysate using NB100-1799. KIAA0310 was also immunoprecipitated by 2 other antibodies.

Knockdown Validated: SEC16A Antibody [NB100-1799] -

Requirement of Sec16A and p115 for optimal type I IFN innate immune response in cells exposed to cytosolic DNA and RNA sensor ligands.(A–D) HeLa cells were transfected with nonsilencing (Ns) RNA duplexes or two different sets of siRNA duplexes that specifically target p115 or Sec16A as indicated. 72 h post-transfection, cells were left untreated (Ctl) or stimulated with poly I:C (2.5 ug/ml), poly dA:dT (1 ug/ml) or SeV (200 HAU/ml) for 6 h to 8 h. RNA was extracted and analyzed by RT-qPCR using primers for ifn beta, ifit1, oas1. Data are means +/− S.D. (n = 3). * Significantly below the induction response; * P<0.05, ** P<0.01, *** P<0.001. (B and D) Cellular extracts were also prepared and subjected to immunoblot analysis using indicated antibodies. One of three independent experiments with similar results is shown. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/22792062), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Knockdown Validated: SEC16A Antibody [NB100-1799] -

Sec16A and p115 are required for the proper positioning of TRAF3 along the mitochondrial network.(A) Confocal microscopy of HeLa cells transfected with 40 nM nonsilencing RNA duplexes (panels 1 and 2) or 40 nM siRNA duplexes that specifically target Sec16A (panels 3 and 4) or p115 (panels 5 and 6) and stained for MAVS and endogenous TRAF3 upon no treatment (panels 1, 3 and 5) or SeV infection (200 HAU/ml) for 4 h (panels 2, 4 and 6). Arrows indicate the colocalization of TRAF3 with MAVS. Bars represent 5 um. One of three independent experiments with similar results is shown. (B) p115 and Sec16A were silenced in HeLa cells as described in (A) and infected with SeV for indicated periods of time. Whole-cell lysates were subjected to immunoprecipitation using an anti-TRAF3 (H-20) antibody followed by immunoblotting for the presence of MAVS and TRAF3. Immunoblot analysis against p115, Sec16A, TRAF3 and SeV proteins are also shown (Input). One of two independent experiments with similar results is shown. (C) Densitometric analysis of the binding activity of MAVS to TRAF3 presented in Figures 6B. Data represent the ratio of immunoprecipitated MAVS over immunoprecipitated TRAF3 and are means +/− S.D. of two experiments. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/22792062), licensed under a CC-BY license. Not internally tested by Novus Biologicals.