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Novus Biologicals polyclonal rabbit anti erp57
Polyclonal Rabbit Anti Erp57, 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
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Average 93 stars, based on 1 article reviews

polyclonal rabbit anti erp57 - by Bioz Stars, 2026-06

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ERp57 KO mice display severe structural ECM defects in knee joint cartilage High-magnification transmission electron microscopic (TEM) analysis of articular cartilage isolated from 18-week-old WT and ERp57 KO mouse knees. KO samples exhibit a significantly lower ECM density around chondrocytes with holes in the territorial/interterritorial matrix (marked with arrows) (A). In microphotographs of WT samples, an average of 96% of the total area was covered with dense matrix, compared to 79% in the KO (B). Statistical evaluation was performed with Student’s t test. Data are mean ± SD. ∗∗ represents a p -value of <0.01. N (number of animals per genotype) ≥ 4; n (number of analyzed images per genotype) = 8; scale bars = 1 μm.

Journal: iScience

Article Title: Extracellular ERp57 promotes fibronectin fibril formation during matrix assembly of articular cartilage

doi: 10.1016/j.isci.2025.114046

Figure Lengend Snippet: ERp57 KO mice display severe structural ECM defects in knee joint cartilage High-magnification transmission electron microscopic (TEM) analysis of articular cartilage isolated from 18-week-old WT and ERp57 KO mouse knees. KO samples exhibit a significantly lower ECM density around chondrocytes with holes in the territorial/interterritorial matrix (marked with arrows) (A). In microphotographs of WT samples, an average of 96% of the total area was covered with dense matrix, compared to 79% in the KO (B). Statistical evaluation was performed with Student’s t test. Data are mean ± SD. ∗∗ represents a p -value of <0.01. N (number of animals per genotype) ≥ 4; n (number of analyzed images per genotype) = 8; scale bars = 1 μm.

Article Snippet: To analyze PDI, extracellular ERp57 or Col II-containing fibrils, a rabbit polyclonal PDI antibody (sc-20132, Santa Cruz Biotechnology, USA, 1:50), a rabbit polyclonal ERp57 antibody (NBP1-84796, Novus, Centennial, USA,1:200) or monoclonal mouse Collagen II antibodies (MAB8887, Merck Darmstadt, Germany, 1:200, or DSHB II6B3, 1:200) were applied.

Techniques: Transmission Assay, Isolation

Primary ERp57 KO chondrocytes produce less fibrillar matrix than WT cells Transmission electron microscopic (TEM) analysis of micromass cultures of primary WT and ERp57 KO chondrocytes isolated from knee joints of newborn mice revealed fewer and shorter cartilage fibrils in KO samples compared to WT controls (A), although the cell number is comparable (B). In microphotographs of WT samples, an average of 37% of the total area was covered with fibrils, compared to 25% in the KO (C). Statistical evaluation was performed with Student’s t test. Data are mean ± SD. ∗∗ represents a p -value of <0.01. ns indicates non-significant p -values. N (number of animals per genotype) = 4; n (number of micromasses per genotype) ≥ 10; scale bars = 500 nm.

Journal: iScience

Article Title: Extracellular ERp57 promotes fibronectin fibril formation during matrix assembly of articular cartilage

doi: 10.1016/j.isci.2025.114046

Figure Lengend Snippet: Primary ERp57 KO chondrocytes produce less fibrillar matrix than WT cells Transmission electron microscopic (TEM) analysis of micromass cultures of primary WT and ERp57 KO chondrocytes isolated from knee joints of newborn mice revealed fewer and shorter cartilage fibrils in KO samples compared to WT controls (A), although the cell number is comparable (B). In microphotographs of WT samples, an average of 37% of the total area was covered with fibrils, compared to 25% in the KO (C). Statistical evaluation was performed with Student’s t test. Data are mean ± SD. ∗∗ represents a p -value of <0.01. ns indicates non-significant p -values. N (number of animals per genotype) = 4; n (number of micromasses per genotype) ≥ 10; scale bars = 500 nm.

Techniques: Transmission Assay, Isolation

Cultured C28/I2 ERp57 KO cells exhibit a reduced extracellular network of fibronectin 1 but unchanged collagen II fibrils Immunofluorescence analyses of the extracellular matrix (ECM) produced by C28/I2 WT and C28/I2 ERp57 KO chondrocytes, examined after fixation (Cells + Matrix) or after decellularization and fixation (Matrix) to visualize the ECM fibrils without cell-derived signals. The figure shows the projections of z-stacks. Punctate Col II signals in non-decellularized samples (Cells + Matrix) reveal Col II-containing vesicles near/above the nuclei of chondrocytes. Fibronectin (FN1) and collagen II (Col II) fibrils were detected in WT samples, including cells and matrix, and also in decellularized samples containing only matrix. The FN1 network was significantly reduced in KO samples (A). In contrast, the Col II network was comparably well developed in ERp57 KO and WT cells (B). Quantitative analysis of the decellularized samples revealed a reduction in the mean staining intensity of the FN1 matrix by more than 60% in the KO samples compared to WT controls and no statistically significant difference in Col II staining in samples of both genotypes. (C) Statistical evaluation was performed with the Student’s t test. Data are mean ± SD. ∗∗∗∗ represents a p -value of <0.0001, ns indicates non-significant p -values. N ≥ 8 (number of experiments), n ≥ 30 (technical replicates). Scale bars = 20 μm.

Journal: iScience

Article Title: Extracellular ERp57 promotes fibronectin fibril formation during matrix assembly of articular cartilage

doi: 10.1016/j.isci.2025.114046

Figure Lengend Snippet: Cultured C28/I2 ERp57 KO cells exhibit a reduced extracellular network of fibronectin 1 but unchanged collagen II fibrils Immunofluorescence analyses of the extracellular matrix (ECM) produced by C28/I2 WT and C28/I2 ERp57 KO chondrocytes, examined after fixation (Cells + Matrix) or after decellularization and fixation (Matrix) to visualize the ECM fibrils without cell-derived signals. The figure shows the projections of z-stacks. Punctate Col II signals in non-decellularized samples (Cells + Matrix) reveal Col II-containing vesicles near/above the nuclei of chondrocytes. Fibronectin (FN1) and collagen II (Col II) fibrils were detected in WT samples, including cells and matrix, and also in decellularized samples containing only matrix. The FN1 network was significantly reduced in KO samples (A). In contrast, the Col II network was comparably well developed in ERp57 KO and WT cells (B). Quantitative analysis of the decellularized samples revealed a reduction in the mean staining intensity of the FN1 matrix by more than 60% in the KO samples compared to WT controls and no statistically significant difference in Col II staining in samples of both genotypes. (C) Statistical evaluation was performed with the Student’s t test. Data are mean ± SD. ∗∗∗∗ represents a p -value of <0.0001, ns indicates non-significant p -values. N ≥ 8 (number of experiments), n ≥ 30 (technical replicates). Scale bars = 20 μm.

Techniques: Cell Culture, Immunofluorescence, Produced, Derivative Assay, Staining

Extracellular ERp57 colocalizes with fibronectin 1 fibrils Co-Immunofluorescence analysis of FN1/ERp57 (A, top panel) and Col II/ERp57 (B, bottom panel) on decellularized matrices. In C28/I2 WT samples, ERp57 was detected on FN1 fibrils in different quantities (← ERp57 high, FN1 high, < ERp57 high, FN1 low, ∗ ERp57 low, FN1 high). The Col II network showed no direct colocalization with ERp57, however ERp57 was detectable in close vicinity to Col II structures (◄). N = 3. Scale bars = 20 μm.

Journal: iScience

Article Title: Extracellular ERp57 promotes fibronectin fibril formation during matrix assembly of articular cartilage

doi: 10.1016/j.isci.2025.114046

Figure Lengend Snippet: Extracellular ERp57 colocalizes with fibronectin 1 fibrils Co-Immunofluorescence analysis of FN1/ERp57 (A, top panel) and Col II/ERp57 (B, bottom panel) on decellularized matrices. In C28/I2 WT samples, ERp57 was detected on FN1 fibrils in different quantities (← ERp57 high, FN1 high, < ERp57 high, FN1 low, ∗ ERp57 low, FN1 high). The Col II network showed no direct colocalization with ERp57, however ERp57 was detectable in close vicinity to Col II structures (◄). N = 3. Scale bars = 20 μm.

Techniques: Immunofluorescence

Extracellular ERp57 interacts directly with fibronectin 1 fibrils Proximity ligation assays (PLA) showed FN1/ERp57 interactions, visible as red dots on fibrillar structures of the extracellular matrix (ECM) (A). The corresponding statistical analysis (B) revealed a mean staining intensity of 0.284 ± 0.1065, which differed significantly from the mean staining intensities in the matrix of ERp57 KO cells and in the negative control (WT matrix without primary antibodies). In contrast, no interactions between Col II and ERp57 were detectable using PLA. The mean staining intensity in the WT-produced ECM did not exceed the background staining of the fibrils produced by ERp57 KO cells or the negative control (WT matrix without both primary antibodies). Short-term incubation with the reducing agent dithiothreitol (DTT) reduced PLA signals (C and D) significantly. Omission of ERp57 or FN1 antibodies reduced PLA signals to background levels (D). Statistical evaluation was performed with one-way ANOVA with Tukey’s post-hoc-test. Data are mean ± SD. ∗ represents a p -value of <0.05. N = 3 (number of experiments), n = 12 (technical replicates). Scale bars = 20 μm.

Journal: iScience

Article Title: Extracellular ERp57 promotes fibronectin fibril formation during matrix assembly of articular cartilage

doi: 10.1016/j.isci.2025.114046

Figure Lengend Snippet: Extracellular ERp57 interacts directly with fibronectin 1 fibrils Proximity ligation assays (PLA) showed FN1/ERp57 interactions, visible as red dots on fibrillar structures of the extracellular matrix (ECM) (A). The corresponding statistical analysis (B) revealed a mean staining intensity of 0.284 ± 0.1065, which differed significantly from the mean staining intensities in the matrix of ERp57 KO cells and in the negative control (WT matrix without primary antibodies). In contrast, no interactions between Col II and ERp57 were detectable using PLA. The mean staining intensity in the WT-produced ECM did not exceed the background staining of the fibrils produced by ERp57 KO cells or the negative control (WT matrix without both primary antibodies). Short-term incubation with the reducing agent dithiothreitol (DTT) reduced PLA signals (C and D) significantly. Omission of ERp57 or FN1 antibodies reduced PLA signals to background levels (D). Statistical evaluation was performed with one-way ANOVA with Tukey’s post-hoc-test. Data are mean ± SD. ∗ represents a p -value of <0.05. N = 3 (number of experiments), n = 12 (technical replicates). Scale bars = 20 μm.

Techniques: Ligation, Staining, Negative Control, Produced, Incubation

Active recombinant ERp57 protein added to the culture medium increases the fibronectin 1 fibrillogenesis around ERp57 KO cells in vitro Immunofluorecence analysis of FN1 and Col II on decellularized matrices of C28/I2 WT and C28/I2 ERp57 KO cells. Some of the KO cells were cultured for the entire culture period of 72 h in the presence of 0.1 μM active recombinant ERp57 protein or in the presence of 0.1 μM active recombinant ERp57 protein with the addition of 5 μM p -Chloromercuriphenylsulfonate (pCMPS) or 300 μM Monobromo (trimethylammonio) bimanbromide (QBBR) (A). KO cells showed in the quantitative analysis a strongly reduced staining intensity of FN1 and an unchanged staining intensity of Col II (B). The addition of active recombinant ERp57 protein to the cell culture medium of KO cells led to an increase in the mean staining intensity of FN1 (partial rescue), which was reduced again by the simultaneous addition of pCMPS and QBBR. The staining intensity of Col II was not significantly affected by the addition of active recombinant ERp57 protein in the presence or absence of pCMPS or QBBR. Statistical evaluation was performed with two-way ANOVA with Tukey’s post-hoc-test. Data are mean ± SD. ∗∗∗∗ represents a p -value of p < 0.0001, ∗∗ represents a p -value of p < 0.01, ns indicates non-significant p -values. N ≥ 5 (number of experiments), n ≥ 16 (technical replicates). Scale bars = 20 μm.

Journal: iScience

Article Title: Extracellular ERp57 promotes fibronectin fibril formation during matrix assembly of articular cartilage

doi: 10.1016/j.isci.2025.114046

Figure Lengend Snippet: Active recombinant ERp57 protein added to the culture medium increases the fibronectin 1 fibrillogenesis around ERp57 KO cells in vitro Immunofluorecence analysis of FN1 and Col II on decellularized matrices of C28/I2 WT and C28/I2 ERp57 KO cells. Some of the KO cells were cultured for the entire culture period of 72 h in the presence of 0.1 μM active recombinant ERp57 protein or in the presence of 0.1 μM active recombinant ERp57 protein with the addition of 5 μM p -Chloromercuriphenylsulfonate (pCMPS) or 300 μM Monobromo (trimethylammonio) bimanbromide (QBBR) (A). KO cells showed in the quantitative analysis a strongly reduced staining intensity of FN1 and an unchanged staining intensity of Col II (B). The addition of active recombinant ERp57 protein to the cell culture medium of KO cells led to an increase in the mean staining intensity of FN1 (partial rescue), which was reduced again by the simultaneous addition of pCMPS and QBBR. The staining intensity of Col II was not significantly affected by the addition of active recombinant ERp57 protein in the presence or absence of pCMPS or QBBR. Statistical evaluation was performed with two-way ANOVA with Tukey’s post-hoc-test. Data are mean ± SD. ∗∗∗∗ represents a p -value of p < 0.0001, ∗∗ represents a p -value of p < 0.01, ns indicates non-significant p -values. N ≥ 5 (number of experiments), n ≥ 16 (technical replicates). Scale bars = 20 μm.

Techniques: Recombinant, In Vitro, Cell Culture, Staining

Figure 2. The PDIA4 expression level is upregulated by LCMV infection both in vitro and in vivo. (A) The expression level of LCMV-NP in A549 cells at 12, 24, 36, and 48 h.p.i. determined by RT-PCR. (B) The expression level of detectable PDIs in A549 cells at 12, 24, 36, and 48 h.p.i. determined by RT-PCR. (C) The protein expression level of PDIA3, PDIA4, PDIA5, and PDIA6 in mock-/LCMV- infected A549 cells at 12, 24, 36, and 48 h.p.i. determined by Western blot. (D) The protein expression level of PDIA3, PDIA4, PDIA5, and PDIA6 in mock-/LCMV-infected HEK293T cells at 12, 24, 36, and 48 h.p.i. determined by Western blot. (E) The protein expression level of PDIA3, PDIA4, PDIA5, and PDIA6 in mock-/LCMV-infected NHBE cells at 48 h.p.i. determined by Western blot. (F) The relative mRNA expression level of PDIA4 in the kidney and lung of mock-/LCMV-infected mice (relative to mock, n = 5, unpaired t test). *** p < 0.001, **** p < 0.0001.

Journal: Viruses

Article Title: PDIA4 Is a Host Factor Important for Lymphocytic Choriomeningitis Virus Infection.

doi: 10.3390/v15122343

Figure Lengend Snippet: Figure 2. The PDIA4 expression level is upregulated by LCMV infection both in vitro and in vivo. (A) The expression level of LCMV-NP in A549 cells at 12, 24, 36, and 48 h.p.i. determined by RT-PCR. (B) The expression level of detectable PDIs in A549 cells at 12, 24, 36, and 48 h.p.i. determined by RT-PCR. (C) The protein expression level of PDIA3, PDIA4, PDIA5, and PDIA6 in mock-/LCMV- infected A549 cells at 12, 24, 36, and 48 h.p.i. determined by Western blot. (D) The protein expression level of PDIA3, PDIA4, PDIA5, and PDIA6 in mock-/LCMV-infected HEK293T cells at 12, 24, 36, and 48 h.p.i. determined by Western blot. (E) The protein expression level of PDIA3, PDIA4, PDIA5, and PDIA6 in mock-/LCMV-infected NHBE cells at 48 h.p.i. determined by Western blot. (F) The relative mRNA expression level of PDIA4 in the kidney and lung of mock-/LCMV-infected mice (relative to mock, n = 5, unpaired t test). *** p < 0.001, **** p < 0.0001.

Article Snippet: The anti-PDIA3 rabbit polyclonal antibody (15967-1-AP), antiPDIA4 rabbit polyclonal antibody (14712-1-AP), anti-PDIA5 rabbit polyclonal antibody (15545-1-AP), anti-V5 antibody (14440-1-AP), horseradish peroxidase (HRP)-conjugated goat anti-rabbit IgG(H+L) (SA00001-2), and HRP-conjugated goat anti-mouse IgG(H+L) (SA00001-1) were purchased from Proteintech Group (Wuhan, China).

Techniques: Expressing, Infection, In Vitro, In Vivo, Reverse Transcription Polymerase Chain Reaction, Western Blot

Fig. 1. The mRNA expression of PDIA3 in multiple human cancers. (A) The mRNA level of PDIA3 in different kinds of cancer lines, which were obtained from TIMER database. (B-S) The mRNA expression of PDIA3 in several malignancies, which were based on TCGA and GTEx normal tissues obtained from GEPIA datasets. *P value <0.05, **P value <0.01, ***P value <0.001.

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 1. The mRNA expression of PDIA3 in multiple human cancers. (A) The mRNA level of PDIA3 in different kinds of cancer lines, which were obtained from TIMER database. (B-S) The mRNA expression of PDIA3 in several malignancies, which were based on TCGA and GTEx normal tissues obtained from GEPIA datasets. *P value <0.05, **P value <0.01, ***P value <0.001.

Article Snippet: After blocking the membranes with 5% skimmed milk at room temperature for 2 h, we incubated them overnight with rabbit anti-GAPDH polyclonal antibody (cat. No. 10494–1-AP, Proteintech, Wuhan, China) and rabbit anti-PDIA3 polyclonal antibody (cat. No. 15967–1-AP, Proteintech, Wuhan, China) at 4 ◦C.

Techniques: Expressing

Fig. 2. The overall survival (OS) analysis of the expression of PDIA3 in various cancers was performed by using the GEPIA database. The OS plot of PDIA3 in BLCA (A), BRCA (B), CESC (C), CHOL (D), COAD (E), ESCA (F), HNSC(G), KICH (H), KIRC (I), KIRP (J), LIHC (K), LUAD (L), LUSC (M), PRAD (N), READ (O), STAD (P), THCA (Q), UCEC (R).

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 2. The overall survival (OS) analysis of the expression of PDIA3 in various cancers was performed by using the GEPIA database. The OS plot of PDIA3 in BLCA (A), BRCA (B), CESC (C), CHOL (D), COAD (E), ESCA (F), HNSC(G), KICH (H), KIRC (I), KIRP (J), LIHC (K), LUAD (L), LUSC (M), PRAD (N), READ (O), STAD (P), THCA (Q), UCEC (R).

Techniques: Expressing

Fig. 3. The disease-free survival (DFS) analysis of the expression of PDIA3 in various cancers was performed by using GEPIA database. The RFS plot of PDIA3 in BLCA (A), BRCA (B), CESC (C), CHOL (D), COAD (E), ESCA (F), HNSC(G), KICH (H), KIRC (I), KIRP (J), LIHC (K), LUAD (L), LUSC (M), PRAD (N), READ (O), STAD (P), THCA (Q), UCEC (R).

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 3. The disease-free survival (DFS) analysis of the expression of PDIA3 in various cancers was performed by using GEPIA database. The RFS plot of PDIA3 in BLCA (A), BRCA (B), CESC (C), CHOL (D), COAD (E), ESCA (F), HNSC(G), KICH (H), KIRC (I), KIRP (J), LIHC (K), LUAD (L), LUSC (M), PRAD (N), READ (O), STAD (P), THCA (Q), UCEC (R).

Techniques: Expressing

Fig. 4. The mRNA and the protein expression of PDIA3 in LUAD. (A) The mRNA level of PDIA3 in multiple cancers was determined by using Oncomine database. (B) The mRNA expression of PDIA3 was investigated by R software. (C) The mRNA and the protein level of PDIA3 were validated by qRT-PCR. (D, E) The protein level of PDIA3 were validated by IHC and western blotting analysis analysis respectively.

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 4. The mRNA and the protein expression of PDIA3 in LUAD. (A) The mRNA level of PDIA3 in multiple cancers was determined by using Oncomine database. (B) The mRNA expression of PDIA3 was investigated by R software. (C) The mRNA and the protein level of PDIA3 were validated by qRT-PCR. (D, E) The protein level of PDIA3 were validated by IHC and western blotting analysis analysis respectively.

Techniques: Expressing, Software, Quantitative RT-PCR, Western Blot

Fig. 5. The relationship between the expression of PDIA3 and the clinicopathological parameters were determined by UALCAN database. The relationship between PDIA3 and the patient’s age (A), gender (B), race (C), smoking habits (D), cancer stages (E), and nodal metastasis status (F) was analyzed, respectively.* P value <0.05, **P value <0.01, *** P value <0.001.

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 5. The relationship between the expression of PDIA3 and the clinicopathological parameters were determined by UALCAN database. The relationship between PDIA3 and the patient’s age (A), gender (B), race (C), smoking habits (D), cancer stages (E), and nodal metastasis status (F) was analyzed, respectively.* P value <0.05, **P value <0.01, *** P value <0.001.

Techniques: Expressing

Fig. 6. GO enrichment analysis of PDIA3 in LUAD was determined by performing Spearrman’s correlation test. (A) BP, biological process. (B) CC, cellular component. (C) MF, molecular function.

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 6. GO enrichment analysis of PDIA3 in LUAD was determined by performing Spearrman’s correlation test. (A) BP, biological process. (B) CC, cellular component. (C) MF, molecular function.

Techniques:

Fig. 7. miR-301a-5p was identified as a potential upstream miRNA of PDIA3 in LUAD. (A) The miRNA-PDIA3 regulatory network was established by Cytoscape software. (B) The expression correlation between miRNAs and PDIA3 was predicted in LUAD by using starBase database. (C) The expression of miR-301a-5p in LUAD was compared to that in adjacent normal tissues and analyzed by starBase database. (D) The prognostic value of miR-301a-5p in LUAD was assessed by Kaplan – Meier plotter. (E) qRT-PCR was used to detect PDIA3 levels in LUAD tissues (N = 18). (F) qRT-PCR was used to detect miR-301a-5p levels in LUAD tissues (N = 18). (G) Pearson analysis was used to evaluate correlation of PDIA3 and miR-301a-5p mRNA levels in LUAD tissues (N = 18).

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 7. miR-301a-5p was identified as a potential upstream miRNA of PDIA3 in LUAD. (A) The miRNA-PDIA3 regulatory network was established by Cytoscape software. (B) The expression correlation between miRNAs and PDIA3 was predicted in LUAD by using starBase database. (C) The expression of miR-301a-5p in LUAD was compared to that in adjacent normal tissues and analyzed by starBase database. (D) The prognostic value of miR-301a-5p in LUAD was assessed by Kaplan – Meier plotter. (E) qRT-PCR was used to detect PDIA3 levels in LUAD tissues (N = 18). (F) qRT-PCR was used to detect miR-301a-5p levels in LUAD tissues (N = 18). (G) Pearson analysis was used to evaluate correlation of PDIA3 and miR-301a-5p mRNA levels in LUAD tissues (N = 18).

Techniques: Software, Expressing, Quantitative RT-PCR

Fig. 8. The correlation between immune cell infiltration and PDIA3 expression in LUAD. (A) The infiltration level of various immune cells was estimated under different copy numbers of PDIA3 in LUAD. (B-G) The relationship of PDIA3 level and B cell (B), CD8+ T cell (C), CD4+ T cell (D), macrophage (E), neutrophil (F), and dendritic cell (G) infiltration level in LUAD.

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 8. The correlation between immune cell infiltration and PDIA3 expression in LUAD. (A) The infiltration level of various immune cells was estimated under different copy numbers of PDIA3 in LUAD. (B-G) The relationship of PDIA3 level and B cell (B), CD8+ T cell (C), CD4+ T cell (D), macrophage (E), neutrophil (F), and dendritic cell (G) infiltration level in LUAD.

Techniques: Expressing

Fig. 10. The model of miR-301a-5p/ PDIA3 axis during the progression of LUAD.

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 10. The model of miR-301a-5p/ PDIA3 axis during the progression of LUAD.

Techniques:

Fig. 9. The correlation of PDIA3 expression with PD- 1, PD-L1, and CTLA-4 expression in LUAD.(A) Spearman correlation of PDIA3 was based on purity and obtained by using TIMER database. (B) Spearman correlation of PDIA3 indicated the expression of PD- L1 in LUAD, and it was adjusted according to purity by using TIMER database. (C) Spearman correlation of PDIA3 elicited the expression of CTLA-4 in LUAD and was adjusted for purity by using TIMER database. (D) The expression correlation of PDIA3 with PD-1 in LUAD was determined by using GEPIA database. (E) The expression correlation of PDIA3 with PD-L1 in LUAD was determined by using GEPIA database. (F) The expression correlation of PDIA3 with CTLA-4 in LUAD was determined by using GEPIA database.

Journal: Genomics

Article Title: MicroRNA-mediated high expression of PDIA3 was correlated with poor prognosis of patients with LUAD.

doi: 10.1016/j.ygeno.2022.110417

Figure Lengend Snippet: Fig. 9. The correlation of PDIA3 expression with PD- 1, PD-L1, and CTLA-4 expression in LUAD.(A) Spearman correlation of PDIA3 was based on purity and obtained by using TIMER database. (B) Spearman correlation of PDIA3 indicated the expression of PD- L1 in LUAD, and it was adjusted according to purity by using TIMER database. (C) Spearman correlation of PDIA3 elicited the expression of CTLA-4 in LUAD and was adjusted for purity by using TIMER database. (D) The expression correlation of PDIA3 with PD-1 in LUAD was determined by using GEPIA database. (E) The expression correlation of PDIA3 with PD-L1 in LUAD was determined by using GEPIA database. (F) The expression correlation of PDIA3 with CTLA-4 in LUAD was determined by using GEPIA database.

Techniques: Expressing

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