rabbit polyclonal anti rab9 Search Results


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ABclonal Biotechnology anti rab9a rabbit mab
FIGURE 9. Interaction and colocalization of IFITM3 with <t>Rab9a.</t> (A) Exogenous co-IP analysis of Rab9a and
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FIGURE 9. Interaction and colocalization of IFITM3 with <t>Rab9a.</t> (A) Exogenous co-IP analysis of Rab9a and
Anti Rab9, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Immunohistochemical results of bilateral adnexal masses. The results indicated that the serous carcinoma component was (A) positive for cytokeratin and (B) P53, (C) squamous cell carcinoma was positive for <t>P40,</t> and (D) chondrosarcoma was positive for S100 and (E) rhabdomyosarcoma was positive for MyoD1 (magnification, x100).
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Cell Signaling Technology Inc monoclonal rabbit anti rab5 rab7 rab9
Fig. 1. Acquisition of Rab GTPases onto the Cryptococcus-containing phagosome. At 15 min and 2 h, <t>Rab5</t> (A), <t>Rab11</t> (B), <t>Rab9</t> (C) and <t>Rab7</t> (D) recruitment to phagosomes containing live cryptococci was monitored. Recruitment at 5 min is comparable between phagosomes containing live C. neoformans H99, heat-killed H99 and a variety of inert targets (E). All data were collected from immunofluorescence analysis of J774 phagocytosed particles. All bars represent data collected from observing 100–664 phagosomes for each target at each time point over three to six biological repeats, mean ± SEM. Data presented for H99 and HK H99 at 15 and 120 min are replicated in A and E. ***P < 0.001, **P < 0.01 Fisher’s exact test.
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Danaher Inc rabbit polyclonal anti rab9
Fig. 1. Acquisition of Rab GTPases onto the Cryptococcus-containing phagosome. At 15 min and 2 h, <t>Rab5</t> (A), <t>Rab11</t> (B), <t>Rab9</t> (C) and <t>Rab7</t> (D) recruitment to phagosomes containing live cryptococci was monitored. Recruitment at 5 min is comparable between phagosomes containing live C. neoformans H99, heat-killed H99 and a variety of inert targets (E). All data were collected from immunofluorescence analysis of J774 phagocytosed particles. All bars represent data collected from observing 100–664 phagosomes for each target at each time point over three to six biological repeats, mean ± SEM. Data presented for H99 and HK H99 at 15 and 120 min are replicated in A and E. ***P < 0.001, **P < 0.01 Fisher’s exact test.
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Boster Bio rab9 antibody
Fig. 1. Acquisition of Rab GTPases onto the Cryptococcus-containing phagosome. At 15 min and 2 h, <t>Rab5</t> (A), <t>Rab11</t> (B), <t>Rab9</t> (C) and <t>Rab7</t> (D) recruitment to phagosomes containing live cryptococci was monitored. Recruitment at 5 min is comparable between phagosomes containing live C. neoformans H99, heat-killed H99 and a variety of inert targets (E). All data were collected from immunofluorescence analysis of J774 phagocytosed particles. All bars represent data collected from observing 100–664 phagosomes for each target at each time point over three to six biological repeats, mean ± SEM. Data presented for H99 and HK H99 at 15 and 120 min are replicated in A and E. ***P < 0.001, **P < 0.01 Fisher’s exact test.
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Promega mouse anti-halo
Fig. 1. Acquisition of Rab GTPases onto the Cryptococcus-containing phagosome. At 15 min and 2 h, <t>Rab5</t> (A), <t>Rab11</t> (B), <t>Rab9</t> (C) and <t>Rab7</t> (D) recruitment to phagosomes containing live cryptococci was monitored. Recruitment at 5 min is comparable between phagosomes containing live C. neoformans H99, heat-killed H99 and a variety of inert targets (E). All data were collected from immunofluorescence analysis of J774 phagocytosed particles. All bars represent data collected from observing 100–664 phagosomes for each target at each time point over three to six biological repeats, mean ± SEM. Data presented for H99 and HK H99 at 15 and 120 min are replicated in A and E. ***P < 0.001, **P < 0.01 Fisher’s exact test.
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Bio-Techne corporation synaptored c2
Fig. 1. Acquisition of Rab GTPases onto the Cryptococcus-containing phagosome. At 15 min and 2 h, <t>Rab5</t> (A), <t>Rab11</t> (B), <t>Rab9</t> (C) and <t>Rab7</t> (D) recruitment to phagosomes containing live cryptococci was monitored. Recruitment at 5 min is comparable between phagosomes containing live C. neoformans H99, heat-killed H99 and a variety of inert targets (E). All data were collected from immunofluorescence analysis of J774 phagocytosed particles. All bars represent data collected from observing 100–664 phagosomes for each target at each time point over three to six biological repeats, mean ± SEM. Data presented for H99 and HK H99 at 15 and 120 min are replicated in A and E. ***P < 0.001, **P < 0.01 Fisher’s exact test.
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Image Search Results


FIGURE 9. Interaction and colocalization of IFITM3 with Rab9a. (A) Exogenous co-IP analysis of Rab9a and

Journal: International journal of biological macromolecules

Article Title: Novel interacting proteins identified by tandem affinity purification and mass spectrometry associated with IFITM3 protein during PDCoV infection.

doi: 10.1016/j.ijbiomac.2024.132755

Figure Lengend Snippet: FIGURE 9. Interaction and colocalization of IFITM3 with Rab9a. (A) Exogenous co-IP analysis of Rab9a and

Article Snippet: The monolayers were incubated with anti-Rab9a Rabbit mAb (ABclonal) and probed using an Alexa Fluor 594 AffiniPure goat anti-rabbit IgG (H+L) antibody (Yeasen).

Techniques: Co-Immunoprecipitation Assay

Immunohistochemical results of bilateral adnexal masses. The results indicated that the serous carcinoma component was (A) positive for cytokeratin and (B) P53, (C) squamous cell carcinoma was positive for P40, and (D) chondrosarcoma was positive for S100 and (E) rhabdomyosarcoma was positive for MyoD1 (magnification, x100).

Journal: Experimental and Therapeutic Medicine

Article Title: Management of a rare ovarian carcinosarcoma: A case report and literature review

doi: 10.3892/etm.2022.11520

Figure Lengend Snippet: Immunohistochemical results of bilateral adnexal masses. The results indicated that the serous carcinoma component was (A) positive for cytokeratin and (B) P53, (C) squamous cell carcinoma was positive for P40, and (D) chondrosarcoma was positive for S100 and (E) rhabdomyosarcoma was positive for MyoD1 (magnification, x100).

Article Snippet: Primary antibodies applied in the IHC analysis were mainly as follows: Monoclonal mouse anti-human cytokeratin (CK) (AE1/AE3), mouse anti-human tumor protein p53 monoclonal antibody (DO-7), rabbit polyclonal anti-human S100 protein, monoclonal mouse anti-vimentin (V9; all from Dako; Agilent Technologies, Inc.), mouse anti-human tumor protein P40 monoclonal antibody (cat. no. 66622-1-Ig) and MYOD1 rabbit polyclonal antibody (cat. no. 18943-1-AP; both from ProteinTech Group, Inc.).

Techniques: Immunohistochemical staining

Fig. 1. Acquisition of Rab GTPases onto the Cryptococcus-containing phagosome. At 15 min and 2 h, Rab5 (A), Rab11 (B), Rab9 (C) and Rab7 (D) recruitment to phagosomes containing live cryptococci was monitored. Recruitment at 5 min is comparable between phagosomes containing live C. neoformans H99, heat-killed H99 and a variety of inert targets (E). All data were collected from immunofluorescence analysis of J774 phagocytosed particles. All bars represent data collected from observing 100–664 phagosomes for each target at each time point over three to six biological repeats, mean ± SEM. Data presented for H99 and HK H99 at 15 and 120 min are replicated in A and E. ***P < 0.001, **P < 0.01 Fisher’s exact test.

Journal: Cellular microbiology

Article Title: The fungal pathogen Cryptococcus neoformans manipulates macrophage phagosome maturation.

doi: 10.1111/cmi.12394

Figure Lengend Snippet: Fig. 1. Acquisition of Rab GTPases onto the Cryptococcus-containing phagosome. At 15 min and 2 h, Rab5 (A), Rab11 (B), Rab9 (C) and Rab7 (D) recruitment to phagosomes containing live cryptococci was monitored. Recruitment at 5 min is comparable between phagosomes containing live C. neoformans H99, heat-killed H99 and a variety of inert targets (E). All data were collected from immunofluorescence analysis of J774 phagocytosed particles. All bars represent data collected from observing 100–664 phagosomes for each target at each time point over three to six biological repeats, mean ± SEM. Data presented for H99 and HK H99 at 15 and 120 min are replicated in A and E. ***P < 0.001, **P < 0.01 Fisher’s exact test.

Article Snippet: Cells were then treated with 50 nM NH4Cl for 10 min and permeabilized in 0.1% Triton X-100 for 4 min. Coverslips were then blocked with 5% goat serum for 1 h and then washed in PBS before being treated with 0.5 μg ml−1 primary antibody (monoclonal rabbit anti-Rab5, Rab7, Rab9 or Rab11) (Cell Signaling) with 2.5 μg ml−1 human IgG for 30 min. After PBS washing, coverslips were then treated with 2 μg ml−1 secondary goat anti-rabbit IgGFITC (Sigma) with 10 μg ml−1 human IgG for 30 min. Coverslips were visualized with a Nikon Eclipse Ti-S microscope, Plan Apo 60×/1.40 NA oil DIC objective (Nikon) and captured with QICAM Fast1394 camera (QImaging).

Techniques: