fimbrin antibodies Search Results


t plastin fimbrin  (Santa Cruz Biotechnology)
92
Santa Cruz Biotechnology t plastin fimbrin
Timing of arrival of actin binding proteins in the bleb relative to actin. (A–C) Kymographs showing the localization of actin (red) compared with actin-binding proteins (green) during bleb retraction. Bleb extension is shown on the horizontal axis and time is shown on the vertical axis. Ezrin (A, green) arrives in the bleb significantly before actin and, consequently, a green trace can be seen at the bleb rim. As actin gets recruited to the rim, the trace turns yellow because of colocalization with ezrin. α-Actinin (B, green) and MRLC (C, green) are recruited after actin (red) and, consequently, a red trace can be seen first at the bleb rim. This trace turns yellow as these proteins are recruited to the rim. (D) Timing of arrival of the different actin-binding proteins in relationship to actin (t = 0 s). The error bars represent SD. Asterisks denote significant differences in timing. Ezrin arrives at the bleb rim significantly before actin. Coronin, α-actinin, and tropomyosin arrive significantly later than actin. Finally, <t>fimbrin</t> and myosin II appear last.
T Plastin Fimbrin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fimbrin+antibodies/T-Plastin+Antibody/pmc02064524-264-2-10
Average 92 stars, based on 1 article reviews
t plastin fimbrin - by Bioz Stars, 2026-11
92/100 stars
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mouse anti l plastin  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology mouse anti l plastin
Timing of arrival of actin binding proteins in the bleb relative to actin. (A–C) Kymographs showing the localization of actin (red) compared with actin-binding proteins (green) during bleb retraction. Bleb extension is shown on the horizontal axis and time is shown on the vertical axis. Ezrin (A, green) arrives in the bleb significantly before actin and, consequently, a green trace can be seen at the bleb rim. As actin gets recruited to the rim, the trace turns yellow because of colocalization with ezrin. α-Actinin (B, green) and MRLC (C, green) are recruited after actin (red) and, consequently, a red trace can be seen first at the bleb rim. This trace turns yellow as these proteins are recruited to the rim. (D) Timing of arrival of the different actin-binding proteins in relationship to actin (t = 0 s). The error bars represent SD. Asterisks denote significant differences in timing. Ezrin arrives at the bleb rim significantly before actin. Coronin, α-actinin, and tropomyosin arrive significantly later than actin. Finally, <t>fimbrin</t> and myosin II appear last.
Mouse Anti L Plastin, supplied by Santa Cruz Biotechnology, 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/product/fimbrin+antibodies/L-Plastin+Antibody/pm30928664-72-8-11
Average 93 stars, based on 1 article reviews
mouse anti l plastin - by Bioz Stars, 2026-11
93/100 stars
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lcp1  (Proteintech)
94
Proteintech lcp1
Timing of arrival of actin binding proteins in the bleb relative to actin. (A–C) Kymographs showing the localization of actin (red) compared with actin-binding proteins (green) during bleb retraction. Bleb extension is shown on the horizontal axis and time is shown on the vertical axis. Ezrin (A, green) arrives in the bleb significantly before actin and, consequently, a green trace can be seen at the bleb rim. As actin gets recruited to the rim, the trace turns yellow because of colocalization with ezrin. α-Actinin (B, green) and MRLC (C, green) are recruited after actin (red) and, consequently, a red trace can be seen first at the bleb rim. This trace turns yellow as these proteins are recruited to the rim. (D) Timing of arrival of the different actin-binding proteins in relationship to actin (t = 0 s). The error bars represent SD. Asterisks denote significant differences in timing. Ezrin arrives at the bleb rim significantly before actin. Coronin, α-actinin, and tropomyosin arrive significantly later than actin. Finally, <t>fimbrin</t> and myosin II appear last.
Lcp1, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fimbrin+antibodies/L-Plastin+Antibody/pm41484613-115-11-14
Average 94 stars, based on 1 article reviews
lcp1 - by Bioz Stars, 2026-11
94/100 stars
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rabbit polyclonal antibodies against t plastin  (Novus Biologicals)
90
Novus Biologicals rabbit polyclonal antibodies against t plastin
Timing of arrival of actin binding proteins in the bleb relative to actin. (A–C) Kymographs showing the localization of actin (red) compared with actin-binding proteins (green) during bleb retraction. Bleb extension is shown on the horizontal axis and time is shown on the vertical axis. Ezrin (A, green) arrives in the bleb significantly before actin and, consequently, a green trace can be seen at the bleb rim. As actin gets recruited to the rim, the trace turns yellow because of colocalization with ezrin. α-Actinin (B, green) and MRLC (C, green) are recruited after actin (red) and, consequently, a red trace can be seen first at the bleb rim. This trace turns yellow as these proteins are recruited to the rim. (D) Timing of arrival of the different actin-binding proteins in relationship to actin (t = 0 s). The error bars represent SD. Asterisks denote significant differences in timing. Ezrin arrives at the bleb rim significantly before actin. Coronin, α-actinin, and tropomyosin arrive significantly later than actin. Finally, <t>fimbrin</t> and myosin II appear last.
Rabbit Polyclonal Antibodies Against T Plastin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fimbrin+antibodies/T+Plastin+Antibody/pmc07511357-278-3-10
Average 90 stars, based on 1 article reviews
rabbit polyclonal antibodies against t plastin - by Bioz Stars, 2026-11
90/100 stars
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l plastin  (Novus Biologicals)
93
Novus Biologicals l plastin
Telomerase depletion is associated with increased inflammation in the aged zebrafish brain. (A) Representative images of mpeg‐mcherry <t>and</t> <t>L‐plastin</t> staining in the diencephalon of adult zebrafish (schematic figure highlights the region imaged as diencephalon). The yellow arrows highlight Lplastin + ; mpeg − cells. (A1) Quantifications of L‐plastin‐positive; mpeg‐positive cells (orange; from red and green co‐localisation) and (A2) L‐plastin‐positive; mpeg‐negative cells (red) in the whole zebrafish brain show an increased number of macrophages/microglia (L‐plastin‐positive; mpeg‐positive cells) with natural ageing, and this is accelerated in the absence of telomerase (in tert −/− at 2–6 months of age). However, we observed no differences in the number of T/B cells and neutrophils (L‐plastin‐positive; mpeg‐negative cells) with ageing, in the WT or tert −/− fish. N = −6 per group. (B) Schematic figure of the chitotriosidase assay (left). Quantifications (right) show that chitotriosidase activity increases with natural ageing at > 30 months of age, and that this is accelerated in the tert −/− at the age of 9–16 months. (C) Representative images of co‐staining with SA‐β‐Gal (blue) and L‐plastin (white) in brain sections show that most of the L‐plastin‐positive cells do not co‐localise with the SA‐β‐Gal staining (left). Staining quantification shows a significant correlation between increased number of immune cells and increased expression of SA‐β‐Gal with ageing in both WT and tert −/− (right). (A1, A2, B) Each dot represents one animal. (A1, A2, B, C) Bar errors represent the SEM. * < 0.05; ** < 0.01.
L Plastin, supplied by Novus Biologicals, 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/product/fimbrin+antibodies/Plastin+L+Antibody+(29G10)/pmc12686574-2-0-8
Average 93 stars, based on 1 article reviews
l plastin - by Bioz Stars, 2026-11
93/100 stars
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anti pls3 antibodies  (Santa Cruz Biotechnology)
90
Santa Cruz Biotechnology anti pls3 antibodies
Relationship between peripheral blood <t> PLS3 </t> expression and clinicopathologic factors in breast cancer patients
Anti Pls3 Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fimbrin+antibodies/Plastin+Antibody/pmc04453677-94-16-19
Average 90 stars, based on 1 article reviews
anti pls3 antibodies - by Bioz Stars, 2026-11
90/100 stars
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fimbrin antibodies  (Chemie GmbH)
90
Chemie GmbH fimbrin antibodies
Relationship between peripheral blood <t> PLS3 </t> expression and clinicopathologic factors in breast cancer patients
Fimbrin Antibodies, supplied by Chemie GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fimbrin+antibodies/fimbrin+antibodies/pm07876360-160-24-19
Average 90 stars, based on 1 article reviews
fimbrin antibodies - by Bioz Stars, 2026-11
90/100 stars
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anti-bacteria fimbrin monoclonal antibody  (Creative BioMart)
N/A
-20 °C, Avoid freeze / thaw cycleshttp://www.creative-diagnostics.com/Anti-Bacteria-Fimbrin-Antibody-53248-144.htm
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Image Search Results


Timing of arrival of actin binding proteins in the bleb relative to actin. (A–C) Kymographs showing the localization of actin (red) compared with actin-binding proteins (green) during bleb retraction. Bleb extension is shown on the horizontal axis and time is shown on the vertical axis. Ezrin (A, green) arrives in the bleb significantly before actin and, consequently, a green trace can be seen at the bleb rim. As actin gets recruited to the rim, the trace turns yellow because of colocalization with ezrin. α-Actinin (B, green) and MRLC (C, green) are recruited after actin (red) and, consequently, a red trace can be seen first at the bleb rim. This trace turns yellow as these proteins are recruited to the rim. (D) Timing of arrival of the different actin-binding proteins in relationship to actin (t = 0 s). The error bars represent SD. Asterisks denote significant differences in timing. Ezrin arrives at the bleb rim significantly before actin. Coronin, α-actinin, and tropomyosin arrive significantly later than actin. Finally, fimbrin and myosin II appear last.

Journal: The Journal of Cell Biology

Article Title: Reassembly of contractile actin cortex in cell blebs

doi: 10.1083/jcb.200602085

Figure Lengend Snippet: Timing of arrival of actin binding proteins in the bleb relative to actin. (A–C) Kymographs showing the localization of actin (red) compared with actin-binding proteins (green) during bleb retraction. Bleb extension is shown on the horizontal axis and time is shown on the vertical axis. Ezrin (A, green) arrives in the bleb significantly before actin and, consequently, a green trace can be seen at the bleb rim. As actin gets recruited to the rim, the trace turns yellow because of colocalization with ezrin. α-Actinin (B, green) and MRLC (C, green) are recruited after actin (red) and, consequently, a red trace can be seen first at the bleb rim. This trace turns yellow as these proteins are recruited to the rim. (D) Timing of arrival of the different actin-binding proteins in relationship to actin (t = 0 s). The error bars represent SD. Asterisks denote significant differences in timing. Ezrin arrives at the bleb rim significantly before actin. Coronin, α-actinin, and tropomyosin arrive significantly later than actin. Finally, fimbrin and myosin II appear last.

Article Snippet: Polyclonal anti-spectrin, T-Plastin (fimbrin), and adducin antibodies were purchased from Santa Cruz Biotechnologies, Inc., and they were all used at 1:100 dilution.

Techniques: Binding Assay

Protein composition of the principal cellular actin structures

Journal: The Journal of Cell Biology

Article Title: Reassembly of contractile actin cortex in cell blebs

doi: 10.1083/jcb.200602085

Figure Lengend Snippet: Protein composition of the principal cellular actin structures

Article Snippet: Polyclonal anti-spectrin, T-Plastin (fimbrin), and adducin antibodies were purchased from Santa Cruz Biotechnologies, Inc., and they were all used at 1:100 dilution.

Techniques: Immunostaining, Membrane

Localization of proteins relative to actin during bleb retraction. All images were acquired using confocal microscopy. In all images, actin is in red and the protein of interest in green. Timing relative to the first image is indicated in white text. (A) MRLC is originally not present (0–15 s) in the bleb, but assembles in distinct foci underneath the actin shell. (B) Coronin appears shortly after actin and forms a continuous rim colocalized with the actin shell. (C) Fimbrin appears after actin (44 vs. 18 s) and forms a continuous rim colocalized with the actin shell. Bars, 2 μm.

Journal: The Journal of Cell Biology

Article Title: Reassembly of contractile actin cortex in cell blebs

doi: 10.1083/jcb.200602085

Figure Lengend Snippet: Localization of proteins relative to actin during bleb retraction. All images were acquired using confocal microscopy. In all images, actin is in red and the protein of interest in green. Timing relative to the first image is indicated in white text. (A) MRLC is originally not present (0–15 s) in the bleb, but assembles in distinct foci underneath the actin shell. (B) Coronin appears shortly after actin and forms a continuous rim colocalized with the actin shell. (C) Fimbrin appears after actin (44 vs. 18 s) and forms a continuous rim colocalized with the actin shell. Bars, 2 μm.

Article Snippet: Polyclonal anti-spectrin, T-Plastin (fimbrin), and adducin antibodies were purchased from Santa Cruz Biotechnologies, Inc., and they were all used at 1:100 dilution.

Techniques: Confocal Microscopy

Telomerase depletion is associated with increased inflammation in the aged zebrafish brain. (A) Representative images of mpeg‐mcherry and L‐plastin staining in the diencephalon of adult zebrafish (schematic figure highlights the region imaged as diencephalon). The yellow arrows highlight Lplastin + ; mpeg − cells. (A1) Quantifications of L‐plastin‐positive; mpeg‐positive cells (orange; from red and green co‐localisation) and (A2) L‐plastin‐positive; mpeg‐negative cells (red) in the whole zebrafish brain show an increased number of macrophages/microglia (L‐plastin‐positive; mpeg‐positive cells) with natural ageing, and this is accelerated in the absence of telomerase (in tert −/− at 2–6 months of age). However, we observed no differences in the number of T/B cells and neutrophils (L‐plastin‐positive; mpeg‐negative cells) with ageing, in the WT or tert −/− fish. N = −6 per group. (B) Schematic figure of the chitotriosidase assay (left). Quantifications (right) show that chitotriosidase activity increases with natural ageing at > 30 months of age, and that this is accelerated in the tert −/− at the age of 9–16 months. (C) Representative images of co‐staining with SA‐β‐Gal (blue) and L‐plastin (white) in brain sections show that most of the L‐plastin‐positive cells do not co‐localise with the SA‐β‐Gal staining (left). Staining quantification shows a significant correlation between increased number of immune cells and increased expression of SA‐β‐Gal with ageing in both WT and tert −/− (right). (A1, A2, B) Each dot represents one animal. (A1, A2, B, C) Bar errors represent the SEM. * < 0.05; ** < 0.01.

Journal: Aging Cell

Article Title: Telomerase Depletion Accelerates Ageing of the Zebrafish Brain

doi: 10.1111/acel.70280

Figure Lengend Snippet: Telomerase depletion is associated with increased inflammation in the aged zebrafish brain. (A) Representative images of mpeg‐mcherry and L‐plastin staining in the diencephalon of adult zebrafish (schematic figure highlights the region imaged as diencephalon). The yellow arrows highlight Lplastin + ; mpeg − cells. (A1) Quantifications of L‐plastin‐positive; mpeg‐positive cells (orange; from red and green co‐localisation) and (A2) L‐plastin‐positive; mpeg‐negative cells (red) in the whole zebrafish brain show an increased number of macrophages/microglia (L‐plastin‐positive; mpeg‐positive cells) with natural ageing, and this is accelerated in the absence of telomerase (in tert −/− at 2–6 months of age). However, we observed no differences in the number of T/B cells and neutrophils (L‐plastin‐positive; mpeg‐negative cells) with ageing, in the WT or tert −/− fish. N = −6 per group. (B) Schematic figure of the chitotriosidase assay (left). Quantifications (right) show that chitotriosidase activity increases with natural ageing at > 30 months of age, and that this is accelerated in the tert −/− at the age of 9–16 months. (C) Representative images of co‐staining with SA‐β‐Gal (blue) and L‐plastin (white) in brain sections show that most of the L‐plastin‐positive cells do not co‐localise with the SA‐β‐Gal staining (left). Staining quantification shows a significant correlation between increased number of immune cells and increased expression of SA‐β‐Gal with ageing in both WT and tert −/− (right). (A1, A2, B) Each dot represents one animal. (A1, A2, B, C) Bar errors represent the SEM. * < 0.05; ** < 0.01.

Article Snippet: L‐plastin (Lcp1), rabbit polyclonal , 1:200 , GTX124420; Novus Biologicals, Littleton, CO, USA.

Techniques: Staining, Activity Assay, Expressing

Relationship between peripheral blood PLS3 expression and clinicopathologic factors in breast cancer patients

Journal: British Journal of Cancer

Article Title: Circulating tumour cell-derived plastin3 is a novel marker for predicting long-term prognosis in patients with breast cancer

doi: 10.1038/bjc.2015.132

Figure Lengend Snippet: Relationship between peripheral blood PLS3 expression and clinicopathologic factors in breast cancer patients

Article Snippet: Immunocytochemical double staining was performed using anti-pan cytokeratin (panCK) antibodies (AE1/AE3, Dako) together with two different anti-PLS3 antibodies (C15, Santa Cruz Biotechnology (Plastin antibody 1) or PA5-27883, Thermo Scientific (Plastin antibody 2)).

Techniques: Expressing, Adjuvant

Analysis of PLS3 protein and mRNA levels. ( A ) Comparison of PLS3 expression in breast cancer cell lines from primary tumours and a DTC cell line from the bone marrow of patients with breast cancer (BC-M1). The lung cancer DTC cell line LC-M1 served as an additional reference for a tumour cell population from a distant site. α -Tubulin served as a loading control. ( B ) Quantitative western blot analysis of PLS3 expression in the indicated cell lines. The dimensionless signal intensities are the average of three independent experiments (given as numbers), and vertical error bars indicate s.d. The signal intensities were normalised to the expression of α -tubulin. ( C ) Analysis of PLS3 expression in PBMCs from three different healthy control individuals by western blot. The breast cancer cell lines served as a reference for PLS3 expression in breast cancer cells, and α -tubulin served as a loading control. We observed lower signal intensities for α -tubulin in PBMCs than in the other cell lines. Hence, X-ray films with prolonged exposition times are presented to substantiate that PLS3 expression was below the detection limit in PBMCs. ( D ) Comparison of PLS3 gene expression between breast cancer cell lines and PBMCs of five different healthy control individuals. Analysis of the housekeeping gene hprt confirmed that the analyses for PLS3 provided comparable results between the breast cancer cell lines and the PBMCs. The water control was designated as H20 Cont. Unlike for PLS3 protein, weak signals for PLS3 mRNA were detected in PBMCs. MDA-231, MDA-MB-231 cells; MDA-468, MDA-MB-468 cells. All experiments: n =3.

Journal: British Journal of Cancer

Article Title: Circulating tumour cell-derived plastin3 is a novel marker for predicting long-term prognosis in patients with breast cancer

doi: 10.1038/bjc.2015.132

Figure Lengend Snippet: Analysis of PLS3 protein and mRNA levels. ( A ) Comparison of PLS3 expression in breast cancer cell lines from primary tumours and a DTC cell line from the bone marrow of patients with breast cancer (BC-M1). The lung cancer DTC cell line LC-M1 served as an additional reference for a tumour cell population from a distant site. α -Tubulin served as a loading control. ( B ) Quantitative western blot analysis of PLS3 expression in the indicated cell lines. The dimensionless signal intensities are the average of three independent experiments (given as numbers), and vertical error bars indicate s.d. The signal intensities were normalised to the expression of α -tubulin. ( C ) Analysis of PLS3 expression in PBMCs from three different healthy control individuals by western blot. The breast cancer cell lines served as a reference for PLS3 expression in breast cancer cells, and α -tubulin served as a loading control. We observed lower signal intensities for α -tubulin in PBMCs than in the other cell lines. Hence, X-ray films with prolonged exposition times are presented to substantiate that PLS3 expression was below the detection limit in PBMCs. ( D ) Comparison of PLS3 gene expression between breast cancer cell lines and PBMCs of five different healthy control individuals. Analysis of the housekeeping gene hprt confirmed that the analyses for PLS3 provided comparable results between the breast cancer cell lines and the PBMCs. The water control was designated as H20 Cont. Unlike for PLS3 protein, weak signals for PLS3 mRNA were detected in PBMCs. MDA-231, MDA-MB-231 cells; MDA-468, MDA-MB-468 cells. All experiments: n =3.

Article Snippet: Immunocytochemical double staining was performed using anti-pan cytokeratin (panCK) antibodies (AE1/AE3, Dako) together with two different anti-PLS3 antibodies (C15, Santa Cruz Biotechnology (Plastin antibody 1) or PA5-27883, Thermo Scientific (Plastin antibody 2)).

Techniques: Comparison, Expressing, Control, Western Blot, Gene Expression

Comparison of PLS3 expression in breast cancer cell lines with PLS3 expression in peripheral blood mononuclear cells of healthy control individuals by immunocytochemical double staining. Cells of the assigned cell lines were spiked in the blood samples. Identification of the tumour cells was supported by the cytokeratin-specific antibody AE1/AE3. Nuclei were stained with DAPI, and the composite image is an overlay of the DAPI, cytokeratin, and PLS3 images. Two different PLS3 antibodies were applied for the analysis. ( A ) For MDA-MB-468 (MDA-468), an enlarged view of stained cells is shown. ( B ) BC-M1 analysis for PLS3 and blood samples without cell spiking. PLS3 signals in PBMC were labelled with arrows.

Journal: British Journal of Cancer

Article Title: Circulating tumour cell-derived plastin3 is a novel marker for predicting long-term prognosis in patients with breast cancer

doi: 10.1038/bjc.2015.132

Figure Lengend Snippet: Comparison of PLS3 expression in breast cancer cell lines with PLS3 expression in peripheral blood mononuclear cells of healthy control individuals by immunocytochemical double staining. Cells of the assigned cell lines were spiked in the blood samples. Identification of the tumour cells was supported by the cytokeratin-specific antibody AE1/AE3. Nuclei were stained with DAPI, and the composite image is an overlay of the DAPI, cytokeratin, and PLS3 images. Two different PLS3 antibodies were applied for the analysis. ( A ) For MDA-MB-468 (MDA-468), an enlarged view of stained cells is shown. ( B ) BC-M1 analysis for PLS3 and blood samples without cell spiking. PLS3 signals in PBMC were labelled with arrows.

Article Snippet: Immunocytochemical double staining was performed using anti-pan cytokeratin (panCK) antibodies (AE1/AE3, Dako) together with two different anti-PLS3 antibodies (C15, Santa Cruz Biotechnology (Plastin antibody 1) or PA5-27883, Thermo Scientific (Plastin antibody 2)).

Techniques: Comparison, Expressing, Control, Double Staining, Staining

Prognostic significance of PLS3 expression in breast cancer cases. Comparison of the OS rate in 298 test sample sets ( A ) and 296 validation sets ( B ) from PLS3 (+) and PLS3 (−) breast cancer cases of all stages. Comparison of the DFS rate in 293 test sample sets ( C ) and 292 validation sets ( D ) from PLS3 (+) and PLS3 (−) breast cancer cases of stage I–III. In 594 patients (for the analysis of all stages), we compared OS rates between PLS3 (+) and PLS3 (−) cases ( E ). DFS was compared in the 585 cases of stage I–III cancers ( PLS3 (+) vs PLS3 (−) ( F ). OS was compared in 361 cases of all stages and DFS was compared in 359 cases of stages I–III; all cases did not have lymph node metastasis at the time of operation ( G , H ).

Journal: British Journal of Cancer

Article Title: Circulating tumour cell-derived plastin3 is a novel marker for predicting long-term prognosis in patients with breast cancer

doi: 10.1038/bjc.2015.132

Figure Lengend Snippet: Prognostic significance of PLS3 expression in breast cancer cases. Comparison of the OS rate in 298 test sample sets ( A ) and 296 validation sets ( B ) from PLS3 (+) and PLS3 (−) breast cancer cases of all stages. Comparison of the DFS rate in 293 test sample sets ( C ) and 292 validation sets ( D ) from PLS3 (+) and PLS3 (−) breast cancer cases of stage I–III. In 594 patients (for the analysis of all stages), we compared OS rates between PLS3 (+) and PLS3 (−) cases ( E ). DFS was compared in the 585 cases of stage I–III cancers ( PLS3 (+) vs PLS3 (−) ( F ). OS was compared in 361 cases of all stages and DFS was compared in 359 cases of stages I–III; all cases did not have lymph node metastasis at the time of operation ( G , H ).

Article Snippet: Immunocytochemical double staining was performed using anti-pan cytokeratin (panCK) antibodies (AE1/AE3, Dako) together with two different anti-PLS3 antibodies (C15, Santa Cruz Biotechnology (Plastin antibody 1) or PA5-27883, Thermo Scientific (Plastin antibody 2)).

Techniques: Expressing, Comparison, Biomarker Discovery

Univariate and multivariate analysis for survival of peripheral blood PLS3 status and clinicopathological factors in breast cancer patients ( n =591)

Journal: British Journal of Cancer

Article Title: Circulating tumour cell-derived plastin3 is a novel marker for predicting long-term prognosis in patients with breast cancer

doi: 10.1038/bjc.2015.132

Figure Lengend Snippet: Univariate and multivariate analysis for survival of peripheral blood PLS3 status and clinicopathological factors in breast cancer patients ( n =591)

Article Snippet: Immunocytochemical double staining was performed using anti-pan cytokeratin (panCK) antibodies (AE1/AE3, Dako) together with two different anti-PLS3 antibodies (C15, Santa Cruz Biotechnology (Plastin antibody 1) or PA5-27883, Thermo Scientific (Plastin antibody 2)).

Techniques: