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rat col iii elisa kits  (Cusabio)


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    Cusabio rat col iii elisa kits
    Rat Col Iii Elisa Kits, supplied by Cusabio, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rat+collagen+type+iii+elisa+kit/10__1093_slash_burnst_slash_tkaf022-88-20-24?v=Cusabio
    Average 93 stars, based on 4 article reviews
    rat col iii elisa kits - by Bioz Stars, 2026-08
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    Cusabio rat col iii elisa kits
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    Novus Biologicals collagen type iii
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    Cusabio rat collagen type iii elisa kit
    Col <t>I/III</t> production from co-cultures with and without mechanically loaded myoblasts. ( A , D ) Relative mRNA expression of Col 1a1 and Col 3a1 in tenocytes. ( B , E ) Quantification of Col 1 content in tenocyte lysate by <t>ELISA.</t> ( C , F ) Quantification of Col I/III content and the ratio in the cell culture medium. ( G ) Immunofluorescence staining of Col I on tenocytes. Teno ctrl: tenocytes alone, Co ctrl: tenocytes co-cultured with myoblasts, Dyn: tenocyte co-cultured with dynamically loaded myoblasts, Stat: tenocyte co-cultured with statically loaded myoblasts. Data are represented as mean ± standard deviation. n = 3. Student’s t -test was performed when comparing Teno ctrl and co ctrl. One-way ANOVA with Tukey’s multiple comparisons was performed when comparing between Co ctrl, Dyn and Stat groups. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.
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    Elabscience Biotechnology rat collagen type iii
    Protein concentration in cell culture supernatants of ligament fibroblasts. Values were measured on the 6 th day and 10 th day after stimulation period for type <t>I</t> <t>collagen,</t> type <t>III</t> collagen, and fibronectin.
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    Abbexa Ltd rat collagen type iii elisa kit abx573727
    SGLT1 is downregulated in the experimental diabetic cardiac fibrosis model and high-glucose–induced CFs. (A) The mRNA level of SGLT1 was detected using RT‐qPCR ( n = 6). (B) The protein level of SGLT1 was analyzed using western blot analysis ( n = 6). (C) The protein levels of SGLT1, collagen I, and <t>collagen</t> <t>III</t> were evaluated using immunohistochemical staining. Relative expression of SGLT1 (D) and collagen I and collagen III (E) was found using semiquantitative analysis based on immunohistochemistry. (F) The morphology of CFs with or without high-glucose stimulation was imaged under an optical microscope. (G) The protein level of SGLT1 was analyzed by immunofluorescent staining in high-glucose–induced CFs. (H) The protein levels of SGLT1, collagen I, and collagen III were analyzed using western blot analysis in high-glucose–induced CFs ( n = 3).
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    Cusabio collagen type iii level
    In the in vitro model of arachnoid cell fibrosis, the expression of miR-30a decreased, and the expression of TRAF3IP2 was upregulated. (a) Differential mRNA expression of miR-30a, TRAF3IP2, and TGF-β1 in arachnoid cells between the fibrotic group and control group (** P < 0.01 compared with the control group). (b) Differential protein expression of TRAF3IP2, TGF-β1, and α-SMA in arachnoid cells between the fibrotic and control groups (** P < 0.01 compared with the control group; * P < 0.05 compared with the control group). (c) Differential content of collagen I and <t>collagen</t> <t>III</t> in the model of arachnoid cell fibrosis (** P < 0.01 compared with the control group).
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    Image Search Results


    Col I/III production from co-cultures with and without mechanically loaded myoblasts. ( A , D ) Relative mRNA expression of Col 1a1 and Col 3a1 in tenocytes. ( B , E ) Quantification of Col 1 content in tenocyte lysate by ELISA. ( C , F ) Quantification of Col I/III content and the ratio in the cell culture medium. ( G ) Immunofluorescence staining of Col I on tenocytes. Teno ctrl: tenocytes alone, Co ctrl: tenocytes co-cultured with myoblasts, Dyn: tenocyte co-cultured with dynamically loaded myoblasts, Stat: tenocyte co-cultured with statically loaded myoblasts. Data are represented as mean ± standard deviation. n = 3. Student’s t -test was performed when comparing Teno ctrl and co ctrl. One-way ANOVA with Tukey’s multiple comparisons was performed when comparing between Co ctrl, Dyn and Stat groups. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Journal: International Journal of Molecular Sciences

    Article Title: Secretome from In Vitro Mechanically Loaded Myoblasts Induces Tenocyte Migration, Transition to a Fibroblastic Phenotype and Suppression of Collagen Production

    doi: 10.3390/ijms222313089

    Figure Lengend Snippet: Col I/III production from co-cultures with and without mechanically loaded myoblasts. ( A , D ) Relative mRNA expression of Col 1a1 and Col 3a1 in tenocytes. ( B , E ) Quantification of Col 1 content in tenocyte lysate by ELISA. ( C , F ) Quantification of Col I/III content and the ratio in the cell culture medium. ( G ) Immunofluorescence staining of Col I on tenocytes. Teno ctrl: tenocytes alone, Co ctrl: tenocytes co-cultured with myoblasts, Dyn: tenocyte co-cultured with dynamically loaded myoblasts, Stat: tenocyte co-cultured with statically loaded myoblasts. Data are represented as mean ± standard deviation. n = 3. Student’s t -test was performed when comparing Teno ctrl and co ctrl. One-way ANOVA with Tukey’s multiple comparisons was performed when comparing between Co ctrl, Dyn and Stat groups. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Article Snippet: Collagen I and collagen III were assessed using Rat Collagen Type I ELISA kit (Cusabio, Wuhan, China, #CSB-E08084r) and Rat Collagen Type III ELISA kit (Cusabio, Wuhan, China, #CSB-E07924r) according to the manufacturer’s protocol.

    Techniques: Expressing, Enzyme-linked Immunosorbent Assay, Cell Culture, Immunofluorescence, Staining, Standard Deviation

    Protein concentration in cell culture supernatants of ligament fibroblasts. Values were measured on the 6 th day and 10 th day after stimulation period for type I collagen, type III collagen, and fibronectin.

    Journal: bioRxiv

    Article Title: Effect of therapeutic ultrasound on the mechanical and biological properties of fibroblasts

    doi: 10.1101/2021.11.22.469508

    Figure Lengend Snippet: Protein concentration in cell culture supernatants of ligament fibroblasts. Values were measured on the 6 th day and 10 th day after stimulation period for type I collagen, type III collagen, and fibronectin.

    Article Snippet: We used rat collagen type I (E-EL-R0233), rat collagen type III (E-EL-R0235), and rat fibronectin (E-EL-R0578) Elabscience® ELISA kits.

    Techniques: Protein Concentration, Cell Culture

    SGLT1 is downregulated in the experimental diabetic cardiac fibrosis model and high-glucose–induced CFs. (A) The mRNA level of SGLT1 was detected using RT‐qPCR ( n = 6). (B) The protein level of SGLT1 was analyzed using western blot analysis ( n = 6). (C) The protein levels of SGLT1, collagen I, and collagen III were evaluated using immunohistochemical staining. Relative expression of SGLT1 (D) and collagen I and collagen III (E) was found using semiquantitative analysis based on immunohistochemistry. (F) The morphology of CFs with or without high-glucose stimulation was imaged under an optical microscope. (G) The protein level of SGLT1 was analyzed by immunofluorescent staining in high-glucose–induced CFs. (H) The protein levels of SGLT1, collagen I, and collagen III were analyzed using western blot analysis in high-glucose–induced CFs ( n = 3).

    Journal: Frontiers in Pharmacology

    Article Title: SGLT1 Knockdown Attenuates Cardiac Fibroblast Activation in Diabetic Cardiac Fibrosis

    doi: 10.3389/fphar.2021.700366

    Figure Lengend Snippet: SGLT1 is downregulated in the experimental diabetic cardiac fibrosis model and high-glucose–induced CFs. (A) The mRNA level of SGLT1 was detected using RT‐qPCR ( n = 6). (B) The protein level of SGLT1 was analyzed using western blot analysis ( n = 6). (C) The protein levels of SGLT1, collagen I, and collagen III were evaluated using immunohistochemical staining. Relative expression of SGLT1 (D) and collagen I and collagen III (E) was found using semiquantitative analysis based on immunohistochemistry. (F) The morphology of CFs with or without high-glucose stimulation was imaged under an optical microscope. (G) The protein level of SGLT1 was analyzed by immunofluorescent staining in high-glucose–induced CFs. (H) The protein levels of SGLT1, collagen I, and collagen III were analyzed using western blot analysis in high-glucose–induced CFs ( n = 3).

    Article Snippet: The expression levels of collagen I, collagen III, and transforming growth factor-β1 (TGF-β1) in CFs and rat serum were detected using the rat collagen I Type I ELISA Kit (abx052369, Abbexa, United Kingdom), rat collagen type III ELISA Kit (abx573727, Abbexa), and TGF-β1 ELISA Kit (PT878, Beyotime, Jiangsu, China), respectively, following the instructions of the manufacturer.

    Techniques: Quantitative RT-PCR, Western Blot, Immunohistochemical staining, Staining, Expressing, Immunohistochemistry, Microscopy

    Knockdown of SGLT1 inhibited high-glucose–induced CF activation. CFs were transfected with SGLT1 siRNAs, and SGLT1 mRNA and protein levels were detected using RT‐qPCR (A) and western blotting, respectively (B) . CCK-8 assay was used to detect the proliferation of CFs under high-glucose condition with or without SGLT1 inhibition. (D, E) The representative images of the wound-healing assay were obtained at 0 and 24 h after knockdown of SGLT1, and the migrative ability of CFs was compared. (F–H) ELISA was used to detect the levels of collagen-synthesis–related markers, including TGF-β1, collagen I, and collagen III in the cell supernatant ( n = 6). (I) Western blotting analysis was performed to investigate the phosphorylation levels of p38 mitogen-activated protein kinase (MAPK) and extracellular signal-regulated kinase (ERK)1/2 in CFs under high-glucose condition with or without SGLT1 inhibition.

    Journal: Frontiers in Pharmacology

    Article Title: SGLT1 Knockdown Attenuates Cardiac Fibroblast Activation in Diabetic Cardiac Fibrosis

    doi: 10.3389/fphar.2021.700366

    Figure Lengend Snippet: Knockdown of SGLT1 inhibited high-glucose–induced CF activation. CFs were transfected with SGLT1 siRNAs, and SGLT1 mRNA and protein levels were detected using RT‐qPCR (A) and western blotting, respectively (B) . CCK-8 assay was used to detect the proliferation of CFs under high-glucose condition with or without SGLT1 inhibition. (D, E) The representative images of the wound-healing assay were obtained at 0 and 24 h after knockdown of SGLT1, and the migrative ability of CFs was compared. (F–H) ELISA was used to detect the levels of collagen-synthesis–related markers, including TGF-β1, collagen I, and collagen III in the cell supernatant ( n = 6). (I) Western blotting analysis was performed to investigate the phosphorylation levels of p38 mitogen-activated protein kinase (MAPK) and extracellular signal-regulated kinase (ERK)1/2 in CFs under high-glucose condition with or without SGLT1 inhibition.

    Article Snippet: The expression levels of collagen I, collagen III, and transforming growth factor-β1 (TGF-β1) in CFs and rat serum were detected using the rat collagen I Type I ELISA Kit (abx052369, Abbexa, United Kingdom), rat collagen type III ELISA Kit (abx573727, Abbexa), and TGF-β1 ELISA Kit (PT878, Beyotime, Jiangsu, China), respectively, following the instructions of the manufacturer.

    Techniques: Knockdown, Activation Assay, Transfection, Quantitative RT-PCR, Western Blot, CCK-8 Assay, Inhibition, Wound Healing Assay, Enzyme-linked Immunosorbent Assay, Phospho-proteomics

    SGLT1 overexpression promotes collagen release via the p38 and ERK1/2 signaling pathway in CFs. CFs were transfected with an SGLT1 plasmid or vector, and SGLT1 expression levels were detected using RT‐qPCR (A) or western blotting analysis (B) . (C) After overexpression of SGLT1 in CFs, CCK-8 assay was used to detect the proliferation of CFs under normal or high-glucose condition ( n = 6). (D–F) After overexpressing SGLT1 in CFs, the collagen-synthesis–related markers, including TGF-β1, collagen I, and collagen III, in the cell supernatant were measured using ELISA ( n = 6). (G) After overexpressing SGLT1 in CFs, the protein levels of phosphorylated p38 and p-ERK1/2 were analyzed using western blotting in CFs both under normal or high-glucose condition ( n = 3).

    Journal: Frontiers in Pharmacology

    Article Title: SGLT1 Knockdown Attenuates Cardiac Fibroblast Activation in Diabetic Cardiac Fibrosis

    doi: 10.3389/fphar.2021.700366

    Figure Lengend Snippet: SGLT1 overexpression promotes collagen release via the p38 and ERK1/2 signaling pathway in CFs. CFs were transfected with an SGLT1 plasmid or vector, and SGLT1 expression levels were detected using RT‐qPCR (A) or western blotting analysis (B) . (C) After overexpression of SGLT1 in CFs, CCK-8 assay was used to detect the proliferation of CFs under normal or high-glucose condition ( n = 6). (D–F) After overexpressing SGLT1 in CFs, the collagen-synthesis–related markers, including TGF-β1, collagen I, and collagen III, in the cell supernatant were measured using ELISA ( n = 6). (G) After overexpressing SGLT1 in CFs, the protein levels of phosphorylated p38 and p-ERK1/2 were analyzed using western blotting in CFs both under normal or high-glucose condition ( n = 3).

    Article Snippet: The expression levels of collagen I, collagen III, and transforming growth factor-β1 (TGF-β1) in CFs and rat serum were detected using the rat collagen I Type I ELISA Kit (abx052369, Abbexa, United Kingdom), rat collagen type III ELISA Kit (abx573727, Abbexa), and TGF-β1 ELISA Kit (PT878, Beyotime, Jiangsu, China), respectively, following the instructions of the manufacturer.

    Techniques: Over Expression, Transfection, Plasmid Preparation, Expressing, Quantitative RT-PCR, Western Blot, CCK-8 Assay, Enzyme-linked Immunosorbent Assay

    SGLT1 inhibition alleviated myocardial fibrosis and apoptosis in diabetic rat hearts ( n = 6). (A, B) Knockdown of SGLT1 was achieved by continuous intravenous injection into the tail vein with specific SGLT1 siRNA in DCM rats, and the knockdown efficiency was identified by detecting SGLT1 expression in myocardial tissues using RT-qPCR and western blotting analysis. (C) SGLT1 protein levels in myocardial tissue were measured by immunohistochemistry staining. (D) Masson’s trichrome staining of myocardial tissue shows interstitial fibrosis in DCM rats treated with si-NC or si-SGLT1. (E, F) Relative protein levels of collagen I and collagen III in myocardial tissue were measured using immunohistochemical staining and western blotting analysis ( n = 6). (G) Wheat germ agglutinin staining and quantitation of myocardial cell size in DCM rats treated with si-NC or si-SGLT1 ( n = 6).

    Journal: Frontiers in Pharmacology

    Article Title: SGLT1 Knockdown Attenuates Cardiac Fibroblast Activation in Diabetic Cardiac Fibrosis

    doi: 10.3389/fphar.2021.700366

    Figure Lengend Snippet: SGLT1 inhibition alleviated myocardial fibrosis and apoptosis in diabetic rat hearts ( n = 6). (A, B) Knockdown of SGLT1 was achieved by continuous intravenous injection into the tail vein with specific SGLT1 siRNA in DCM rats, and the knockdown efficiency was identified by detecting SGLT1 expression in myocardial tissues using RT-qPCR and western blotting analysis. (C) SGLT1 protein levels in myocardial tissue were measured by immunohistochemistry staining. (D) Masson’s trichrome staining of myocardial tissue shows interstitial fibrosis in DCM rats treated with si-NC or si-SGLT1. (E, F) Relative protein levels of collagen I and collagen III in myocardial tissue were measured using immunohistochemical staining and western blotting analysis ( n = 6). (G) Wheat germ agglutinin staining and quantitation of myocardial cell size in DCM rats treated with si-NC or si-SGLT1 ( n = 6).

    Article Snippet: The expression levels of collagen I, collagen III, and transforming growth factor-β1 (TGF-β1) in CFs and rat serum were detected using the rat collagen I Type I ELISA Kit (abx052369, Abbexa, United Kingdom), rat collagen type III ELISA Kit (abx573727, Abbexa), and TGF-β1 ELISA Kit (PT878, Beyotime, Jiangsu, China), respectively, following the instructions of the manufacturer.

    Techniques: Inhibition, Knockdown, Injection, Expressing, Quantitative RT-PCR, Western Blot, Immunohistochemistry, Staining, Immunohistochemical staining, Quantitation Assay

    In the in vitro model of arachnoid cell fibrosis, the expression of miR-30a decreased, and the expression of TRAF3IP2 was upregulated. (a) Differential mRNA expression of miR-30a, TRAF3IP2, and TGF-β1 in arachnoid cells between the fibrotic group and control group (** P < 0.01 compared with the control group). (b) Differential protein expression of TRAF3IP2, TGF-β1, and α-SMA in arachnoid cells between the fibrotic and control groups (** P < 0.01 compared with the control group; * P < 0.05 compared with the control group). (c) Differential content of collagen I and collagen III in the model of arachnoid cell fibrosis (** P < 0.01 compared with the control group).

    Journal: Translational Neuroscience

    Article Title: Decreased MiR-30a promotes TGF-β1-mediated arachnoid fibrosis in post-hemorrhagic hydrocephalus

    doi: 10.1515/tnsci-2020-0010

    Figure Lengend Snippet: In the in vitro model of arachnoid cell fibrosis, the expression of miR-30a decreased, and the expression of TRAF3IP2 was upregulated. (a) Differential mRNA expression of miR-30a, TRAF3IP2, and TGF-β1 in arachnoid cells between the fibrotic group and control group (** P < 0.01 compared with the control group). (b) Differential protein expression of TRAF3IP2, TGF-β1, and α-SMA in arachnoid cells between the fibrotic and control groups (** P < 0.01 compared with the control group; * P < 0.05 compared with the control group). (c) Differential content of collagen I and collagen III in the model of arachnoid cell fibrosis (** P < 0.01 compared with the control group).

    Article Snippet: ELISA kit was used to detect the TGF-β1 level (EK0514, Wuhan Boster Biological Technology, Ltd, China), collagen type I level (CSB-E08084r, CUSABIO, China), and collagen type III level (CSB-E07924r, CUSABIO, China) following the protocols constructions.

    Techniques: In Vitro, Expressing, Control

    MiR-30a inhibits subarachnoid fibrosis through inhibiting TRAF3IP2. (a and b) The mRNA and protein expression of miR-30a, TRAF3IP2, TGF-β1 and α-SMA from different groups (** P < 0.01 compared with the control group; *** P < 0.001 compared with the control group). (c) The content of collagen I and collagen III from different groups (*** P < 0.001 compared with the control group. ** P < 0.01 compared with the control group; * P < 0.05 compared with the control group).

    Journal: Translational Neuroscience

    Article Title: Decreased MiR-30a promotes TGF-β1-mediated arachnoid fibrosis in post-hemorrhagic hydrocephalus

    doi: 10.1515/tnsci-2020-0010

    Figure Lengend Snippet: MiR-30a inhibits subarachnoid fibrosis through inhibiting TRAF3IP2. (a and b) The mRNA and protein expression of miR-30a, TRAF3IP2, TGF-β1 and α-SMA from different groups (** P < 0.01 compared with the control group; *** P < 0.001 compared with the control group). (c) The content of collagen I and collagen III from different groups (*** P < 0.001 compared with the control group. ** P < 0.01 compared with the control group; * P < 0.05 compared with the control group).

    Article Snippet: ELISA kit was used to detect the TGF-β1 level (EK0514, Wuhan Boster Biological Technology, Ltd, China), collagen type I level (CSB-E08084r, CUSABIO, China), and collagen type III level (CSB-E07924r, CUSABIO, China) following the protocols constructions.

    Techniques: Expressing, Control