Journal: Frontiers in Physiology

Article Title: Dual roles of syndecan-4 in regulating chicken fibrosis in vitro

doi: 10.3389/fphys.2026.1782914

Figure Lengend Snippet: Overexpression of SDC4 in SL-29 chicken fibroblast cells. (A) Chicken embryonic SL-29 fibroblasts were transiently transfected with HA-tagged SDC4, fixed with 4% PFA, stained with mouse α-HA (left) and rabbit α-SDC4 (middle) followed by goat anti-mouse Alexa Fluor 488 and goat anti-rabbit Alexa Fluor 546 before fluorescence microscopy analyses. NucBlue was used to stain nuclei (blue). The inserts represent a higher magnification of the framed areas. Arrows indicate focal adhesions. Scalebar 50 µm. (B) SL-29 cells were transiently transfected with SDC4 (n = 6), or HA-SDC4 (n = 3) plasmids. Lipofectamine only was used as control (Ctrl). Bars show the relative mRNA gene expression in transfected cells compared with the mean average of Ctrl cells (n = 6). The bars are presented as ± SEM. Asterisks denote significant differences between Ctrl and transfected cells, statistics assessed using unpaired t-test with Welch correction (ns > 0.05; *p ≤ 0.05; **p ≤ 0.01). (C) A representative western blot showing the level of SDC4 after transient transfection of the chicken fibroblasts. Cells treated as in B were subjected to western blotting using antibodies against HA tag adding a molecular size increase around nine amino acid (top) or only the cytoplasmic part of SDC4 (middle panel). The lowermost panel shows total protein. (D) Quantification of the levels of the 15 and 20 kDa SDC4 fragments, normalized to total protein level. The bars represent n = 8 in one technical replicate for SDC4 and Ctrl, and n = 4 in one technical replicate for HA-SDC4. The bars are presented as ± SEM. Asterisks denote significant differences between Ctrl and transfected cells, statistics assessed using unpaired Mann-Whitney non-parametric t-test (ns > 0.05; **p ≤ 0.01; ***p ≤ 0.001).

Article Snippet: SDC4 , Gg03370419_m1.

Techniques: Over Expression, Transfection, Staining, Fluorescence, Microscopy, Control, Gene Expression, Western Blot, MANN-WHITNEY

Journal: Frontiers in Physiology

Article Title: Dual roles of syndecan-4 in regulating chicken fibrosis in vitro

doi: 10.3389/fphys.2026.1782914

Figure Lengend Snippet: Effect of SDC4 overexpression on fibrosis markers in chicken fibroblasts SL-29. Protein expression of (A) pro-collagen I beta chain (250 kDa) and alpha chain (100 kDa), (B) pro-collagen III (250 kDa) and collagen I (100 kDa), (C) MMP-2 and (D) MMP-9 in SDC4 transfected SL-29 cells. GAPDH was used as a reference protein. The bars represent n = 3 in one technical replicate. Gene expression (n = 6 in technical triplicates) of (E) COL1A1, COL3A1, MMP2, MMP9, (F) TGFβ and IL1β in SDC4 transfected SL-29 cells. The bars are presented as ± SEM. Asterisks denote significant differences between Ctrl (lipofectamine only) and transfected cells, statistics assessed using unpaired t-test with Welch correction and Mann-Whitney U (ns > 0.05; *p ≤ 0.05; **p ≤ 0.001).

Article Snippet: SDC4 , Gg03370419_m1.

Techniques: Over Expression, Expressing, Transfection, Gene Expression, MANN-WHITNEY

Journal: Frontiers in Physiology

Article Title: Dual roles of syndecan-4 in regulating chicken fibrosis in vitro

doi: 10.3389/fphys.2026.1782914

Figure Lengend Snippet: Effect of SDC4 overexpression on signaling pathways chicken fibroblasts. Protein expression analysis following SDC4 overexpression in SL-29 chicken fibroblasts. Detected proteins include (A) phosphorylated p38 at Thr186/Tyr182 and total p38, (B) phosphorylated Akt at Ser473 (pSer473- Akt) and total Akt, (C) phosphorylated ribosomal protein S6 at Ser240/244 (pSer240/244-S6) and total ribosomal protein S6, and (D) non-phosphorylated (active) β-catenin at Ser33/37 and Thr41 and total β-catenin. The ratio of phosphorylated to total or active to total protein was calculated for each protein, illustrating the impact of SDC4 overexpression. As a control (ctrl) was used treatment with lipofectamine only. GAPDH was used as a reference protein. The bars are presented as ± SEM from n = 3-6 in one technical replicate. Asterisks denote significant differences between Ctrl and transfected cells, statistics assessed using either unpaired t-test with Welch correction or Mann-Whitney U test (ns > 0.05; *p ≤ 0.05; **p ≤ 0.01).

Article Snippet: SDC4 , Gg03370419_m1.

Techniques: Over Expression, Protein-Protein interactions, Expressing, Control, Transfection, MANN-WHITNEY

Journal: Frontiers in Physiology

Article Title: Dual roles of syndecan-4 in regulating chicken fibrosis in vitro

doi: 10.3389/fphys.2026.1782914

Figure Lengend Snippet: Effect of blocking peptides on SDC4 shedding. (A) Alignment of human and chicken SDC4 protein sequences, highlighting amino acid percentage identity (dark blue >80%, lighter shades of blue are >60% and >40%, white <40%). Five overlapping blocking peptides (BP1-5) representing the SDC4 ectodomain were designed and are marked by different colors below the chicken SDC4 sequence. Red arrows indicate MMP cleavage sites in human SDC4 . Alignment created by Jalview 2.11.4.0. (B) Effect of BP1-5 on SDC4 shedding in SDC4-overexpressing chicken fibroblasts (N = 4 in one technical replicate). Total protein is used as a loading control. The bars on the right are presented as ± SEM. SDC4-overexpressing fibroblasts treated with the solvent of BP serve as the control (Ctrl, stippled line). Asterisks denote significant differences between Ctrl and transfected cells, statistics assessed using either unpaired t-test with Welch correction or Mann-Whitney U test (*p ≤ 0.05; **p ≤ 0.01).

Article Snippet: SDC4 , Gg03370419_m1.

Techniques: Blocking Assay, Sequencing, Control, Solvent, Transfection, MANN-WHITNEY

Journal: Frontiers in Physiology

Article Title: Dual roles of syndecan-4 in regulating chicken fibrosis in vitro

doi: 10.3389/fphys.2026.1782914

Figure Lengend Snippet: Effect of blocking peptides on the gene expression of the various SDCs. Effect of BP1-5 on the levels of SDC1-4 expression in SDC4 transfected chicken fibroblasts SL-29 showing no significant differences compared to control (Ctrl). All results were compared to the appropriate solvent for each blocking peptide. Gene expression was measured in three biological replicates, each performed in technical triplicates, and statistical significance was calculated using one-way ANOVA with Welch and Brown-Forsythe corrections. The bars are presented as ± SEM.

Article Snippet: SDC4 , Gg03370419_m1.

Techniques: Blocking Assay, Gene Expression, Expressing, Transfection, Control, Solvent

Journal: Frontiers in Physiology

Article Title: Dual roles of syndecan-4 in regulating chicken fibrosis in vitro

doi: 10.3389/fphys.2026.1782914

Figure Lengend Snippet: Effect of blocking peptides on the gene expression of fibrosis markers. Effect of BP1-5 on TGFB1, COL1A1, COL3A1, MMP9, MMP2, IL1B, ACTA2, DCN gene expression levels in SDC4 transfected chicken fibroblasts SL-29. All results were compared to the appropriate solvent for each blocking peptide. Gene expression was measured in three biological replicates, each performed in technical triplicates, and statistical significance was calculated using one-way ANOVA with Welch and Brown-Forsythe corrections. The bars are presented as ± SEM.

Article Snippet: SDC4 , Gg03370419_m1.

Techniques: Blocking Assay, Gene Expression, Transfection, Solvent

Journal: Frontiers in Physiology

Article Title: Dual roles of syndecan-4 in regulating chicken fibrosis in vitro

doi: 10.3389/fphys.2026.1782914

Figure Lengend Snippet: Effect of TGF-β1 on different gene and protein expression levels. Chicken fibroblasts were treated with TGF-β1 for 24 h. The gene expression levels were assessed for (A) syndecans (SDC1-4) and various fibrotic markers, including (B) COL1A1, (C) COL3A1, (D) MMP2, and (E) MMP9. Additionally, cytokines such as (F) TGFB1 and (G) IL1B were measured, and the expression of (H) ACTA2, a myofibroblast marker, and (I) DCN, a small leucine-rich proteoglycan. Results are expressed as fold change relative to the control (Ctrl; SL-29 cells treated with the solvent of TGF-β1). Gene expression (n = 7, in technical triplicates) was calculated by an unpaired t-test with Welch’s correction. ns > 0.05; *p ≤ 0.05; **p ≤ 0.01. The bars are presented as ± SEM. (J) Immunoblotting analysis of the 20 kDa SDC4 fragment following 24-h treatment with TGF-β1, compared to control (Ctrl) conditions. Quantification (N = 3 in one technical replicate) is presented as the mean, normalized to total protein, and expressed as a percentage relative to the control.

Article Snippet: SDC4 , Gg03370419_m1.

Techniques: Expressing, Gene Expression, Marker, Control, Solvent, Western Blot

Journal: Biochimica et biophysica acta

Article Title: Syndecan-4 ectodomain evokes mobilization of podocyte TRPC6 channels and their associated pathways: An essential role for integrin signaling.

doi: 10.1016/j.bbamcr.2015.07.011

Figure Lengend Snippet: Fig. 1. Sdc4 modulates podocyte TRPC6 channels. (a) Knockdown of endogenous Sdc4 using siRNA reduces steady-state surface expression of TRPC6 in immortalized mouse podocytes. Blots on the left are results of representative cell-surface biotinylation assay. Note substantial reduction of surface TRPC6, and total Sdc4 in cells transfected with siRNA targeting Sdc4 com- pared to cells transfected with non-targeting siRNA. Bar graphs to the right show densitometric analyses of three repetitions of this experiment. In this and subsequent figures, bars rep- resent mean ± standard deviation except as noted below. Ordinates represent fold changes in signal compared to control.(b) Overexpression of Sdc4 increases steady-state surface expression of TRPC6. Representative cell-surface biotinylation assay and densitometric analysis is shown below the blot. (c) Exposing podocytes to recombinant Sdc4 ectodomain (20 ng/ml) for 24 h caused a marked increase in steady-state surface expression of TRPC6. (d) Representative whole-cell recordings from podocytes showing cationic currents evoked by 100 μM OAG and blockade of these currents by 50 μM La3+. Traces shown are of cationic currents recorded during application of voltage ramps (−80 mV to +80 mV over 2.5 s). Note that cationic current in the presence of OAG is larger in the Sdc4-treated cell. (e) Summary of the fold increase in current at +80 mV evoked by OAG over baseline in control cells and cells exposed to Sdc4 ectodomain for 24 h. This bar graph plots mean ± s.e.m. from 10 cells in each group. Asterisk indicates P b 0.05 by Student's unpaired t-test.

Article Snippet: An expression vector encoding full-length untagged mouse Sdc4 was purchased from Origene Inc. (Rockville,MD, USA), andwas transfected into podocytes using Lipofectamine 3000TM (Life Technologies, Grand Island, NY, USA) according to the manufacturer's instructions.

Techniques: Knockdown, Expressing, Cell Surface Biotinylation Assay, Transfection, Standard Deviation, Control, Over Expression, Recombinant

Journal: Biochimica et biophysica acta

Article Title: Syndecan-4 ectodomain evokes mobilization of podocyte TRPC6 channels and their associated pathways: An essential role for integrin signaling.

doi: 10.1016/j.bbamcr.2015.07.011

Figure Lengend Snippet: Fig. 2. Sdc4 interacts with β3-integrin in podocytes. (a) Representative experiment showing that β3-integrin can be detected in the material precipitated by an antibody against Sdc4, but not by a control IgG. (b) Confocal immunofluorescence showing co-localization of Sdc4 and β3-integrin in immortalized podocytes. These cells were not permeabilized before exposure to primary antibodies. (c) Representative immunoblot showing that 24 h exposure to Sdc4 ectodomain increases total expression of β3-integrin in podocytes (left) and densitometric analysis of three repetitions of this experiment (right). (d) In contrast to β3-integrin, TRPC6 channels are not detected in the material precipitated by an antibody against Sdc4.

Article Snippet: An expression vector encoding full-length untagged mouse Sdc4 was purchased from Origene Inc. (Rockville,MD, USA), andwas transfected into podocytes using Lipofectamine 3000TM (Life Technologies, Grand Island, NY, USA) according to the manufacturer's instructions.

Techniques: Control, Western Blot, Expressing

Journal: Biochimica et biophysica acta

Article Title: Syndecan-4 ectodomain evokes mobilization of podocyte TRPC6 channels and their associated pathways: An essential role for integrin signaling.

doi: 10.1016/j.bbamcr.2015.07.011

Figure Lengend Snippet: Fig. 3. Sdc4 ectodomain affects ROS generation, small GTPases and NFATc1 in podocytes. (a) Increased ROS generation detected in the bulk cytosol evoked by 24 h exposure to Sdc4 ectodomain. Treatment with Sdc4 ectodomain for as little as 1 h also caused a reduction in RhoA activation (b) and an increase in Rac1 activation (c) assessed using ELISA assays that detect that GTP-bound forms of these enzymes. (d) Sdc4 ectodomain treatment caused an increase in the amount of NFATc1 detected by immunoblot in nuclear extracts prepared from podocytes (left) but did not cause change in NFATc1 detected in total cellular lysates (right). All of these assays were carried out in triplicate.

Article Snippet: An expression vector encoding full-length untagged mouse Sdc4 was purchased from Origene Inc. (Rockville,MD, USA), andwas transfected into podocytes using Lipofectamine 3000TM (Life Technologies, Grand Island, NY, USA) according to the manufacturer's instructions.

Techniques: Activation Assay, Enzyme-linked Immunosorbent Assay, Western Blot

Journal: Biochimica et biophysica acta

Article Title: Syndecan-4 ectodomain evokes mobilization of podocyte TRPC6 channels and their associated pathways: An essential role for integrin signaling.

doi: 10.1016/j.bbamcr.2015.07.011

Figure Lengend Snippet: Fig. 4. Role of integrins on surface expression of TRPC6 channels evoked by Sdc4 ectodomain. Effects of Sdc4 ectodomain on steady-state surface expression of podocyte TRPC6 (a) and total expression of β3-integrin (b) are blocked by treatment with 1 μM cilengitide (CGT), an inhibitor of outside-in signaling through integrins that contain αv subunits, such as αvβ3-integrin.

Article Snippet: An expression vector encoding full-length untagged mouse Sdc4 was purchased from Origene Inc. (Rockville,MD, USA), andwas transfected into podocytes using Lipofectamine 3000TM (Life Technologies, Grand Island, NY, USA) according to the manufacturer's instructions.

Techniques: Expressing

Journal: Biochimica et biophysica acta

Article Title: Syndecan-4 ectodomain evokes mobilization of podocyte TRPC6 channels and their associated pathways: An essential role for integrin signaling.

doi: 10.1016/j.bbamcr.2015.07.011

Figure Lengend Snippet: Fig. 5. Role of integrins in Sdc4 ectodomain signaling in podocytes. (a) Effects of 1 μM cilengitide (CGT) on bulk cytosolic ROS generation. (b) Effects of cilengitide on inhibition of RhoA by Sdc4. (c) Effects of cilengitide on activation of Rac1 by Sdc4. (d) Effects of cilengitide on NFATc1 activation evoked by Sdc4.

Article Snippet: An expression vector encoding full-length untagged mouse Sdc4 was purchased from Origene Inc. (Rockville,MD, USA), andwas transfected into podocytes using Lipofectamine 3000TM (Life Technologies, Grand Island, NY, USA) according to the manufacturer's instructions.

Techniques: Inhibition, Activation Assay

Journal: Biochimica et biophysica acta

Article Title: Syndecan-4 ectodomain evokes mobilization of podocyte TRPC6 channels and their associated pathways: An essential role for integrin signaling.

doi: 10.1016/j.bbamcr.2015.07.011

Figure Lengend Snippet: Fig. 6. Signaling pathways in the mobilization of TRPC6 channels evoked by Sdc4. (a) Effects of Sdc4 on steady-state surface expression of TRPC6 are blocked by TEMPOL, a membrane permeable ROS quencher and superoxide dismutase mimetic agent. Effects of Sdc4 on the trafficking of TRPC6 persist in the presence of 20 μM cyclosporine A, an inhibitor of calcineurin (b) or the NFATc1 inhibitor 11R-VIVIT (10 μM) (c). (d) The effects of Sdc4 ectodomain on surface expression of TRPC6 were blocked by 50 μM NS-23766, an inhibitor of Rac1-mediated signaling. (e) Application of 1 μM membrane-permeable C3 transferase (C3T), an inhibitor of Rho enzymes, caused an increase in steady state surface expression of TRPC6 but did not exert inhibitory or additive effects with Sdc4 ectodomain.

Article Snippet: An expression vector encoding full-length untagged mouse Sdc4 was purchased from Origene Inc. (Rockville,MD, USA), andwas transfected into podocytes using Lipofectamine 3000TM (Life Technologies, Grand Island, NY, USA) according to the manufacturer's instructions.

Techniques: Protein-Protein interactions, Expressing, Membrane

Journal: Biochimica et biophysica acta

Article Title: Syndecan-4 ectodomain evokes mobilization of podocyte TRPC6 channels and their associated pathways: An essential role for integrin signaling.

doi: 10.1016/j.bbamcr.2015.07.011

Figure Lengend Snippet: Fig. 7. Shedding of the endogenous Sdc4 ectodomain from podocytes is a regulated process. (a) Exposing podocytes to TNF (10 ng/ml) for 24 h causes an increase in the amount of Sdc4 ectodomain that can be detected in the surrounding medium (blot labeled supernatants) but does not affect the amount of Sdc4 that can be detected in the podocytes themselves. Actin expression in podocytes shows that comparable amounts of cells were present in each dish. (b) A similar effect is evoked by exposing cultured podocytes to the serum of a patient with recurrent form of FSGS and taken while he was in relapse (REL). Serum from the same patient sampled while he was in remission (REM) does not affect Sdc4 ectodomain shedding. (c) Sera from two other patients with relapsed recurrent FSGS also evoked Sdc4 shedding. (d) Exposing podocytes to recombinant ADAM17, a metalloproteinase that can cleave Sdc4, also caused Sdc4 shedding from cultured podocytes. Somewhat less Sdc4 ectodomain was shed from podocytes overexpressing the Sdc4 core protein.

Article Snippet: An expression vector encoding full-length untagged mouse Sdc4 was purchased from Origene Inc. (Rockville,MD, USA), andwas transfected into podocytes using Lipofectamine 3000TM (Life Technologies, Grand Island, NY, USA) according to the manufacturer's instructions.

Techniques: Labeling, Expressing, Cell Culture, Recombinant

Journal: Biomatter

Article Title: A novel device to stretch multiple tissue samples with variable patterns: Application for mRNA regulation in tissue-engineered constructs

doi: 10.4161/biom.24650

Figure Lengend Snippet: Figure 4. Relative mRNA expression for syndecan-4, β1 integrin and β3 integrin at 25%, 50% and 75% variability, normalized to the 0% variability condition. Syndecan-4 mRNA levels are statistically significant (p < 0.001), while β1 integrin and β3 integrin do not show a significant difference (p = 0.075 and p = 0.260 respectively).

Article Snippet: ABI TaqMan gene expression assays for rat collagen 1α (Rn00801649-gl), elastin (Rn01499782-m1), lysyl oxidase (Rn00566984-m1), α-smooth muscle actin (Mn01546133-m1), Vegf (Rn01511605-m1), syndecan-4 (Rn00561900-m1), β1 integrin (Mn01253227-m1) and β3 integrin (Rn00596601-m1) were used as target probes.

Techniques: Expressing

Journal: Journal of Molecular Endocrinology

Article Title: Syndecans modulate ghrelin receptor signaling

doi: 10.1530/JME-24-0070

Figure Lengend Snippet: Syndecans (SDCs) enhance ghrelin-stimulated growth hormone secretagogue receptor (GHSR) signaling. (A) Time course of aequorin luminescence after ghrelin treatment in cells expressing GHSR with control or SDC1 expression plasmids at 1:20 ratio. (B) Comparison of peak iCa 2+ responses derived from curve-fitting data from A (* P < 0.05, GHSR alone versus SDC1 co-transfection). (C) Dose–response curves of intracellular ghrelin-stimulated iCa 2+ expressed as % Emax of 1:0 ratio: effect of different GHSR:SDC1 transfection ratios (* P < 0.05, *** P < 0.0005, Emax for GHSR:SDC co-expression versus GHSR alone (GHSR:SDC, 1:0) tested by ANOVA). (D) EC 50 s for ghrelin derived from dose–response curves shown in (C) (SDC1 ratios). (E) Effect of all SDCs co-transfected at a GHSR:SDC ratio of 1:20 (** P < 0.005 (t-test), Emax for GHSR:SDC co-expression versus GHSR alone). (F) Effect of all SDCs co-transfected at a GHSR:SDC ratio of 1:1 (* P ≤ 0.05 (t-test), Emax for GHSR:SDC co-expression versus GHSR alone). (G) EC 50 s for ghrelin derived from SDC1–SDC4 dose–response curves shown in (E) and (F). (H) and (I) Dose–response curves of IP1 accumulation after ghrelin stimulation of cells expressing GHSR in the presence or absence of SDC1 at 1:20 and 1:1 ratios, respectively, corrected for baseline (* P ≤ 0.05 (t-test), Emax ghrelin-induced IP1 levels of 1:0 v. 1:20 or 1:1 ratio). (J) and (K) Dose–response curves of IP1 levels after ghrelin stimulation of cells expressing GHSR in the presence or absence of SDC1 at 1:20 and 1:1 ratios, respectively, expressed as % of maximum response in the absence of SDC1 (* P ≤ 0.05, ** P < 0.01 (t-test), basal IP1 levels of 1:0 v. 1:20 or 1:1 ratio, respectively). Data are mean ± SEM of three or more independent experiments.

Article Snippet: pCMV3 vectors containing cDNAs for human SDC1 (NM_001006946.1), SDC2 (NM_002998.3), SDC4 (NM_002999.2) and negative control were obtained from SinoBiological (Germany).

Techniques: Expressing, Control, Comparison, Derivative Assay, Cotransfection, Transfection

Journal: Journal of Molecular Endocrinology

Article Title: Syndecans modulate ghrelin receptor signaling

doi: 10.1530/JME-24-0070

Figure Lengend Snippet: Syndecans (SDCs) impair β-arrestin2 recruitment at growth hormone secretagogue receptor (GHSR). (A) Effect of SDC1 on ghrelin-stimulated β-arrestin2–GHSR interaction in HEK293 cells. Values were corrected for Emax of the control (*** P < 0.0005 versus 1:0 ratio GHSR:SDC1; # P < 0.05, ## P < 0.005 versus 1:2 ratio GHSR:SDC1). (B) Effect of SDC1 on the kinetic profile of the β-arrestin2–GHSR interaction upon ghrelin stimulation (outcome of RM-ANOVA shown on graph: P T , effect of time; P Ratio , effect of GHSR:SDC ratio; P TxRatio , interaction. * P < 0.05, all other ratios versus 1:0 ratio GHSR:SDC1; # P < 0.05, 1:1 and 1:2 versus 1:0 ratio; $ P < 0.05, 1:2 versus 1:0 ratio). Data derived from curve fitting of the kinetic profiles for β-arrestin2 recruitment by GHSR in cells transfected with control or increasing amounts of SDC1 expression plasmid. (C) Initial rate of recruitment. (D) Magnitude of peak response (letters a and b represent groups that are significantly different from each other ( P < 0.05; one-way ANOVA). Dose–response curve (E) (*** P < 0.0005 versus control; # P < 0.05 versus 1:2 ratio GHSR:SDC1) and kinetic curve (F) of the effect of all SDCs (GHSR:SDC of 1:2) on β-arrestin2 recruitment at GHSR (outcome of RM-ANOVA shown on graph. * P < 0.05, *** P < 0.001, all SDCs versus control; # P < 0.05, SDC1, SDC2 and SDC4 versus control; $ P < 0.05, SDC2 and SDC4 versus control. P T , effect of time; P Ratio , effect of GHSR:SDC ratio; P TxRatio , interaction). Data derived from curve fitting of the kinetic profiles for β-arrestin2 recruitment by GHSR in cells transfected with control or SDC1, SDC2, SDC3 or SDC4 expression plasmids. (G) Initial rate of recruitment. (H) Magnitude of peak response (letters a and b represent groups that are significantly different from each other ( P < 0.05; one-way ANOVA). Data are presented as mean ± SEM of three independent experiments. Emax, maximum response.

Article Snippet: pCMV3 vectors containing cDNAs for human SDC1 (NM_001006946.1), SDC2 (NM_002998.3), SDC4 (NM_002999.2) and negative control were obtained from SinoBiological (Germany).

Techniques: Control, Derivative Assay, Transfection, Expressing, Plasmid Preparation