55135 1 ap Search Results


96
Proteintech α sma
Fig. 6 3D-ABs suppress oxidative stress and cell death, and stimulated angiogenesis in ischaemic flaps. (A) F-CHP staining for damaged collagen detec tion in the skin on POD7. Scale bars, 100 μm. (B) The three groups’ quantified F-CHP intensity (n = 6). (C) CD31 <t>and</t> <t>α-SMA</t> IF staining in the flap on POD7. Scale bars, 50 μm. (D) <t>Quantified</t> <t>CD31/α-SMA-positive</t> blood vessel density among the three groups (n = 6). (E) Dead cells in flap tissue sections on POD7 under the detection of TUNEL staining. Scale bar, 20 μm. (F) TUNEL-positive cell percentage in the dermal layer, quantified for each of the three groups (n = 6). (G) DHE staining of the skin tissues on POD7 among the three groups. Scale bars, 50 μm. (H) Quantified DHE among the three groups (n = 6). SEM error bars are used. Significance (*): p value < 0.05; equal variances ANOVA with LSD post hoc analysis or unequal variances Dunnett’s T3 technique
α Sma, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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98
Proteintech rabbit anti β actin polyclonal antibodies
Fig. 6 3D-ABs suppress oxidative stress and cell death, and stimulated angiogenesis in ischaemic flaps. (A) F-CHP staining for damaged collagen detec tion in the skin on POD7. Scale bars, 100 μm. (B) The three groups’ quantified F-CHP intensity (n = 6). (C) CD31 <t>and</t> <t>α-SMA</t> IF staining in the flap on POD7. Scale bars, 50 μm. (D) <t>Quantified</t> <t>CD31/α-SMA-positive</t> blood vessel density among the three groups (n = 6). (E) Dead cells in flap tissue sections on POD7 under the detection of TUNEL staining. Scale bar, 20 μm. (F) TUNEL-positive cell percentage in the dermal layer, quantified for each of the three groups (n = 6). (G) DHE staining of the skin tissues on POD7 among the three groups. Scale bars, 50 μm. (H) Quantified DHE among the three groups (n = 6). SEM error bars are used. Significance (*): p value < 0.05; equal variances ANOVA with LSD post hoc analysis or unequal variances Dunnett’s T3 technique
Rabbit Anti β Actin Polyclonal Antibodies, supplied by Proteintech, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Proteintech rabbit anti pig mal monoclonal antibodies
Fig. 6 3D-ABs suppress oxidative stress and cell death, and stimulated angiogenesis in ischaemic flaps. (A) F-CHP staining for damaged collagen detec tion in the skin on POD7. Scale bars, 100 μm. (B) The three groups’ quantified F-CHP intensity (n = 6). (C) CD31 <t>and</t> <t>α-SMA</t> IF staining in the flap on POD7. Scale bars, 50 μm. (D) <t>Quantified</t> <t>CD31/α-SMA-positive</t> blood vessel density among the three groups (n = 6). (E) Dead cells in flap tissue sections on POD7 under the detection of TUNEL staining. Scale bar, 20 μm. (F) TUNEL-positive cell percentage in the dermal layer, quantified for each of the three groups (n = 6). (G) DHE staining of the skin tissues on POD7 among the three groups. Scale bars, 50 μm. (H) Quantified DHE among the three groups (n = 6). SEM error bars are used. Significance (*): p value < 0.05; equal variances ANOVA with LSD post hoc analysis or unequal variances Dunnett’s T3 technique
Rabbit Anti Pig Mal Monoclonal Antibodies, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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98
Proteintech β actin rabbit mab
Loss of RNF128 increases β-catenin protein level and its target genes in colorectal cancer. (A) The mRNA expressions of cyclin D1, cyclin E1, cyclin A1 and cyclin B1 were quantified in RNF128 knockdown or overexpression cells compared to their respective controls in DLD1. (B) β-catenin, CCND1, and RNF128 expressions were confirmed using Western blotting. <t>β-actin</t> was used as a loading control. (C) Expression of β-catenin and RNF128 in nuclear and cytoplasmic fractions in RNF128-knockdown cells and control cells of DLD1. β-tubulin was used as the cytoplasmic reference protein. LaminB1 was used as the nuclear reference protein. *P<0.05, **P<0.01 and ***P<0.001. No significant difference (P>0.05, ns). Data represented as mean ± SD.
β Actin Rabbit Mab, supplied by Proteintech, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech rabbit antibodies
Loss of RNF128 increases β-catenin protein level and its target genes in colorectal cancer. (A) The mRNA expressions of cyclin D1, cyclin E1, cyclin A1 and cyclin B1 were quantified in RNF128 knockdown or overexpression cells compared to their respective controls in DLD1. (B) β-catenin, CCND1, and RNF128 expressions were confirmed using Western blotting. <t>β-actin</t> was used as a loading control. (C) Expression of β-catenin and RNF128 in nuclear and cytoplasmic fractions in RNF128-knockdown cells and control cells of DLD1. β-tubulin was used as the cytoplasmic reference protein. LaminB1 was used as the nuclear reference protein. *P<0.05, **P<0.01 and ***P<0.001. No significant difference (P>0.05, ns). Data represented as mean ± SD.
Rabbit Antibodies, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Sanying Ltd antibody against α-sma 55135-1-ap
Loss of RNF128 increases β-catenin protein level and its target genes in colorectal cancer. (A) The mRNA expressions of cyclin D1, cyclin E1, cyclin A1 and cyclin B1 were quantified in RNF128 knockdown or overexpression cells compared to their respective controls in DLD1. (B) β-catenin, CCND1, and RNF128 expressions were confirmed using Western blotting. <t>β-actin</t> was used as a loading control. (C) Expression of β-catenin and RNF128 in nuclear and cytoplasmic fractions in RNF128-knockdown cells and control cells of DLD1. β-tubulin was used as the cytoplasmic reference protein. LaminB1 was used as the nuclear reference protein. *P<0.05, **P<0.01 and ***P<0.001. No significant difference (P>0.05, ns). Data represented as mean ± SD.
Antibody Against α Sma 55135 1 Ap, supplied by Sanying Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Fig. 6 3D-ABs suppress oxidative stress and cell death, and stimulated angiogenesis in ischaemic flaps. (A) F-CHP staining for damaged collagen detec tion in the skin on POD7. Scale bars, 100 μm. (B) The three groups’ quantified F-CHP intensity (n = 6). (C) CD31 and α-SMA IF staining in the flap on POD7. Scale bars, 50 μm. (D) Quantified CD31/α-SMA-positive blood vessel density among the three groups (n = 6). (E) Dead cells in flap tissue sections on POD7 under the detection of TUNEL staining. Scale bar, 20 μm. (F) TUNEL-positive cell percentage in the dermal layer, quantified for each of the three groups (n = 6). (G) DHE staining of the skin tissues on POD7 among the three groups. Scale bars, 50 μm. (H) Quantified DHE among the three groups (n = 6). SEM error bars are used. Significance (*): p value < 0.05; equal variances ANOVA with LSD post hoc analysis or unequal variances Dunnett’s T3 technique

Journal: Journal of nanobiotechnology

Article Title: Evaluating the pro-survival potential of apoptotic bodies derived from 2D- and 3D- cultured adipose stem cells in ischaemic flaps.

doi: 10.1186/s12951-024-02533-1

Figure Lengend Snippet: Fig. 6 3D-ABs suppress oxidative stress and cell death, and stimulated angiogenesis in ischaemic flaps. (A) F-CHP staining for damaged collagen detec tion in the skin on POD7. Scale bars, 100 μm. (B) The three groups’ quantified F-CHP intensity (n = 6). (C) CD31 and α-SMA IF staining in the flap on POD7. Scale bars, 50 μm. (D) Quantified CD31/α-SMA-positive blood vessel density among the three groups (n = 6). (E) Dead cells in flap tissue sections on POD7 under the detection of TUNEL staining. Scale bar, 20 μm. (F) TUNEL-positive cell percentage in the dermal layer, quantified for each of the three groups (n = 6). (G) DHE staining of the skin tissues on POD7 among the three groups. Scale bars, 50 μm. (H) Quantified DHE among the three groups (n = 6). SEM error bars are used. Significance (*): p value < 0.05; equal variances ANOVA with LSD post hoc analysis or unequal variances Dunnett’s T3 technique

Article Snippet: The primary antibodies utilized were specific to CD31 (1:200), CD68 (1:200), α-SMA (1:200; Proteintech, 67735-1-Ig), iNOS (1:200), and Arg1 (1:200).

Techniques: Staining, TUNEL Assay

Loss of RNF128 increases β-catenin protein level and its target genes in colorectal cancer. (A) The mRNA expressions of cyclin D1, cyclin E1, cyclin A1 and cyclin B1 were quantified in RNF128 knockdown or overexpression cells compared to their respective controls in DLD1. (B) β-catenin, CCND1, and RNF128 expressions were confirmed using Western blotting. β-actin was used as a loading control. (C) Expression of β-catenin and RNF128 in nuclear and cytoplasmic fractions in RNF128-knockdown cells and control cells of DLD1. β-tubulin was used as the cytoplasmic reference protein. LaminB1 was used as the nuclear reference protein. *P<0.05, **P<0.01 and ***P<0.001. No significant difference (P>0.05, ns). Data represented as mean ± SD.

Journal: American Journal of Translational Research

Article Title: RNF128 suppresses the malignancy of colorectal cancer cells via inhibition of Wnt/β-catenin signaling

doi:

Figure Lengend Snippet: Loss of RNF128 increases β-catenin protein level and its target genes in colorectal cancer. (A) The mRNA expressions of cyclin D1, cyclin E1, cyclin A1 and cyclin B1 were quantified in RNF128 knockdown or overexpression cells compared to their respective controls in DLD1. (B) β-catenin, CCND1, and RNF128 expressions were confirmed using Western blotting. β-actin was used as a loading control. (C) Expression of β-catenin and RNF128 in nuclear and cytoplasmic fractions in RNF128-knockdown cells and control cells of DLD1. β-tubulin was used as the cytoplasmic reference protein. LaminB1 was used as the nuclear reference protein. *P<0.05, **P<0.01 and ***P<0.001. No significant difference (P>0.05, ns). Data represented as mean ± SD.

Article Snippet: Supernatants were collected for measuring protein concentration by BCA assay (Thermofisher Scientific, USA). β-tubulin Rabbit mAb, Lamin B1 Rabbit mAb and β-actin Rabbit mAb were purchased from Proteintech (china); β-Catenin Rabbit mAb and CCND1 Rabbit mAb were from Cell Signaling Technology (USA); Ub and RNF128 Rat mAb were from Santa Cruz Biotechnology (USA); goat anti-rabbit and goat anti-rat were from Cell Signaling Technology (USA).

Techniques: Over Expression, Western Blot, Expressing