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Santa Cruz Biotechnology mouse anti human par2 antibody

Examination of the mechanism of influence of TF on Tau protein expression and phosphorylation in differentiated SH-SY5Y cells. SH-SY5Y (2 × 10 5 ) were treated with recombinant relipidated Innovin TF (0.65 ng/ml) together with or without human fVIIa (5 nM) or fVIIa alone. In some experiments, the TF aliquots were pre-incubated for 1 h, with 10H10 antibody (20 µg/ml) capable of blocking TF signalling, HTF-1 antibody (20 µg/ml) to block TF-fVIIa protease/procoagulant activity, or a mouse control isotype IgG antibody (20 µg/ml; not shown). In other experiments, fVIIa was pre-incubated for 1 h with the chemical inhibitor PCI27483 (10 µg/ml). Alternatively, the neuronal cells were treated with AIIB2 antibody (20 µg/ml) to block β1-integrin signalling, SAM11 antibody (20 µg/ml) capable of blocking <t>PAR2</t> signalling, or PAR2-activating peptide (PAR2-AP; 20 µM) to induce PAR2 signalling. Cells were harvested at 24 h, and cellular lysates (10 µg protein) were examined for Tau and phospho-Thr181 Tau by western blot analysis. All values were normalised against the respective GAPDH and for comparison, all ratios were calculated against the average from the non-treated cells ± the calculated standard deviation. The number of experiments is shown in each column, and all data groups were determined to have normal distributions and are shown in each column. A SH-SY5Y protein electrophoresis, B SH-SY5Y phospho-Thr181 Tau electrophoresis, C SH-SY5Y Tau protein ratio, and D SH-SY5Y phospho-Thr181 Tau ratio

Mouse Anti Human Par2 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 491 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+par2/pmc12847580-51-21-28?v=Santa+Cruz+Biotechnology
Average 94 stars, based on 491 article reviews

mouse anti human par2 antibody - by Bioz Stars, 2026-07

94/100 stars

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1) Product Images from "Procoagulant Extracellular Vesicles Increase Neuronal Tau expression, Metabolism and Processing Through Tissue Factor and Protease Activated Receptor 2"

Article Title: Procoagulant Extracellular Vesicles Increase Neuronal Tau expression, Metabolism and Processing Through Tissue Factor and Protease Activated Receptor 2

Journal: Cellular and Molecular Neurobiology

doi: 10.1007/s10571-025-01658-7

Figure Legend Snippet: Examination of the mechanism of influence of TF on Tau protein expression and phosphorylation in differentiated SH-SY5Y cells. SH-SY5Y (2 × 10 5 ) were treated with recombinant relipidated Innovin TF (0.65 ng/ml) together with or without human fVIIa (5 nM) or fVIIa alone. In some experiments, the TF aliquots were pre-incubated for 1 h, with 10H10 antibody (20 µg/ml) capable of blocking TF signalling, HTF-1 antibody (20 µg/ml) to block TF-fVIIa protease/procoagulant activity, or a mouse control isotype IgG antibody (20 µg/ml; not shown). In other experiments, fVIIa was pre-incubated for 1 h with the chemical inhibitor PCI27483 (10 µg/ml). Alternatively, the neuronal cells were treated with AIIB2 antibody (20 µg/ml) to block β1-integrin signalling, SAM11 antibody (20 µg/ml) capable of blocking PAR2 signalling, or PAR2-activating peptide (PAR2-AP; 20 µM) to induce PAR2 signalling. Cells were harvested at 24 h, and cellular lysates (10 µg protein) were examined for Tau and phospho-Thr181 Tau by western blot analysis. All values were normalised against the respective GAPDH and for comparison, all ratios were calculated against the average from the non-treated cells ± the calculated standard deviation. The number of experiments is shown in each column, and all data groups were determined to have normal distributions and are shown in each column. A SH-SY5Y protein electrophoresis, B SH-SY5Y phospho-Thr181 Tau electrophoresis, C SH-SY5Y Tau protein ratio, and D SH-SY5Y phospho-Thr181 Tau ratio

Techniques Used: Expressing, Phospho-proteomics, Recombinant, Incubation, Blocking Assay, Activity Assay, Control, Western Blot, Comparison, Standard Deviation, Protein Electrophoresis, Electrophoresis

Time-course analysis of the Tau protein fragments in differentiated SH-SY5Y cells, following treatment with TF . SH-SY5Y (2 × 10 5 ) were treated with as single dose of recombinant relipidated Innovin TF (0.65 ng/ml) together with human fVIIa (5 nM). In some experiments, the TF aliquots were pre-incubated for 1 h, with 10H10 antibody (20 µg/ml) capable of blocking TF signalling, HTF-1 antibody (20 µg/ml) to block TF-fVIIa protease/procoagulant activity, or a mouse control isotype IgG antibody (20 µg/ml; not shown). Alternatively, the neuronal cells were treated with AIIB2 antibody (20 µg/ml) to block β1-integrin signalling, or SAM11 antibody (20 µg/ml) capable of blocking PAR2 signalling. Sets of cells were harvested at A 48 h and D at 72 h and cellular lysates (10 µg protein) were examined for Tau by western blot analysis. All values were normalised against the respective GAPDH (see Supplementary Fig. 6 A and B) and for comparison, all ratios were calculated against the average from the non-treated cells ± the calculated standard deviation. The data were obtained from 6 biological experiments, and all data groups were determined to have normal distributions. A Electrophoresis at 48 h, B calculated ratios of 50 kDa bands at 48 h, C calculated ratios of 30–35 kDa bands at 48 h, D electrophoresis at 72 h, E calculated ratios of 50 kDa bands at 72 h, F calculated ratios of 40 kDa bands at 72 h, G calculated ratios of 30–35 kDa bands at 72 h

Figure Legend Snippet: Time-course analysis of the Tau protein fragments in differentiated SH-SY5Y cells, following treatment with TF . SH-SY5Y (2 × 10 5 ) were treated with as single dose of recombinant relipidated Innovin TF (0.65 ng/ml) together with human fVIIa (5 nM). In some experiments, the TF aliquots were pre-incubated for 1 h, with 10H10 antibody (20 µg/ml) capable of blocking TF signalling, HTF-1 antibody (20 µg/ml) to block TF-fVIIa protease/procoagulant activity, or a mouse control isotype IgG antibody (20 µg/ml; not shown). Alternatively, the neuronal cells were treated with AIIB2 antibody (20 µg/ml) to block β1-integrin signalling, or SAM11 antibody (20 µg/ml) capable of blocking PAR2 signalling. Sets of cells were harvested at A 48 h and D at 72 h and cellular lysates (10 µg protein) were examined for Tau by western blot analysis. All values were normalised against the respective GAPDH (see Supplementary Fig. 6 A and B) and for comparison, all ratios were calculated against the average from the non-treated cells ± the calculated standard deviation. The data were obtained from 6 biological experiments, and all data groups were determined to have normal distributions. A Electrophoresis at 48 h, B calculated ratios of 50 kDa bands at 48 h, C calculated ratios of 30–35 kDa bands at 48 h, D electrophoresis at 72 h, E calculated ratios of 50 kDa bands at 72 h, F calculated ratios of 40 kDa bands at 72 h, G calculated ratios of 30–35 kDa bands at 72 h

Techniques Used: Recombinant, Incubation, Blocking Assay, Activity Assay, Control, Western Blot, Comparison, Standard Deviation, Electrophoresis

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Journal: Cellular and Molecular Neurobiology

Article Title: Procoagulant Extracellular Vesicles Increase Neuronal Tau expression, Metabolism and Processing Through Tissue Factor and Protease Activated Receptor 2

doi: 10.1007/s10571-025-01658-7

Figure Lengend Snippet: Examination of the mechanism of influence of TF on Tau protein expression and phosphorylation in differentiated SH-SY5Y cells. SH-SY5Y (2 × 10 5 ) were treated with recombinant relipidated Innovin TF (0.65 ng/ml) together with or without human fVIIa (5 nM) or fVIIa alone. In some experiments, the TF aliquots were pre-incubated for 1 h, with 10H10 antibody (20 µg/ml) capable of blocking TF signalling, HTF-1 antibody (20 µg/ml) to block TF-fVIIa protease/procoagulant activity, or a mouse control isotype IgG antibody (20 µg/ml; not shown). In other experiments, fVIIa was pre-incubated for 1 h with the chemical inhibitor PCI27483 (10 µg/ml). Alternatively, the neuronal cells were treated with AIIB2 antibody (20 µg/ml) to block β1-integrin signalling, SAM11 antibody (20 µg/ml) capable of blocking PAR2 signalling, or PAR2-activating peptide (PAR2-AP; 20 µM) to induce PAR2 signalling. Cells were harvested at 24 h, and cellular lysates (10 µg protein) were examined for Tau and phospho-Thr181 Tau by western blot analysis. All values were normalised against the respective GAPDH and for comparison, all ratios were calculated against the average from the non-treated cells ± the calculated standard deviation. The number of experiments is shown in each column, and all data groups were determined to have normal distributions and are shown in each column. A SH-SY5Y protein electrophoresis, B SH-SY5Y phospho-Thr181 Tau electrophoresis, C SH-SY5Y Tau protein ratio, and D SH-SY5Y phospho-Thr181 Tau ratio

Article Snippet: Alternatively, the neuronal cells were treated with a rat anti-human antibody (20 μg/ml; AIIB2; Merck KGaA) to block β1-integrin signalling, a mouse anti-human PAR2 antibody, SAM11 (20 μg/ml; Santa Cruz Biotechnology, Heidelberg, Germany), capable of blocking PAR2 signalling, or PAR2-activating peptide (PAR2-AP; 20 μM) to induce PAR2 signalling.

Techniques: Expressing, Phospho-proteomics, Recombinant, Incubation, Blocking Assay, Activity Assay, Control, Western Blot, Comparison, Standard Deviation, Protein Electrophoresis, Electrophoresis

Journal: Cellular and Molecular Neurobiology

Article Title: Procoagulant Extracellular Vesicles Increase Neuronal Tau expression, Metabolism and Processing Through Tissue Factor and Protease Activated Receptor 2

doi: 10.1007/s10571-025-01658-7

Figure Lengend Snippet: Time-course analysis of the Tau protein fragments in differentiated SH-SY5Y cells, following treatment with TF . SH-SY5Y (2 × 10 5 ) were treated with as single dose of recombinant relipidated Innovin TF (0.65 ng/ml) together with human fVIIa (5 nM). In some experiments, the TF aliquots were pre-incubated for 1 h, with 10H10 antibody (20 µg/ml) capable of blocking TF signalling, HTF-1 antibody (20 µg/ml) to block TF-fVIIa protease/procoagulant activity, or a mouse control isotype IgG antibody (20 µg/ml; not shown). Alternatively, the neuronal cells were treated with AIIB2 antibody (20 µg/ml) to block β1-integrin signalling, or SAM11 antibody (20 µg/ml) capable of blocking PAR2 signalling. Sets of cells were harvested at A 48 h and D at 72 h and cellular lysates (10 µg protein) were examined for Tau by western blot analysis. All values were normalised against the respective GAPDH (see Supplementary Fig. 6 A and B) and for comparison, all ratios were calculated against the average from the non-treated cells ± the calculated standard deviation. The data were obtained from 6 biological experiments, and all data groups were determined to have normal distributions. A Electrophoresis at 48 h, B calculated ratios of 50 kDa bands at 48 h, C calculated ratios of 30–35 kDa bands at 48 h, D electrophoresis at 72 h, E calculated ratios of 50 kDa bands at 72 h, F calculated ratios of 40 kDa bands at 72 h, G calculated ratios of 30–35 kDa bands at 72 h

Techniques: Recombinant, Incubation, Blocking Assay, Activity Assay, Control, Western Blot, Comparison, Standard Deviation, Electrophoresis

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