Journal: Spinal cord

Article Title: Sodium hyaluronate-CNTF gelatinous particles promote axonal growth, neurogenesis and functional recovery after spinal cord injury.

doi: 10.1038/sc.2014.54

Figure Lengend Snippet: Figure 4 The b-tubulin-III–positive neuron-like cells and the differentiation of endogenous progenitors in the sodium hyaluronate-CNTF group. (a) At 1 month PO in the sodium hyaluronate-CNTF group, many small and process-extending b-tubulin-III–positive neuron-like cells (shown by white arrows) were observed at the lesion edge of the host cord. (b) The b-tubulin-III–positive neuron-like cells were immunoreactive for NeuN (shown by white arrows). (c) At 1 month PO in the sodium hyaluronate-CNTF group, the b-tubulin-III–positive neuron-like cells (shown by white arrows) were detectable in the lesion area. (d) High magnification of the boxed area in panel (c). The b-tubulin-III–positive neuronal fiber (shown by white arrowhead) extended and the b-tubulin-III– positive neuron-like cell seemed to form cell contacts (shown by white arrow). (e–h) At 4 days PO in the sodium hyaluronate-CNTF group, BrdU (red) and DCX (green) double-positive cells were observed at the lesion edge of the host cord, with neuron-like appearance. The cells directed by white arrows in panel (g) are shown in panel (h). (i–l) At 11 days PO in the sodium hyaluronate-CNTF group, BrdU (red) and b-tubulin-III (green) double-positive cells were observed in the lesion area. The cell directed by the white arrow in panel (k) is shown in panel (l). The dotted lines indicate the boundary between the host and lesion area. Scale bars: (a, e–g), 100mm; (b, c and h), 50mm; d, 25 mm; (i–k), 75 mm. A full color version of this figure is available at the Spinal Cord journal online.

Article Snippet: Spinal cord sections were incubated in the following primary antibodies (Ab) at 4 1C for 48 h: mouse anti-neurofilament (Pan) monoclonal Ab (NF, 1:50, Zymed Laboratories, South San Francisco, CA, USA); rabbit anti-b-tubulin-III protein polyclonal Ab (btubulin-III, 1:100, Sigma); rabbit anti-glial fibrillary acidic protein polyclonal Ab (1:150, Zymed Laboratories); mouse anti-BrdU monoclonal Ab (1:70, Bioss, Woburn, MA, USA); and rabbit anti-doublecortin protein polyclonal Ab (DCX, 1:100, Abcam, Cambridge, MA, USA).

Techniques:

Journal: Alzheimer's research & therapy

Article Title: TMEM106B expression is reduced in Alzheimer's disease brains.

doi: 10.1186/alzrt247

Figure Lengend Snippet: Figure 1 Multiple sequence alignment of TMEM106B protein. Multiple amino acid sequence alignment was performed by importing the corresponding amino acid sequences into CLC Free Workbench (CLC Bio/Qiagen, Aarhus, Denmark). (a) Multiple amino acid sequence alignment of TMEM106B orthologs derived from Homo sapiens, Pan troglodytes, Canis lupus familiaris, Bos Taurus, Mus musclus, Rattus norvegicus, Gallus gallus, Danio rerio, and Xenopus laevis. (b) Multiple amino acid sequence alignment of the human TMEM106A, TMEM106B, and TMEM106C proteins.

Article Snippet: After gel electrophoresis, the protein was transferred onto nitrocellulose membranes, followed by incubation at room temperature overnight with the anti-TMEM106B antibody A303-439A, rabbit polyclonal anti-TMEM106B antibody raised against a peptide spanning amino acid residues 101 to 200 of the human TMEM106B protein (bs-11694R; Bioss, Boston, MA, USA), rabbit polyclonal anti-TMEM106B antibody raised against the human TMEM106B-GST fusion protein (20995-1-AP; Proteintech, Chicago, IL, USA), or mouse monoclonal anti-Xpress antibody (Invitrogen).

Techniques: Sequencing, Derivative Assay

Journal: Alzheimer's research & therapy

Article Title: TMEM106B expression is reduced in Alzheimer's disease brains.

doi: 10.1186/alzrt247

Figure Lengend Snippet: Figure 2 Universal expression of TMEM106B mRNAs in human neural cells. mRNA expression was studied by reverse transcriptase (RT)-polymerase chain reaction (PCR) in human tissues and cultured cells. (a) TMEM106A, (b) TMEM106B, (c) TMEM106C, (d) progranulin (PGRN), and (e) G3PDH, a housekeeping gene for a positive control. The lanes indicate (1) the frontal cortex of the human cerebrum (CBR) with inclusion of the RT step, (2) CBR without inclusion of the RT step, (3) astrocytes (AS), (4) neuronal progenitor (NP) cells, (5) NTera2 teratocarcinoma-derived neurons, (6) SK-N-SH neuroblastoma, (7) IMR-32 neuroblastoma, (8) U-373MG glioblastoma, (9) T98G glioblastoma, and (10) HMO6 microglia. TMEM106A, TMEM106B, TMEM106C, and PGRN were amplified for 35 cycles, while G3PDH was amplified for 28 cycles.

Article Snippet: After gel electrophoresis, the protein was transferred onto nitrocellulose membranes, followed by incubation at room temperature overnight with the anti-TMEM106B antibody A303-439A, rabbit polyclonal anti-TMEM106B antibody raised against a peptide spanning amino acid residues 101 to 200 of the human TMEM106B protein (bs-11694R; Bioss, Boston, MA, USA), rabbit polyclonal anti-TMEM106B antibody raised against the human TMEM106B-GST fusion protein (20995-1-AP; Proteintech, Chicago, IL, USA), or mouse monoclonal anti-Xpress antibody (Invitrogen).

Techniques: Expressing, Reverse Transcription, Polymerase Chain Reaction, Cell Culture, Positive Control, Derivative Assay, Amplification

Journal: Alzheimer's research & therapy

Article Title: TMEM106B expression is reduced in Alzheimer's disease brains.

doi: 10.1186/alzrt247

Figure Lengend Snippet: Figure 3 Reduced expression of TMEM106B mRNA in Alzheimer’s disease brains. TMEM106B and progranulin (PGRN) mRNA expression levels were studied by quantitative reverse transcriptase-polymerase chain reaction (qPCR) in human brain tissues derived from a reference of the human frontal cortex (REF), four non-neurological control cases (NC), six amyotrophic lateral sclerosis (ALS) cases, four Parkinson’s disease (PD) cases, and seven Alzheimer’s disease (AD) cases. The expression levels were standardized against those of G3PDH. (a) TMEM106B mRNA expression. (b) PGRN mRNA expression. (c) Difference in TMEM106B levels between AD and non-AD cases. *P = 0.0035 by Student’s t test. (d) Difference in PGRN levels between AD and non-AD cases. **P = 0.0027 by Student’s t test. (e) Pearson’s correlation between TMEM106B and PGRN mRNA levels. Pearson’s correlation coefficient indicates −0.555 (P = 0.0090).

Article Snippet: After gel electrophoresis, the protein was transferred onto nitrocellulose membranes, followed by incubation at room temperature overnight with the anti-TMEM106B antibody A303-439A, rabbit polyclonal anti-TMEM106B antibody raised against a peptide spanning amino acid residues 101 to 200 of the human TMEM106B protein (bs-11694R; Bioss, Boston, MA, USA), rabbit polyclonal anti-TMEM106B antibody raised against the human TMEM106B-GST fusion protein (20995-1-AP; Proteintech, Chicago, IL, USA), or mouse monoclonal anti-Xpress antibody (Invitrogen).

Techniques: Expressing, Reverse Transcription, Polymerase Chain Reaction, Derivative Assay, Control

Journal: Alzheimer's research & therapy

Article Title: TMEM106B expression is reduced in Alzheimer's disease brains.

doi: 10.1186/alzrt247

Figure Lengend Snippet: Figure 4 Positive correlation between TMEM106B and neurofilament, heavy polypeptide mRNA levels. Neurofilament, heavy polypeptide (NFH), glial fibrillary acidic protein (GFAP), and RNA-binding protein, fox-1 homolog (Caenorhabditis elegans)-3 (RBFOX3, NEUN) mRNA expression levels were studied by quantitative reverse transcriptase-polymerase chain reaction (qPCR) in human brain tissues derived from a reference of the human frontal cortex (REF), four non-neurological causes (NC) cases, six amyotrophic lateral sclerosis (ALS) cases, four Parkinson’s disease PD cases, and seven AD cases. The expression levels were standardized against those of G3PDH. (a) NFH expression. (b) GFAP expression. (c) NEUN expression. (d) Pearson’s correlation between TMEM106B and NFH mRNA levels. Pearson’s correlation coefficient indicates 0.496 (P = 0.0221).

Article Snippet: After gel electrophoresis, the protein was transferred onto nitrocellulose membranes, followed by incubation at room temperature overnight with the anti-TMEM106B antibody A303-439A, rabbit polyclonal anti-TMEM106B antibody raised against a peptide spanning amino acid residues 101 to 200 of the human TMEM106B protein (bs-11694R; Bioss, Boston, MA, USA), rabbit polyclonal anti-TMEM106B antibody raised against the human TMEM106B-GST fusion protein (20995-1-AP; Proteintech, Chicago, IL, USA), or mouse monoclonal anti-Xpress antibody (Invitrogen).

Techniques: RNA Binding Assay, Expressing, Reverse Transcription, Polymerase Chain Reaction, Derivative Assay

Journal: Alzheimer's research & therapy

Article Title: TMEM106B expression is reduced in Alzheimer's disease brains.

doi: 10.1186/alzrt247

Figure Lengend Snippet: Figure 5 Characterization of anti-TMEM106B antibody. The full-length open reading frame (ORF) cloned in the vector that expresses a fusion protein with an N-terminal Xpress tag was transiently expressed in HeLa cells. Total protein extract was processed for western blot. Lanes represent the protein of (1) untransfected cells and the cells expressing (2) TMEM106A, (3) TMEM106B, or (4) TMEM106C, and the protein of (5) human brain #1, (6) human brain #2, or (7) IMR-32 neuroblastoma cells. Immunoblots of (a, d) TMEM106B (the A303-439A antibody), (b) Xpress, and (c, e) HSP60, an internal control for protein loading.

Article Snippet: After gel electrophoresis, the protein was transferred onto nitrocellulose membranes, followed by incubation at room temperature overnight with the anti-TMEM106B antibody A303-439A, rabbit polyclonal anti-TMEM106B antibody raised against a peptide spanning amino acid residues 101 to 200 of the human TMEM106B protein (bs-11694R; Bioss, Boston, MA, USA), rabbit polyclonal anti-TMEM106B antibody raised against the human TMEM106B-GST fusion protein (20995-1-AP; Proteintech, Chicago, IL, USA), or mouse monoclonal anti-Xpress antibody (Invitrogen).

Techniques: Clone Assay, Plasmid Preparation, Western Blot, Expressing, Control

Journal: Alzheimer's research & therapy

Article Title: TMEM106B expression is reduced in Alzheimer's disease brains.

doi: 10.1186/alzrt247

Figure Lengend Snippet: Figure 6 Reduced expression of TMEM106B protein in Alzheimer’s disease brains. Protein expression levels were studied by western blot in human brain tissues derived from four non-neurological causes (NC) cases, six amyotrophic lateral sclerosis (ALS) cases, four Parkinson’s disease (PD) cases, and seven Alzheimer’s disease (AD) cases. The expression levels were standardized against those of HSP60. (A) TMEM106B expression: (a) TMEM106B and (b) HSP60. (B) Progranulin (PGRN) expression: (a) PGRN and (b) HSP60. (C) Difference in TMEM106B levels between AD and non-AD cases. *P = 0.0000004 by Student’s t test. (D) Difference in PGRN levels between AD and non-AD cases. ns, non-significant (P = 0.5304 by Student’s t test). (E) Pearson’s correlation between TMEM106B and PGRN protein levels. Pearson’s correlation coefficient indicates −0.242 (P = 0.2912).

Article Snippet: After gel electrophoresis, the protein was transferred onto nitrocellulose membranes, followed by incubation at room temperature overnight with the anti-TMEM106B antibody A303-439A, rabbit polyclonal anti-TMEM106B antibody raised against a peptide spanning amino acid residues 101 to 200 of the human TMEM106B protein (bs-11694R; Bioss, Boston, MA, USA), rabbit polyclonal anti-TMEM106B antibody raised against the human TMEM106B-GST fusion protein (20995-1-AP; Proteintech, Chicago, IL, USA), or mouse monoclonal anti-Xpress antibody (Invitrogen).

Techniques: Expressing, Western Blot, Derivative Assay

Journal: Alzheimer's research & therapy

Article Title: TMEM106B expression is reduced in Alzheimer's disease brains.

doi: 10.1186/alzrt247

Figure Lengend Snippet: Figure 7 TMEM106B immunoreactivity in non-Alzheimer’s disease brains. Expression of TMEM106 immunoreactivity was studied in 13 non-Alzheimer’s disease brains presented in Table 1 by immunohistochemistry using the A303-439A antibody. (a) Non-neurological causes (NC), the frontal cortex, cytoplasmic staining of cortical neurons; (b) amyotrophic lateral sclerosis (ALS), the frontal cortex, cytoplasmic staining of cortical neurons; (c) NC, the hippocampal CA1 region, cytoplasmic staining of pyramidal neurons; (d) ALS, the hippocampal CA1 region, cytoplasmic staining of pyramidal neurons; (e) NC, the hippocampal CA1 region, intense staining of small nodular structures accumulated in the perinuclear region of pyramidal neurons; (f) NC, the frontal white matter, cytoplasmic staining of oligodendrocytes, reactive astrocytes, and microglia.

Article Snippet: After gel electrophoresis, the protein was transferred onto nitrocellulose membranes, followed by incubation at room temperature overnight with the anti-TMEM106B antibody A303-439A, rabbit polyclonal anti-TMEM106B antibody raised against a peptide spanning amino acid residues 101 to 200 of the human TMEM106B protein (bs-11694R; Bioss, Boston, MA, USA), rabbit polyclonal anti-TMEM106B antibody raised against the human TMEM106B-GST fusion protein (20995-1-AP; Proteintech, Chicago, IL, USA), or mouse monoclonal anti-Xpress antibody (Invitrogen).

Techniques: Expressing, Immunohistochemistry, Staining

Journal: Alzheimer's research & therapy

Article Title: TMEM106B expression is reduced in Alzheimer's disease brains.

doi: 10.1186/alzrt247

Figure Lengend Snippet: Figure 8 TMEM106B and PGRN immunoreactivities in Alzheimer’s disease brains. Expression of TMEM106 and progranulin (PGRN) immunoreactivities was studied in six Alzheimer’s disease brains presented in Table 1 by immunohistochemistry using the A303-439A antibody. (a) TMEM106B, the frontal cortex, moderate neuronal cytoplasmic staining and faint senile plaque staining; (b) PGRN, same region as (a), moderate senile plaque staining and diffuse neuropil staining; (c) TMEM106B, the hippocampal CA1 region, intense neuronal and astroglial cytoplasmic staining; (d) PGRN, same region as (c), intense perivascular neuropil staining; (e) TMEM106B, the hippocampal CA1 region, no staining of senile plaques and neurofibrillary tangles; (f) PGRN, same region as (e), moderate staining of numerous senile plaques and neurofibrillary tangles.

Article Snippet: After gel electrophoresis, the protein was transferred onto nitrocellulose membranes, followed by incubation at room temperature overnight with the anti-TMEM106B antibody A303-439A, rabbit polyclonal anti-TMEM106B antibody raised against a peptide spanning amino acid residues 101 to 200 of the human TMEM106B protein (bs-11694R; Bioss, Boston, MA, USA), rabbit polyclonal anti-TMEM106B antibody raised against the human TMEM106B-GST fusion protein (20995-1-AP; Proteintech, Chicago, IL, USA), or mouse monoclonal anti-Xpress antibody (Invitrogen).

Techniques: Expressing, Immunohistochemistry, Staining

Journal: BioMed Research International

Article Title: Isolation and Characterization of Chicken Dermis-Derived Mesenchymal Stem/Progenitor Cells

doi: 10.1155/2013/626258

Figure Lengend Snippet: Primer sequences used in RT-PCR assay.

Article Snippet: The cells were blocked with 10% normal goat serum (Santa Cruz Biotechnology, Santa Cruz, CA, USA) for 30 min and then incubated at room temperature for 1 h in 3% bovine serum albumin (BSA) containing the following antibodies: mouse anti- β -integrin (1 : 100; Abcam, Cambridge, MA, USA), mouse anti-CD44 (1 : 200; Abcam), mouse anti-nestin (1 : 200; Abcam), rabbit anti-synaptophysin (SYP) (1 : 100; Bioss, Beijing, China), rabbit anti-CD71 (1 : 200; Bioss), rabbit anti-CD73 (1 : 200; Bioss), rabbit anti-neurofilament (NF) (1 : 200; Bioss), or goat anti- β -III tubulin (1 : 200; Santa Cruz Biotechnology).

Techniques: Sequencing

Journal: BioMed Research International

Article Title: Isolation and Characterization of Chicken Dermis-Derived Mesenchymal Stem/Progenitor Cells

doi: 10.1155/2013/626258

Figure Lengend Snippet: Surface antigen characterization of DMS/PCs at different passages. DMS/PCs expressed numerous surface markers such as β -integrin, CD44, CD71, and CD73 but not CD34 (a hematopoietic marker). Immunofluorescence showed that β -integrin and CD44 were positive, while CD34 was negative (scale bar: 100 μ m).

Article Snippet: The cells were blocked with 10% normal goat serum (Santa Cruz Biotechnology, Santa Cruz, CA, USA) for 30 min and then incubated at room temperature for 1 h in 3% bovine serum albumin (BSA) containing the following antibodies: mouse anti- β -integrin (1 : 100; Abcam, Cambridge, MA, USA), mouse anti-CD44 (1 : 200; Abcam), mouse anti-nestin (1 : 200; Abcam), rabbit anti-synaptophysin (SYP) (1 : 100; Bioss, Beijing, China), rabbit anti-CD71 (1 : 200; Bioss), rabbit anti-CD73 (1 : 200; Bioss), rabbit anti-neurofilament (NF) (1 : 200; Bioss), or goat anti- β -III tubulin (1 : 200; Santa Cruz Biotechnology).

Techniques: Marker, Immunofluorescence

Journal: BioMed Research International

Article Title: Isolation and Characterization of Chicken Dermis-Derived Mesenchymal Stem/Progenitor Cells

doi: 10.1155/2013/626258

Figure Lengend Snippet: RT-PCR assays RT-PCR analysis showed that different passages DMS/PCs expressed β -integrin, CD44, CD71, and CD73. CD34 expression was negative. GAPDH served as the internal control.

Article Snippet: The cells were blocked with 10% normal goat serum (Santa Cruz Biotechnology, Santa Cruz, CA, USA) for 30 min and then incubated at room temperature for 1 h in 3% bovine serum albumin (BSA) containing the following antibodies: mouse anti- β -integrin (1 : 100; Abcam, Cambridge, MA, USA), mouse anti-CD44 (1 : 200; Abcam), mouse anti-nestin (1 : 200; Abcam), rabbit anti-synaptophysin (SYP) (1 : 100; Bioss, Beijing, China), rabbit anti-CD71 (1 : 200; Bioss), rabbit anti-CD73 (1 : 200; Bioss), rabbit anti-neurofilament (NF) (1 : 200; Bioss), or goat anti- β -III tubulin (1 : 200; Santa Cruz Biotechnology).

Techniques: Reverse Transcription Polymerase Chain Reaction, Expressing

Journal: EBioMedicine

Article Title: Batf3-dependent CD8α + Dendritic Cells Aggravates Atherosclerosis via Th1 Cell Induction and Enhanced CCL5 Expression in Plaque Macrophages

doi: 10.1016/j.ebiom.2017.04.008

Figure Lengend Snippet: Lack of CD8α + DCs led to decreased IFN-γ and CCL5 expression in the aorta. The Apoe −/− mice (n = 8) and the Batf3 −/− Apoe −/− mice (n = 8) were fed either a chow diet or Western diet for 12 weeks. (a) Analysis of aortic Ifng , Foxp3 , and Tbx21 mRNA expression by qPCR. (b) An aortic tissue ELISA analysis of IFN-γ. Data represent pg/mg aortic protein. (c) qPCR analysis of Il12a , Tnf , Il6 , Tgfb1 , and Il10 mRNA expression. (d) qPCR analysis of Ccl5 expression. (e) ELISA analysis of the CCL5 concentration in the aortic tissue. Data represent pg per mg aortic protein. Data are presented as mean ± SD. Differences of a P < 0.05 were considered to be statistically significant. * P < 0.05; ** P < 0.01; *** P < 0.001; ns, not significant. Data are representative of three independent experiments. See also Fig. S6.

Article Snippet: For the immunohistofluorescence analysis, the cryosections were stained with an antibody against CD45 (104; eBioscience Cat# 47-0451-82, RRID: AB_1548781 ), Mac3 (M3/84; BD Biosciences Cat# 550292, RRID: AB_393587 ), CCL5 (Bioss Inc. Cat# bs-1324R-Biotin, RRID: AB_11099534 ).

Techniques: Expressing, Western Blot, Enzyme-linked Immunosorbent Assay, Concentration Assay

Journal: EBioMedicine

Article Title: Batf3-dependent CD8α + Dendritic Cells Aggravates Atherosclerosis via Th1 Cell Induction and Enhanced CCL5 Expression in Plaque Macrophages

doi: 10.1016/j.ebiom.2017.04.008

Figure Lengend Snippet: IFN-γ promoted CCL5 expression on macrophages, promoting leukocytes infiltration into the plaque area. (a) Female Apoe −/− mice (n = 15) were put on a Western diet for eight weeks, then the aortic cells were pooled to prepared as described in the methods and stained with an antibody against CD45. Then, CD45 + leukocytes and CD45 − non-leukocytes were sorted by FACS, and qPCR was used to analyze Ccl5 mRNA expression. (b and c) Immunofluorescence of the aortic root. The Apoe −/− mice (n = 8) and the Batf3 −/− Apoe −/− mice (n = 8) were fed a Western diet for 12 weeks. The cryosections of the aortic root were stained with an antibody against CD45 (red), MAC3 (red), and CCL5 (green). The cell nuclei were counterstained with 4′,6-diamidino-2-phenylindole (DAPI) (blue). Images were viewed and captured with a Laser Scanning Confocal Microscope. Scale bars: 100 μm, dashed lines indicate the internal elastic lamina, arrows pointing to representative colocalized cells. (d) Primary splenic macrophages were sorted as described in supplementary data, and then treated with100 ng/mL IFN-γ for 6 h. Ccl5 mRNA expression was analyzed by qPCR. The Apoe −/− mice (n = 8) and the Batf3 −/− Apoe −/− mice (n = 8) were fed a Western diet for 6 weeks, and cryosections of the aortic root were performed. (e) H&E staining. Scale bars: 100 μm. (f) Immunohistochemistry. Representative images of leukocytes (CD45), T cells (CD3), DCs (CD11c), and macrophages (Mac3) in the aortic are shown. Scale bars: 200 μm. Data are presented as mean ± SD. Differences of a P < 0.05 were considered to be statistically significant. ** P < 0.01; *** P < 0.001; ns, not significant. Data are representative of three independent experiments.

Article Snippet: For the immunohistofluorescence analysis, the cryosections were stained with an antibody against CD45 (104; eBioscience Cat# 47-0451-82, RRID: AB_1548781 ), Mac3 (M3/84; BD Biosciences Cat# 550292, RRID: AB_393587 ), CCL5 (Bioss Inc. Cat# bs-1324R-Biotin, RRID: AB_11099534 ).

Techniques: Expressing, Western Blot, Staining, Immunofluorescence, Microscopy, Immunohistochemistry

Journal: Oncology Letters

Article Title: Role of T helper 17 cytokines in the tumour immune inflammation response of patients with laryngeal squamous cell carcinoma

doi: 10.3892/ol.2017.6253

Figure Lengend Snippet: Positive and negative expression of IL17/IL17R immunohistochemistry in tissue microarray sections. (A) Positive and (B) negative expression of IL17. (C) Positive and (D) negative expression of IL17R. Original magnification, ×20. IL, interleukin; R, receptor.

Article Snippet: The following anti-human monoclonal antibodies were used: Rabbit anti-IL17 (#bs-2140R; BIOSS, Beijing, China) and rabbit anti-IL17A receptor (IL17R; #bs-2606R; BIOSS).

Techniques: Expressing, Immunohistochemistry, Microarray

Journal: Oncology Letters

Article Title: Role of T helper 17 cytokines in the tumour immune inflammation response of patients with laryngeal squamous cell carcinoma

doi: 10.3892/ol.2017.6253

Figure Lengend Snippet: Positive results of IL17/IL17R immunohistochemistry in tumors and controls.

Article Snippet: The following anti-human monoclonal antibodies were used: Rabbit anti-IL17 (#bs-2140R; BIOSS, Beijing, China) and rabbit anti-IL17A receptor (IL17R; #bs-2606R; BIOSS).

Techniques: Immunohistochemistry

Journal: Oncology Letters

Article Title: Role of T helper 17 cytokines in the tumour immune inflammation response of patients with laryngeal squamous cell carcinoma

doi: 10.3892/ol.2017.6253

Figure Lengend Snippet: Reverse transcription-quantitative polymerase chain reaction analysis of the Th17-associated intracellular cytokines and transcription factors IL17, IL23 and RORγt in tumors and controls. *P<0.05. IL, interleukin; ROR, RAR-related orphan receptor; Cq, quantification cycle.

Article Snippet: The following anti-human monoclonal antibodies were used: Rabbit anti-IL17 (#bs-2140R; BIOSS, Beijing, China) and rabbit anti-IL17A receptor (IL17R; #bs-2606R; BIOSS).

Techniques: Real-time Polymerase Chain Reaction