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full length human rab8a  (TaKaRa)


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    Structured Review

    TaKaRa full length human rab8a
    Transport of latent TGFB1 to the cell surface requires <t>RAB8A-mediated</t> secretion. (A) Immunofluorescence analysis of human Wi26 fibroblasts expressing HA-LAP-TGFB1 (red), stained for endogenous RAB8A (green) and GOLGA2 (magenta) identified colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset). Scale bar: 10 μm. (B) Immunofluorescence analysis of murine control and Ilk cKO fibroblasts, transfected with HA-tagged RAB8A (green; DAPI-stained nuclei appear blue) showed relocalization of RAB8A to perinuclear aggregates. Scale bar: 10 μm. (C and D) Immunoblots illustrating knockdown efficiency of RAB8A (C) and RAB8B (D) in comparison to control (si-Scr). ACTB levels were used to indicate comparable loading. (E and F) Secreted TGFB1 levels were significantly reduced upon knockdown of RAB8A (P<0.001) (E); whereas no change in TGFB1 secretion was detected upon knockdown of RAB8B (F). Each symbol represents one independent transfectant. (G and H) Autophagy was analyzed in human Wi26 fibroblasts following treatment either with DMSO, or with 100 nM BafA, or with 20 μg/ml rapamycin (Rapa) for 4 h. The upper and lower ‘<’ symbols in the immunoblots indicate the position of the MAP1LC3B-I and -II variants, respectively. Autophagy was visualized by the presence of MAP1LC3-II and SQSTM1 bands in immunoblots. Depletion of RAB8A (G) and of RAB8B (H) did not affect basal or stimulated autophagy. Data are representative of 3 experiments. Signal intensities were quantified densitometrically and the ratio of MAP1LC3-II to ACTB is presented below the blots. (I) Immunofluorescence analysis of MEFs derived from atg5 KO or Atg5 WT animals expressing HA-LAP-TGFB1 (red) and stained for endogenous RAB8A (green) identified partial colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset), which is not observed in atg5 KO cells. Scale bar: 5 μm. (J) The images of 20 Atg5 WT and 26 atg5 KO cells were used to determine the Pearson correlation coefficient, which reflects the extent of colocalization of TGFB1 with RAB8A (LAP and RAB8A). Values of about 0.15 confirmed selective colocalization.
    Full Length Human Rab8a, supplied by TaKaRa, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/full+length+human+rab8a/pmc05915026-643-0-13?v=TaKaRa
    Average 86 stars, based on 1 article reviews
    full length human rab8a - by Bioz Stars, 2026-08
    86/100 stars

    Images

    1) Product Images from "TGFB1 is secreted through an unconventional pathway dependent on the autophagic machinery and cytoskeletal regulators"

    Article Title: TGFB1 is secreted through an unconventional pathway dependent on the autophagic machinery and cytoskeletal regulators

    Journal: Autophagy

    doi: 10.1080/15548627.2017.1422850

    Transport of latent TGFB1 to the cell surface requires RAB8A-mediated secretion. (A) Immunofluorescence analysis of human Wi26 fibroblasts expressing HA-LAP-TGFB1 (red), stained for endogenous RAB8A (green) and GOLGA2 (magenta) identified colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset). Scale bar: 10 μm. (B) Immunofluorescence analysis of murine control and Ilk cKO fibroblasts, transfected with HA-tagged RAB8A (green; DAPI-stained nuclei appear blue) showed relocalization of RAB8A to perinuclear aggregates. Scale bar: 10 μm. (C and D) Immunoblots illustrating knockdown efficiency of RAB8A (C) and RAB8B (D) in comparison to control (si-Scr). ACTB levels were used to indicate comparable loading. (E and F) Secreted TGFB1 levels were significantly reduced upon knockdown of RAB8A (P<0.001) (E); whereas no change in TGFB1 secretion was detected upon knockdown of RAB8B (F). Each symbol represents one independent transfectant. (G and H) Autophagy was analyzed in human Wi26 fibroblasts following treatment either with DMSO, or with 100 nM BafA, or with 20 μg/ml rapamycin (Rapa) for 4 h. The upper and lower ‘<’ symbols in the immunoblots indicate the position of the MAP1LC3B-I and -II variants, respectively. Autophagy was visualized by the presence of MAP1LC3-II and SQSTM1 bands in immunoblots. Depletion of RAB8A (G) and of RAB8B (H) did not affect basal or stimulated autophagy. Data are representative of 3 experiments. Signal intensities were quantified densitometrically and the ratio of MAP1LC3-II to ACTB is presented below the blots. (I) Immunofluorescence analysis of MEFs derived from atg5 KO or Atg5 WT animals expressing HA-LAP-TGFB1 (red) and stained for endogenous RAB8A (green) identified partial colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset), which is not observed in atg5 KO cells. Scale bar: 5 μm. (J) The images of 20 Atg5 WT and 26 atg5 KO cells were used to determine the Pearson correlation coefficient, which reflects the extent of colocalization of TGFB1 with RAB8A (LAP and RAB8A). Values of about 0.15 confirmed selective colocalization.
    Figure Legend Snippet: Transport of latent TGFB1 to the cell surface requires RAB8A-mediated secretion. (A) Immunofluorescence analysis of human Wi26 fibroblasts expressing HA-LAP-TGFB1 (red), stained for endogenous RAB8A (green) and GOLGA2 (magenta) identified colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset). Scale bar: 10 μm. (B) Immunofluorescence analysis of murine control and Ilk cKO fibroblasts, transfected with HA-tagged RAB8A (green; DAPI-stained nuclei appear blue) showed relocalization of RAB8A to perinuclear aggregates. Scale bar: 10 μm. (C and D) Immunoblots illustrating knockdown efficiency of RAB8A (C) and RAB8B (D) in comparison to control (si-Scr). ACTB levels were used to indicate comparable loading. (E and F) Secreted TGFB1 levels were significantly reduced upon knockdown of RAB8A (P<0.001) (E); whereas no change in TGFB1 secretion was detected upon knockdown of RAB8B (F). Each symbol represents one independent transfectant. (G and H) Autophagy was analyzed in human Wi26 fibroblasts following treatment either with DMSO, or with 100 nM BafA, or with 20 μg/ml rapamycin (Rapa) for 4 h. The upper and lower ‘<’ symbols in the immunoblots indicate the position of the MAP1LC3B-I and -II variants, respectively. Autophagy was visualized by the presence of MAP1LC3-II and SQSTM1 bands in immunoblots. Depletion of RAB8A (G) and of RAB8B (H) did not affect basal or stimulated autophagy. Data are representative of 3 experiments. Signal intensities were quantified densitometrically and the ratio of MAP1LC3-II to ACTB is presented below the blots. (I) Immunofluorescence analysis of MEFs derived from atg5 KO or Atg5 WT animals expressing HA-LAP-TGFB1 (red) and stained for endogenous RAB8A (green) identified partial colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset), which is not observed in atg5 KO cells. Scale bar: 5 μm. (J) The images of 20 Atg5 WT and 26 atg5 KO cells were used to determine the Pearson correlation coefficient, which reflects the extent of colocalization of TGFB1 with RAB8A (LAP and RAB8A). Values of about 0.15 confirmed selective colocalization.

    Techniques Used: Immunofluorescence, Expressing, Staining, Derivative Assay, Transfection, Western Blot

    siRNA-mediated gene silencing
    Figure Legend Snippet: siRNA-mediated gene silencing

    Techniques Used:



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    full length human rab8a  (TaKaRa)
    86
    TaKaRa full length human rab8a
    Transport of latent TGFB1 to the cell surface requires <t>RAB8A-mediated</t> secretion. (A) Immunofluorescence analysis of human Wi26 fibroblasts expressing HA-LAP-TGFB1 (red), stained for endogenous RAB8A (green) and GOLGA2 (magenta) identified colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset). Scale bar: 10 μm. (B) Immunofluorescence analysis of murine control and Ilk cKO fibroblasts, transfected with HA-tagged RAB8A (green; DAPI-stained nuclei appear blue) showed relocalization of RAB8A to perinuclear aggregates. Scale bar: 10 μm. (C and D) Immunoblots illustrating knockdown efficiency of RAB8A (C) and RAB8B (D) in comparison to control (si-Scr). ACTB levels were used to indicate comparable loading. (E and F) Secreted TGFB1 levels were significantly reduced upon knockdown of RAB8A (P<0.001) (E); whereas no change in TGFB1 secretion was detected upon knockdown of RAB8B (F). Each symbol represents one independent transfectant. (G and H) Autophagy was analyzed in human Wi26 fibroblasts following treatment either with DMSO, or with 100 nM BafA, or with 20 μg/ml rapamycin (Rapa) for 4 h. The upper and lower ‘<’ symbols in the immunoblots indicate the position of the MAP1LC3B-I and -II variants, respectively. Autophagy was visualized by the presence of MAP1LC3-II and SQSTM1 bands in immunoblots. Depletion of RAB8A (G) and of RAB8B (H) did not affect basal or stimulated autophagy. Data are representative of 3 experiments. Signal intensities were quantified densitometrically and the ratio of MAP1LC3-II to ACTB is presented below the blots. (I) Immunofluorescence analysis of MEFs derived from atg5 KO or Atg5 WT animals expressing HA-LAP-TGFB1 (red) and stained for endogenous RAB8A (green) identified partial colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset), which is not observed in atg5 KO cells. Scale bar: 5 μm. (J) The images of 20 Atg5 WT and 26 atg5 KO cells were used to determine the Pearson correlation coefficient, which reflects the extent of colocalization of TGFB1 with RAB8A (LAP and RAB8A). Values of about 0.15 confirmed selective colocalization.
    Full Length Human Rab8a, supplied by TaKaRa, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/full+length+human+rab8a/pmc05915026-643-0-13?v=TaKaRa
    Average 86 stars, based on 1 article reviews
    full length human rab8a - by Bioz Stars, 2026-08
    86/100 stars
    		  Buy from Supplier

    Image Search Results


    Transport of latent TGFB1 to the cell surface requires RAB8A-mediated secretion. (A) Immunofluorescence analysis of human Wi26 fibroblasts expressing HA-LAP-TGFB1 (red), stained for endogenous RAB8A (green) and GOLGA2 (magenta) identified colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset). Scale bar: 10 μm. (B) Immunofluorescence analysis of murine control and Ilk cKO fibroblasts, transfected with HA-tagged RAB8A (green; DAPI-stained nuclei appear blue) showed relocalization of RAB8A to perinuclear aggregates. Scale bar: 10 μm. (C and D) Immunoblots illustrating knockdown efficiency of RAB8A (C) and RAB8B (D) in comparison to control (si-Scr). ACTB levels were used to indicate comparable loading. (E and F) Secreted TGFB1 levels were significantly reduced upon knockdown of RAB8A (P<0.001) (E); whereas no change in TGFB1 secretion was detected upon knockdown of RAB8B (F). Each symbol represents one independent transfectant. (G and H) Autophagy was analyzed in human Wi26 fibroblasts following treatment either with DMSO, or with 100 nM BafA, or with 20 μg/ml rapamycin (Rapa) for 4 h. The upper and lower ‘<’ symbols in the immunoblots indicate the position of the MAP1LC3B-I and -II variants, respectively. Autophagy was visualized by the presence of MAP1LC3-II and SQSTM1 bands in immunoblots. Depletion of RAB8A (G) and of RAB8B (H) did not affect basal or stimulated autophagy. Data are representative of 3 experiments. Signal intensities were quantified densitometrically and the ratio of MAP1LC3-II to ACTB is presented below the blots. (I) Immunofluorescence analysis of MEFs derived from atg5 KO or Atg5 WT animals expressing HA-LAP-TGFB1 (red) and stained for endogenous RAB8A (green) identified partial colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset), which is not observed in atg5 KO cells. Scale bar: 5 μm. (J) The images of 20 Atg5 WT and 26 atg5 KO cells were used to determine the Pearson correlation coefficient, which reflects the extent of colocalization of TGFB1 with RAB8A (LAP and RAB8A). Values of about 0.15 confirmed selective colocalization.

    Journal: Autophagy

    Article Title: TGFB1 is secreted through an unconventional pathway dependent on the autophagic machinery and cytoskeletal regulators

    doi: 10.1080/15548627.2017.1422850

    Figure Lengend Snippet: Transport of latent TGFB1 to the cell surface requires RAB8A-mediated secretion. (A) Immunofluorescence analysis of human Wi26 fibroblasts expressing HA-LAP-TGFB1 (red), stained for endogenous RAB8A (green) and GOLGA2 (magenta) identified colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset). Scale bar: 10 μm. (B) Immunofluorescence analysis of murine control and Ilk cKO fibroblasts, transfected with HA-tagged RAB8A (green; DAPI-stained nuclei appear blue) showed relocalization of RAB8A to perinuclear aggregates. Scale bar: 10 μm. (C and D) Immunoblots illustrating knockdown efficiency of RAB8A (C) and RAB8B (D) in comparison to control (si-Scr). ACTB levels were used to indicate comparable loading. (E and F) Secreted TGFB1 levels were significantly reduced upon knockdown of RAB8A (P<0.001) (E); whereas no change in TGFB1 secretion was detected upon knockdown of RAB8B (F). Each symbol represents one independent transfectant. (G and H) Autophagy was analyzed in human Wi26 fibroblasts following treatment either with DMSO, or with 100 nM BafA, or with 20 μg/ml rapamycin (Rapa) for 4 h. The upper and lower ‘<’ symbols in the immunoblots indicate the position of the MAP1LC3B-I and -II variants, respectively. Autophagy was visualized by the presence of MAP1LC3-II and SQSTM1 bands in immunoblots. Depletion of RAB8A (G) and of RAB8B (H) did not affect basal or stimulated autophagy. Data are representative of 3 experiments. Signal intensities were quantified densitometrically and the ratio of MAP1LC3-II to ACTB is presented below the blots. (I) Immunofluorescence analysis of MEFs derived from atg5 KO or Atg5 WT animals expressing HA-LAP-TGFB1 (red) and stained for endogenous RAB8A (green) identified partial colocalization of HA-LAP with RAB8A at Golgi-derived autophagosomal intermediates (yellow in merged inset), which is not observed in atg5 KO cells. Scale bar: 5 μm. (J) The images of 20 Atg5 WT and 26 atg5 KO cells were used to determine the Pearson correlation coefficient, which reflects the extent of colocalization of TGFB1 with RAB8A (LAP and RAB8A). Values of about 0.15 confirmed selective colocalization.

    Article Snippet: Full-length human RAB8A , acc. no. {"type":"entrez-nucleotide","attrs":{"text":"NM_005370","term_id":"1519241776","term_text":"NM_005370"}} NM_005370 , was cloned into pCMV-HA (Clontech, 631604).

    Techniques: Immunofluorescence, Expressing, Staining, Derivative Assay, Transfection, Western Blot

    siRNA-mediated gene silencing

    Journal: Autophagy

    Article Title: TGFB1 is secreted through an unconventional pathway dependent on the autophagic machinery and cytoskeletal regulators

    doi: 10.1080/15548627.2017.1422850

    Figure Lengend Snippet: siRNA-mediated gene silencing

    Article Snippet: Full-length human RAB8A , acc. no. {"type":"entrez-nucleotide","attrs":{"text":"NM_005370","term_id":"1519241776","term_text":"NM_005370"}} NM_005370 , was cloned into pCMV-HA (Clontech, 631604).

    Techniques: