Review

stt3a (Proteintech)

Proteintech is a verified supplier

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Proteintech stt3a

<t>STT3A</t> involved in HCC progression via promoting FCN3 N-glycosylation. ( A ) Bioinformatics analysis revealing STT3A expression in normal and HCC liver tissues. ( B - D ) qRT-PCR, WB and IHC assays were performed to assess STT3A levels in HCC tumor and adjacent non-tumor tissues. ( E - F ) The mRNA and protein levels of STT3A in normal hepatocyte and HCC cell lines were analyzed by qRT-PCR and WB. ( G ) Correlation analysis between STT3A protein expression and FCN3 protein expression in tumor tissues from HCC patients. ( H ) Co-IP assay verified STT3A-FCN3 interaction. ( I ) WB analysis of FCN3 glycosylation in Hep3B cells transfected with sh-STT3A or sh-NC. ( J - K ) The effects of sh-STT3A on the expression of APC and β-catenin in Hep3B cells were examined by qRT-PCR and WB. ( L ) ELISA showing TGF-β1 and IL-10 levels in Hep3B cell supernatants following sh-STT3A or sh-NC treatment. ( M - Q ) Wound healing, Transwell and flow cytometry assays were conducted to evaluate the effects of sh-STT3A on Hep3B cell migration, invasion and apoptosis. ( R ) The influence of sh-STT3A on the proportion of CD4⁺CD25⁺FOXP3 + Treg cells in Hep3B-PBMC co-cultures was assessed by flow cytometry. *** p < 0.001, ** p < 0.01, * p < 0.05 vs. N/ THLE-2/ sh-NC

Stt3a, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+stt3a/STT3A+Antibody/pmc12774965-70-18-21
Average 94 stars, based on 39 article reviews

stt3a - by Bioz Stars, 2026-10

94/100 stars

Images

1) Product Images from "STT3A-mediated FCN3 N-glycosylation promotes Treg cell activation to drive hepatocellular carcinoma progression via Wnt/β-catenin"

Article Title: STT3A-mediated FCN3 N-glycosylation promotes Treg cell activation to drive hepatocellular carcinoma progression via Wnt/β-catenin

Journal: Cellular Oncology (Dordrecht, Netherlands)

doi: 10.1007/s13402-025-01159-1

STT3A involved in HCC progression via promoting FCN3 N-glycosylation. ( A ) Bioinformatics analysis revealing STT3A expression in normal and HCC liver tissues. ( B - D ) qRT-PCR, WB and IHC assays were performed to assess STT3A levels in HCC tumor and adjacent non-tumor tissues. ( E - F ) The mRNA and protein levels of STT3A in normal hepatocyte and HCC cell lines were analyzed by qRT-PCR and WB. ( G ) Correlation analysis between STT3A protein expression and FCN3 protein expression in tumor tissues from HCC patients. ( H ) Co-IP assay verified STT3A-FCN3 interaction. ( I ) WB analysis of FCN3 glycosylation in Hep3B cells transfected with sh-STT3A or sh-NC. ( J - K ) The effects of sh-STT3A on the expression of APC and β-catenin in Hep3B cells were examined by qRT-PCR and WB. ( L ) ELISA showing TGF-β1 and IL-10 levels in Hep3B cell supernatants following sh-STT3A or sh-NC treatment. ( M - Q ) Wound healing, Transwell and flow cytometry assays were conducted to evaluate the effects of sh-STT3A on Hep3B cell migration, invasion and apoptosis. ( R ) The influence of sh-STT3A on the proportion of CD4⁺CD25⁺FOXP3 + Treg cells in Hep3B-PBMC co-cultures was assessed by flow cytometry. *** p < 0.001, ** p < 0.01, * p < 0.05 vs. N/ THLE-2/ sh-NC

Figure Legend Snippet: STT3A involved in HCC progression via promoting FCN3 N-glycosylation. ( A ) Bioinformatics analysis revealing STT3A expression in normal and HCC liver tissues. ( B - D ) qRT-PCR, WB and IHC assays were performed to assess STT3A levels in HCC tumor and adjacent non-tumor tissues. ( E - F ) The mRNA and protein levels of STT3A in normal hepatocyte and HCC cell lines were analyzed by qRT-PCR and WB. ( G ) Correlation analysis between STT3A protein expression and FCN3 protein expression in tumor tissues from HCC patients. ( H ) Co-IP assay verified STT3A-FCN3 interaction. ( I ) WB analysis of FCN3 glycosylation in Hep3B cells transfected with sh-STT3A or sh-NC. ( J - K ) The effects of sh-STT3A on the expression of APC and β-catenin in Hep3B cells were examined by qRT-PCR and WB. ( L ) ELISA showing TGF-β1 and IL-10 levels in Hep3B cell supernatants following sh-STT3A or sh-NC treatment. ( M - Q ) Wound healing, Transwell and flow cytometry assays were conducted to evaluate the effects of sh-STT3A on Hep3B cell migration, invasion and apoptosis. ( R ) The influence of sh-STT3A on the proportion of CD4⁺CD25⁺FOXP3 + Treg cells in Hep3B-PBMC co-cultures was assessed by flow cytometry. *** p < 0.001, ** p < 0.01, * p < 0.05 vs. N/ THLE-2/ sh-NC

Techniques Used: Glycoproteomics, Expressing, Quantitative RT-PCR, Co-Immunoprecipitation Assay, Transfection, Enzyme-linked Immunosorbent Assay, Flow Cytometry, Migration

STT3A promoted HCC development by regulating Treg cell activation in vivo. ( A ) Representative tumors of C57BL/6 mice at day 21 post-inoculation of Hepa1-6 cells with sh-STT3A or sh-NC transfection. ( B - C ) Tumor volume and body weight recorded during 21 days post Hepa1-6 cell inoculation demonstrated the effect of sh-STT3A on HCC tumor growth. ( D - F ) qRT-PCR and WB analysis of FOXP3 and CD25 in tumor tissues from HCC mice with sh-STT3A or sh-NC. ( G ) H&E-stained lung sections showing the impact of sh-STT3A on the number of metastatic nodules in HCC mice. ( H - J ) Tumor growth evaluation (images, volume, weight) in mice receiving Hepa1-6 cells with OE-NC, OE-STT3A, or OE-STT3A + DT. ( K - L ) ELISA assessing the influence of OE-STT3A and OE-STT3A + DT on TGF-β1 and IL-10 in HCC mouse tumor tissues. ( M ) Assessment of lung metastasis in HCC mice with OE-NC, OE-STT3A, or OE-STT3A + DT treatment using H&E staining. *** p < 0.001, ** p < 0.01, * p < 0.05 vs. sh-NC/ OE-NC/ OE-STT3A

Figure Legend Snippet: STT3A promoted HCC development by regulating Treg cell activation in vivo. ( A ) Representative tumors of C57BL/6 mice at day 21 post-inoculation of Hepa1-6 cells with sh-STT3A or sh-NC transfection. ( B - C ) Tumor volume and body weight recorded during 21 days post Hepa1-6 cell inoculation demonstrated the effect of sh-STT3A on HCC tumor growth. ( D - F ) qRT-PCR and WB analysis of FOXP3 and CD25 in tumor tissues from HCC mice with sh-STT3A or sh-NC. ( G ) H&E-stained lung sections showing the impact of sh-STT3A on the number of metastatic nodules in HCC mice. ( H - J ) Tumor growth evaluation (images, volume, weight) in mice receiving Hepa1-6 cells with OE-NC, OE-STT3A, or OE-STT3A + DT. ( K - L ) ELISA assessing the influence of OE-STT3A and OE-STT3A + DT on TGF-β1 and IL-10 in HCC mouse tumor tissues. ( M ) Assessment of lung metastasis in HCC mice with OE-NC, OE-STT3A, or OE-STT3A + DT treatment using H&E staining. *** p < 0.001, ** p < 0.01, * p < 0.05 vs. sh-NC/ OE-NC/ OE-STT3A

Techniques Used: Activation Assay, In Vivo, Transfection, Quantitative RT-PCR, Staining, Enzyme-linked Immunosorbent Assay

other:

Article Title: MIIP downregulation drives colorectal cancer progression through inducing peri-cancerous adipose tissue browning
Article Snippet: The primary antibodies used in this study included anti-UCP1 (23,673–1-AP, RRID: AB_2828003), anti-PGC-1α (66,369–1-Ig, RRID: AB_2828002), anti-FABP4 (12,802–1-AP, RRID: AB_2102442), anti-STT3A (12,034–1-AP, RRID: AB_2877818), and anti-STT3B (15,323–1-AP, RRID: AB_2198046), which were purchased from Proteintech Group, Inc (Rosemont, IL, US).

Article Title: Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation
Article Snippet: Western blotting was performed using a Pierce Fast Western Blot Kit (Thermo Scientific) according to the manufacturer’s instructions.

Article Title: Interferon-Inducible Guanylate-Binding Protein 5 Inhibits Replication of Multiple Viruses by Binding to the Oligosaccharyltransferase Complex and Inhibiting Glycoprotein Maturation
Article Snippet: Western blotting was performed using a Pierce Fast Western Blot Kit (Thermo Scientific) according to the manufacturer’s instructions.

Article Title: STT3-mediated aberrant N-glycosylation of CD24 inhibits paclitaxel sensitivity in triple-negative breast cancer.
Article Snippet: Paclitaxel is one of the main chemotherapic medicines against triple-negative breast cancer (TNBC) in clinic.. However, it has been perplexed by paclitaxel resistance in TNBC patients, resulting in a poor prognosis.. Abnormal protein glycosylation is closely related to the occurrence and progression of tumors and malignant phenotypes such as chemotherapy resistance.

Article Title: Signal recognition particle receptor-β (SR-β) coordinates cotranslational N-glycosylation
Article Snippet: The following primary antibodies were used: anti-ALG12 (1:1000; PA5-50316, Invitrogen), anti-FNDC3B (1:1000; B-1, sc-393997, Santa Cruz Biotechnology, Dallas, TX), anti-GP130 (1:1000; M-20, sc-656, Santa Cruz Biotechnology), anti-HaloTag (1:3000; G9281, Promega, Madison, WI), anti-HPRT (1:1000; F-4, sc-376922, Santa Cruz Biotechnology), anti-phospho-RPS6 S253/236 (1:1000; 2211, Cell Signaling Technology, Danvers, MA), anti-RPN1 (1:500; 12894-1-AP, Proteintech, Rosemont, IL), anti-RPS6 kinase (1:1000; 54D2, 2317, Cell Signaling Technology), anti-Sec61A1 (1:500; D7Q6V, 14868, Cell Signaling Technology), anti–SR-α (1:1000; PA5-28295, Invitrogen), anti–SR-β (1:500; 14636-1-AP, Proteintech), anti-SSR2 (1:500; 10278-1-AP, Proteintech), anti-STT3A (1:500; 12034-1-AP, Proteintech), anti-STT3B (1:500; 15323-1-AP, Proteintech), anti-UBE2J1 (1:800; B-6, sc-377002, Santa Cruz Biotechnology), and anti-vinculin (1:2000; E1E9V, 13901, Cell Signaling Technology).

Article Title: MIIP downregulation drives colorectal cancer progression through inducing peri-cancerous adipose tissue browning.
Article Snippet: The primary antibodies used in this study included antiUCP1 (23,673–1-AP, RRID: AB_2828003), anti-PGC-1α (66,369–1-Ig, RRID: AB_2828002), anti-FABP4 (12,802– 1-AP, RRID: AB_2102442), anti-STT3A (12,034–1-AP, RRID: AB_2877818), and anti-STT3B (15,323–1-AP, RRID: AB_2198046), which were purchased from Proteintech Group, Inc (Rosemont, IL, US).

Article Title: Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation.
Article Snippet: The following antibodies were used: anti-S2 antibody (which detects the S2 subunit of SARS-CoV-2 and SARS-CoV) was from Novus (NB100-56578); anti-FLAG antibody was from Sigma (F1804); anti-gp120 was from NIH-ARP (clone 16H3, ARP-12559); anti-RPN2 was from ABClonal (A8352); and anti-HA (51064-2-AP), anti-MYC (16286-1-AP), anti-GBP5 (13220-1-AP), anti-RPN1 (12894-1-AP), anti-DDOST(14916-1-AP), anti-STT3B (15323-1-AP), anti-STT3A (12034-1- AP), HRP-conjugated anti-α-tubulin (HRP-66031) and HRP-conjugated anti-GAPDH (HRP-60004) antibodies were all purchased from Proteintech.

Biomarker Discovery:

Article Title: Structural basis of regulated N-glycosylation at the secretory translocon.
Article Snippet: .. The following have been further validated in the indicated citations: antiCCDC134 (PMID: 39509507, 32181939), anti-PSAP (PMID: 39509507, 27383987), anti-STT3A (Proteintech) (PMID: 39509507), antiSTT3A (Abnova) (PMID:36261522), anti-LRP6 (PMID: 39509507), anti-IGF1Rbeta (PMID: 39509507), anti-GRP94 (Santa Cruz Biotechnology) (PMID: 39509507), anti-FKBP11 (PMID: 39259761) Eukaryotic cell lines Policy information about cell lines and Sex and Gender in Research Cell line source(s) RKO cells were purchased from ATCC, and Flp-In T-REx HEK293 Cell Line are from Invitrogen Authentication Parental RKO cell line came with a certificate of authentication from the vendor (ATCC) and was used without further validation. ..

Image Search Results

(A) Western blot analysis of ASNS in metastatic cells isolated from bone (B-M-1, B-M-2) and lung (L-M-1, L-M-2) lesions. Vinculin was used as loading control. The image is representative of three independent experiments. (B) Schematic representation of asparaginyl-tRNA synthetase 1 (NARS1) mechanism of action. (C) NARS1 mRNA levels in PC3 cells following NARS1 silencing. Cells were transfected with NARS1-targeting small interfering RNA (siRNA) or negative control, and mRNA levels were evaluated after 5 days of incubation in 3D cultures (3D-C) by quantitative RT-PCR, using scramble-transfected cells as reference. (D) Relative cell number of PC3 cells silenced for NARS1 and cultured under standard 2D conditions for 5 days in the presence or absence of Asn (0.1 mM). One-way ANOVA with Sidak’s correction. (E-G) Number of putative N-glycosylation sites in proteins encoded by genes up- or down-regulated in metastatic cells derived from bone (E), lung (F), and liver (G) relative to primary tumor (PT). RNA-seq analysis was conducted as described in . Values are expressed relative to total protein number. (H-I) Fractional enrichment of UDP-GlcNAc isotopologues. PC3 cells were grown in 2D or 3D-C for 5 days and subsequently incubated in a medium containing U- 13 C-glucose for 24h. Labeling enrichment was evaluated by LC-MS analysis, and isotopologue abundance is reported as relative to total UDP-GlcNAc amount. Welch’s t test. (J) Labeling (m+5) enrichment of penotose phosphates from U- 13 C-glucose in PC3 cells growing in 2D or 3D-C for 5 days and subsequently incubated in a medium containing U- 13 C-glucose for 24h. Labeling enrichment was evaluated by LC-MS analysis. (K, L, P) Western blot analysis of GFPT1 (K), STT3a (L), and CD44 (P) expression in PC3 cells silenced for GFPT1, STT3a/b, and CD44 respectively after 48h of gene silencing. Vinculin was used as a loading control. The image is representative of three independent experiments. (M) Concanavalin A lectin binding assay performed on lysates from PC3 cells silenced or not for GFPT1 or STT3a/b and cultured in 3D-C for 5 days. Immunoblot for vinculin was used to confirm equal protein loading across samples. The image is representative of three independent experiments. (N-O) Adhesion of PC3 3D-C to collagen type I (L) and hyaluronic acid (M). Cells were cultured with Asn (0,1 mM) for 5 days and allowed to adhere for 15 min to plates coated with matrix components as reported. Adherent cells were quantified and data are shown relative to untreated cells. Welch’s t-test.

Journal: bioRxiv

Article Title: ASPARAGINE-RICH METASTATIC NICHES DRIVE PROSTATE CANCER ORGANOTROPISM BY ENABLING TRANSLATIONAL REWIRING TOWARD N-GLYCOSYLATED PROTEINS

doi: 10.64898/2026.02.27.708521

Figure Lengend Snippet: (A) Western blot analysis of ASNS in metastatic cells isolated from bone (B-M-1, B-M-2) and lung (L-M-1, L-M-2) lesions. Vinculin was used as loading control. The image is representative of three independent experiments. (B) Schematic representation of asparaginyl-tRNA synthetase 1 (NARS1) mechanism of action. (C) NARS1 mRNA levels in PC3 cells following NARS1 silencing. Cells were transfected with NARS1-targeting small interfering RNA (siRNA) or negative control, and mRNA levels were evaluated after 5 days of incubation in 3D cultures (3D-C) by quantitative RT-PCR, using scramble-transfected cells as reference. (D) Relative cell number of PC3 cells silenced for NARS1 and cultured under standard 2D conditions for 5 days in the presence or absence of Asn (0.1 mM). One-way ANOVA with Sidak’s correction. (E-G) Number of putative N-glycosylation sites in proteins encoded by genes up- or down-regulated in metastatic cells derived from bone (E), lung (F), and liver (G) relative to primary tumor (PT). RNA-seq analysis was conducted as described in . Values are expressed relative to total protein number. (H-I) Fractional enrichment of UDP-GlcNAc isotopologues. PC3 cells were grown in 2D or 3D-C for 5 days and subsequently incubated in a medium containing U- 13 C-glucose for 24h. Labeling enrichment was evaluated by LC-MS analysis, and isotopologue abundance is reported as relative to total UDP-GlcNAc amount. Welch’s t test. (J) Labeling (m+5) enrichment of penotose phosphates from U- 13 C-glucose in PC3 cells growing in 2D or 3D-C for 5 days and subsequently incubated in a medium containing U- 13 C-glucose for 24h. Labeling enrichment was evaluated by LC-MS analysis. (K, L, P) Western blot analysis of GFPT1 (K), STT3a (L), and CD44 (P) expression in PC3 cells silenced for GFPT1, STT3a/b, and CD44 respectively after 48h of gene silencing. Vinculin was used as a loading control. The image is representative of three independent experiments. (M) Concanavalin A lectin binding assay performed on lysates from PC3 cells silenced or not for GFPT1 or STT3a/b and cultured in 3D-C for 5 days. Immunoblot for vinculin was used to confirm equal protein loading across samples. The image is representative of three independent experiments. (N-O) Adhesion of PC3 3D-C to collagen type I (L) and hyaluronic acid (M). Cells were cultured with Asn (0,1 mM) for 5 days and allowed to adhere for 15 min to plates coated with matrix components as reported. Adherent cells were quantified and data are shown relative to untreated cells. Welch’s t-test.

Article Snippet: Membranes were incubated for 1h at room temperature in blocking buffer (5% non-fat dry milk (SantaCruz Biotechnology #sc-2325) in PBS-Tween 0.1%), and then incubated at 4°C over-night with primary antibodies against either ATF-4 (Cell Signaling Technology #11815), ASNS (Cell Signaling Technology #92479S), Phospho-mTOR (Ser2448) (Cell Signaling Technology #5536S), mTOR (Cell Signaling Technology #2983), Phospho-S6K1(Thr389) (Cell Signalig Technology #9205), S6K1 (Cell Signaling Technology #9202), CD44 (Cell Signaling Technology #3570), GFPT1 (ABClonal #A20873), STT3a (Santa Cruz Biotechology #sc-390227), Vinculin (Santa Cruz Biotechology #sc-59803), β-Actin (Santa Cruz Biotechology #sc-47778).

Techniques: Western Blot, Isolation, Control, Transfection, Small Interfering RNA, Negative Control, Incubation, Quantitative RT-PCR, Cell Culture, Glycoproteomics, Derivative Assay, RNA Sequencing, Labeling, Liquid Chromatography with Mass Spectroscopy, Expressing, Binding Assay

(A-C) Number of putative N-glycosylation sites in proteins encoded by genes upregulated in bone-(A), lung-(B), and liver-(C) derived metastatic cells relative to the primary tumor (PT). RNA-seq analysis was conducted as described in . Values are expressed as relative to proteins number. Welch’s t-test. (D) Number of putative N-glycosylation sites in proteins encoded by genes upregulated in bone-, lung-, and liver-derived metastatic cells. One-way ANOVA with Tukey’s correction. (E) Relative incorporation of U- 13 C-glucose carbons in UDP-N-acetyl-glucosamine. PC3 cells were grown in 3D-C for 5 days and subsequently incubated in a medium containing U- 13 C-glucose for 24h. Metabolite abundance and labeling enrichment were evaluated by LC-MS analysis. (F) mRNA levels of oligosaccharyltransferase (OST) in 2D coltures and 3D-C. mRNA expression levels analyzed by quantitative RT-PCR using 2D condition as comparator. Student’s t test. (G) Concanavalin A lectin binding assay performed on lysates from PC3 cells cultured in 2D conditions or 3D-C, with or without Asn supplementation (0.1 mM). Immunoblot for actin was used to confirm equal protein loading across samples. The image is representative of three independent experiments. (H) Concanavalin A lectin binding assay performed on lysates from 3D-C cultured with or without Asn (0.1 mM) in the presence or absence of L-asparaginase (ASNase, 0.25 U/ml). Immunoblot for vinculin was used to confirm equal protein loading across samples. The image is representative of three independent experiments. (I) Total spheroid area of PC3 3D-C grown with or without Asn (0.1 mM) in the presence or absence of Tunicamycin (5ng/µl). One-way ANOVA with Dunnett’s correction. (J) Total spheroid area of Glutamine-fructose-6-phosphate transaminase 1 (GFPT1)-silenced PC3 cells grown in 3D-C with or without Asn (0.1 mM). One-way ANOVA with Dunnett’s correction. (K) Total spheroid area of 3D-C PC3 cells silenced for the OST catalytic subunits STT3A and STT3B with or without Asn (0.1 mM). One-way ANOVA with Dunnett’s correction. (L) Concanavalin A lectin binding assay performed on lysates from liver-derived (Liv-M), bone-derived (B-M-1, B-M-2) and lung-derived (L-M-1, L-M-2) metastatic cells (obtained after intracardiac or caudal artery injection, respectively) grown in 3D-C cultures. Immunoblot for vinculin was used to confirm equal protein loading across samples. The image is representative of three independent experiments. (M-P) Total spheroid area of bone-derived (M, N), and lung-derived (O, P) metastatic cells grown in 3D-C cultures with or without Asn (0.1 mM) in the presence or absence of Tunicamycin (5ng/µl). Two-way ANOVA with Tukey’s correction. ns, not significant; *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001. Data represent mean ± s.e.m. from at least three independent experiments.

Journal: bioRxiv

Article Title: ASPARAGINE-RICH METASTATIC NICHES DRIVE PROSTATE CANCER ORGANOTROPISM BY ENABLING TRANSLATIONAL REWIRING TOWARD N-GLYCOSYLATED PROTEINS

doi: 10.64898/2026.02.27.708521

Figure Lengend Snippet: (A-C) Number of putative N-glycosylation sites in proteins encoded by genes upregulated in bone-(A), lung-(B), and liver-(C) derived metastatic cells relative to the primary tumor (PT). RNA-seq analysis was conducted as described in . Values are expressed as relative to proteins number. Welch’s t-test. (D) Number of putative N-glycosylation sites in proteins encoded by genes upregulated in bone-, lung-, and liver-derived metastatic cells. One-way ANOVA with Tukey’s correction. (E) Relative incorporation of U- 13 C-glucose carbons in UDP-N-acetyl-glucosamine. PC3 cells were grown in 3D-C for 5 days and subsequently incubated in a medium containing U- 13 C-glucose for 24h. Metabolite abundance and labeling enrichment were evaluated by LC-MS analysis. (F) mRNA levels of oligosaccharyltransferase (OST) in 2D coltures and 3D-C. mRNA expression levels analyzed by quantitative RT-PCR using 2D condition as comparator. Student’s t test. (G) Concanavalin A lectin binding assay performed on lysates from PC3 cells cultured in 2D conditions or 3D-C, with or without Asn supplementation (0.1 mM). Immunoblot for actin was used to confirm equal protein loading across samples. The image is representative of three independent experiments. (H) Concanavalin A lectin binding assay performed on lysates from 3D-C cultured with or without Asn (0.1 mM) in the presence or absence of L-asparaginase (ASNase, 0.25 U/ml). Immunoblot for vinculin was used to confirm equal protein loading across samples. The image is representative of three independent experiments. (I) Total spheroid area of PC3 3D-C grown with or without Asn (0.1 mM) in the presence or absence of Tunicamycin (5ng/µl). One-way ANOVA with Dunnett’s correction. (J) Total spheroid area of Glutamine-fructose-6-phosphate transaminase 1 (GFPT1)-silenced PC3 cells grown in 3D-C with or without Asn (0.1 mM). One-way ANOVA with Dunnett’s correction. (K) Total spheroid area of 3D-C PC3 cells silenced for the OST catalytic subunits STT3A and STT3B with or without Asn (0.1 mM). One-way ANOVA with Dunnett’s correction. (L) Concanavalin A lectin binding assay performed on lysates from liver-derived (Liv-M), bone-derived (B-M-1, B-M-2) and lung-derived (L-M-1, L-M-2) metastatic cells (obtained after intracardiac or caudal artery injection, respectively) grown in 3D-C cultures. Immunoblot for vinculin was used to confirm equal protein loading across samples. The image is representative of three independent experiments. (M-P) Total spheroid area of bone-derived (M, N), and lung-derived (O, P) metastatic cells grown in 3D-C cultures with or without Asn (0.1 mM) in the presence or absence of Tunicamycin (5ng/µl). Two-way ANOVA with Tukey’s correction. ns, not significant; *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001. Data represent mean ± s.e.m. from at least three independent experiments.

Techniques: Glycoproteomics, Derivative Assay, RNA Sequencing, Incubation, Labeling, Liquid Chromatography with Mass Spectroscopy, Expressing, Quantitative RT-PCR, Binding Assay, Cell Culture, Western Blot, Injection

Journal: Cellular Oncology (Dordrecht, Netherlands)

Article Title: STT3A-mediated FCN3 N-glycosylation promotes Treg cell activation to drive hepatocellular carcinoma progression via Wnt/β-catenin

doi: 10.1007/s13402-025-01159-1

Figure Lengend Snippet: STT3A involved in HCC progression via promoting FCN3 N-glycosylation. ( A ) Bioinformatics analysis revealing STT3A expression in normal and HCC liver tissues. ( B - D ) qRT-PCR, WB and IHC assays were performed to assess STT3A levels in HCC tumor and adjacent non-tumor tissues. ( E - F ) The mRNA and protein levels of STT3A in normal hepatocyte and HCC cell lines were analyzed by qRT-PCR and WB. ( G ) Correlation analysis between STT3A protein expression and FCN3 protein expression in tumor tissues from HCC patients. ( H ) Co-IP assay verified STT3A-FCN3 interaction. ( I ) WB analysis of FCN3 glycosylation in Hep3B cells transfected with sh-STT3A or sh-NC. ( J - K ) The effects of sh-STT3A on the expression of APC and β-catenin in Hep3B cells were examined by qRT-PCR and WB. ( L ) ELISA showing TGF-β1 and IL-10 levels in Hep3B cell supernatants following sh-STT3A or sh-NC treatment. ( M - Q ) Wound healing, Transwell and flow cytometry assays were conducted to evaluate the effects of sh-STT3A on Hep3B cell migration, invasion and apoptosis. ( R ) The influence of sh-STT3A on the proportion of CD4⁺CD25⁺FOXP3 + Treg cells in Hep3B-PBMC co-cultures was assessed by flow cytometry. *** p < 0.001, ** p < 0.01, * p < 0.05 vs. N/ THLE-2/ sh-NC

Article Snippet: After peroxidase blocking, sections were incubated with primary antibodies against FCN3 (#11867-1-AP, 1:200; Proteintech, Wuhan, Hubei, China) or STT3A (#12034-1-AP, 1:200; Proteintech) at 37 °C for 30 min.

Techniques: Glycoproteomics, Expressing, Quantitative RT-PCR, Co-Immunoprecipitation Assay, Transfection, Enzyme-linked Immunosorbent Assay, Flow Cytometry, Migration

Journal: Cellular Oncology (Dordrecht, Netherlands)

Article Title: STT3A-mediated FCN3 N-glycosylation promotes Treg cell activation to drive hepatocellular carcinoma progression via Wnt/β-catenin

doi: 10.1007/s13402-025-01159-1

Figure Lengend Snippet: STT3A promoted HCC development by regulating Treg cell activation in vivo. ( A ) Representative tumors of C57BL/6 mice at day 21 post-inoculation of Hepa1-6 cells with sh-STT3A or sh-NC transfection. ( B - C ) Tumor volume and body weight recorded during 21 days post Hepa1-6 cell inoculation demonstrated the effect of sh-STT3A on HCC tumor growth. ( D - F ) qRT-PCR and WB analysis of FOXP3 and CD25 in tumor tissues from HCC mice with sh-STT3A or sh-NC. ( G ) H&E-stained lung sections showing the impact of sh-STT3A on the number of metastatic nodules in HCC mice. ( H - J ) Tumor growth evaluation (images, volume, weight) in mice receiving Hepa1-6 cells with OE-NC, OE-STT3A, or OE-STT3A + DT. ( K - L ) ELISA assessing the influence of OE-STT3A and OE-STT3A + DT on TGF-β1 and IL-10 in HCC mouse tumor tissues. ( M ) Assessment of lung metastasis in HCC mice with OE-NC, OE-STT3A, or OE-STT3A + DT treatment using H&E staining. *** p < 0.001, ** p < 0.01, * p < 0.05 vs. sh-NC/ OE-NC/ OE-STT3A

Techniques: Activation Assay, In Vivo, Transfection, Quantitative RT-PCR, Staining, Enzyme-linked Immunosorbent Assay

Review

stt3a (Proteintech)

Structured Review

Images

1) Product Images from "STT3A-mediated FCN3 N-glycosylation promotes Treg cell activation to drive hepatocellular carcinoma progression via Wnt/β-catenin"

Related Articles

other:

Biomarker Discovery:

Similar Products

Image Search Results