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polyclonal abs against alboserpin  (Noble Life Sciences)

 
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    Noble Life Sciences polyclonal abs against alboserpin
    HDMVECns were left untreated (control), treated with <t>Alboserpin</t> (50 nM) or FXa (50 nM), or Alboserpin:FXa for 3 h. (A) Cell supernatants were used for cytokine and chemokine Luminex ELISA. (B) Gene expression of PARs in HDMVECns. Data are shown as relative quantification versus control (resting cells). (C) ERK1/2 protein expression was analyzed by Western blot. Cell lysates were analyzed for levels of p-ERK, and ERK (total ERK) and GAPDH was used as a loading control. ( D ) The ratio of p-ERK/ERK is presented in arbitrary units (A.U). ( E ) ERK1/2 protein expression was analyzed using In-Cell Western blots (ICW). ( F ) Intensity ratio (p-ERK/ERK). ( G and H ) NF-κB gene expression and protein expression were analyzed using RT-PCR and Western blots, respectively. (I and J) ICAM and VCAM gene expression were analyzed using RT-PCR. Data are shown as relative quantification versus control (resting cells). Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.
    Polyclonal Abs Against Alboserpin, supplied by Noble Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal abs against alboserpin/product/Noble Life Sciences
    Average 90 stars, based on 1 article reviews
    polyclonal abs against alboserpin - by Bioz Stars, 2026-04
    90/100 stars

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    1) Product Images from "Alboserpin, the Main Salivary Anticoagulant from the Disease Vector Aedes albopictus , Displays Anti–FXa-PAR Signaling In Vitro and In Vivo"

    Article Title: Alboserpin, the Main Salivary Anticoagulant from the Disease Vector Aedes albopictus , Displays Anti–FXa-PAR Signaling In Vitro and In Vivo

    Journal: ImmunoHorizons

    doi: 10.4049/immunohorizons.2200045

    HDMVECns were left untreated (control), treated with Alboserpin (50 nM) or FXa (50 nM), or Alboserpin:FXa for 3 h. (A) Cell supernatants were used for cytokine and chemokine Luminex ELISA. (B) Gene expression of PARs in HDMVECns. Data are shown as relative quantification versus control (resting cells). (C) ERK1/2 protein expression was analyzed by Western blot. Cell lysates were analyzed for levels of p-ERK, and ERK (total ERK) and GAPDH was used as a loading control. ( D ) The ratio of p-ERK/ERK is presented in arbitrary units (A.U). ( E ) ERK1/2 protein expression was analyzed using In-Cell Western blots (ICW). ( F ) Intensity ratio (p-ERK/ERK). ( G and H ) NF-κB gene expression and protein expression were analyzed using RT-PCR and Western blots, respectively. (I and J) ICAM and VCAM gene expression were analyzed using RT-PCR. Data are shown as relative quantification versus control (resting cells). Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.
    Figure Legend Snippet: HDMVECns were left untreated (control), treated with Alboserpin (50 nM) or FXa (50 nM), or Alboserpin:FXa for 3 h. (A) Cell supernatants were used for cytokine and chemokine Luminex ELISA. (B) Gene expression of PARs in HDMVECns. Data are shown as relative quantification versus control (resting cells). (C) ERK1/2 protein expression was analyzed by Western blot. Cell lysates were analyzed for levels of p-ERK, and ERK (total ERK) and GAPDH was used as a loading control. ( D ) The ratio of p-ERK/ERK is presented in arbitrary units (A.U). ( E ) ERK1/2 protein expression was analyzed using In-Cell Western blots (ICW). ( F ) Intensity ratio (p-ERK/ERK). ( G and H ) NF-κB gene expression and protein expression were analyzed using RT-PCR and Western blots, respectively. (I and J) ICAM and VCAM gene expression were analyzed using RT-PCR. Data are shown as relative quantification versus control (resting cells). Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Techniques Used: Control, Luminex, Enzyme-linked Immunosorbent Assay, Gene Expression, Quantitative Proteomics, Expressing, Western Blot, In-Cell ELISA, Reverse Transcription Polymerase Chain Reaction

    Representative data of FXa cleavage on PAR-2 peptide was investigated based on fluorescence resonance energy transfer (FRET) technology. Peptide sequence that spans the cleavage sites for mouse PAR-2 (NSKGRSLIGR) was synthesized with the fluorescent group Mca (7-methoxycoumarin-4-acetic acid) and the quenching group Dnp (2,4-DNP) at the N- and C-terminal ends, respectively. FXa (10 nM) was incubated with different concentrations of purified Alboserpin (0–200 nM) at 37°C in 20mMTris–HCl, 150 mM NaCl, Tween 20 0.01% (pH 7.4). After 15-min incubation, peptide was added in a 100 μl final reaction volume. The peptide hydrolysis rate was followed at 320 nm excitation and 420 nm emission in kinetic mode at 30°C in a microplate reader
    Figure Legend Snippet: Representative data of FXa cleavage on PAR-2 peptide was investigated based on fluorescence resonance energy transfer (FRET) technology. Peptide sequence that spans the cleavage sites for mouse PAR-2 (NSKGRSLIGR) was synthesized with the fluorescent group Mca (7-methoxycoumarin-4-acetic acid) and the quenching group Dnp (2,4-DNP) at the N- and C-terminal ends, respectively. FXa (10 nM) was incubated with different concentrations of purified Alboserpin (0–200 nM) at 37°C in 20mMTris–HCl, 150 mM NaCl, Tween 20 0.01% (pH 7.4). After 15-min incubation, peptide was added in a 100 μl final reaction volume. The peptide hydrolysis rate was followed at 320 nm excitation and 420 nm emission in kinetic mode at 30°C in a microplate reader

    Techniques Used: Fluorescence, Förster Resonance Energy Transfer, Sequencing, Synthesized, Incubation, Purification

    Effect of Alboserpin in paw edema assay triggered by FXa. ( A ) Footpads of C3H/HeJ mice were intradermally injected with 30 μl of FXa (50 nM) alone or incubated along with 50 nM Alboserpin. As a control, 30 μl of PBS or 30 ml of 1 mg Alboserpin was injected. Formation of edema (increasein paw thickness in millimeters) was measured using a caliper before injection of FXa or after 15, 30, 45, and 60 min of injections. Data represent SEM of five footpads per experimental group. ( B ) Effect of Alboserpin in FXa-induced inflammatory cytokine and chemokine. Cytokine and chemokine levels in paw tissue extracts after 60 min of intradermal injection were determined by Luminex ELISA assay. Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM of eight footpads per experimental group. Error bars indicate SEM. ** p < 0.01, **** p < 0.0001. ns, not significant.
    Figure Legend Snippet: Effect of Alboserpin in paw edema assay triggered by FXa. ( A ) Footpads of C3H/HeJ mice were intradermally injected with 30 μl of FXa (50 nM) alone or incubated along with 50 nM Alboserpin. As a control, 30 μl of PBS or 30 ml of 1 mg Alboserpin was injected. Formation of edema (increasein paw thickness in millimeters) was measured using a caliper before injection of FXa or after 15, 30, 45, and 60 min of injections. Data represent SEM of five footpads per experimental group. ( B ) Effect of Alboserpin in FXa-induced inflammatory cytokine and chemokine. Cytokine and chemokine levels in paw tissue extracts after 60 min of intradermal injection were determined by Luminex ELISA assay. Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM of eight footpads per experimental group. Error bars indicate SEM. ** p < 0.01, **** p < 0.0001. ns, not significant.

    Techniques Used: Injection, Incubation, Control, Luminex, Enzyme-linked Immunosorbent Assay

    Endothelial cell monolayer permeability assay using FITC-dextran. ( A ) Crystal violet staining of the HDMVECn monolayer pretreated with Alboserpin and FXa at 50 nM for 4 h. ( B ) The fluorescence intensity of FITC-conjugated dextran leaking from the upper to the lower chambers was measured at different time points after treatment of HDMVECns with either FXa alone, Alboserpin, or Alboserpin along with FXa. Data from three independent experiments performed in duplicate are plotted. Error bars indicate SEM. ( C and D ) Schematic representation of the sequential steps of the Miles assay in the mouse and corresponding inoculations in different locations in skin biopsies. ( E ) Spectrophotometric analysis (610 nm) of vascular leaked formamide-extracted Evans blue dye content in the skin injected with 50 μM Alboserpin, FXa, and both FXa-Alboserpin at the same concentration. PBS was used as a negative control. * p < 0.05, *** p < 0.001, **** p < 0.0001. ns, not significant.
    Figure Legend Snippet: Endothelial cell monolayer permeability assay using FITC-dextran. ( A ) Crystal violet staining of the HDMVECn monolayer pretreated with Alboserpin and FXa at 50 nM for 4 h. ( B ) The fluorescence intensity of FITC-conjugated dextran leaking from the upper to the lower chambers was measured at different time points after treatment of HDMVECns with either FXa alone, Alboserpin, or Alboserpin along with FXa. Data from three independent experiments performed in duplicate are plotted. Error bars indicate SEM. ( C and D ) Schematic representation of the sequential steps of the Miles assay in the mouse and corresponding inoculations in different locations in skin biopsies. ( E ) Spectrophotometric analysis (610 nm) of vascular leaked formamide-extracted Evans blue dye content in the skin injected with 50 μM Alboserpin, FXa, and both FXa-Alboserpin at the same concentration. PBS was used as a negative control. * p < 0.05, *** p < 0.001, **** p < 0.0001. ns, not significant.

    Techniques Used: Permeability, Staining, Fluorescence, Injection, Concentration Assay, Negative Control

    During a mosquito bite, tissue injury causes the initiation of signaling through the extrinsic and intrinsic pathways that leads to the formation of FXa. FXa further converts prothrombin to thrombin, leading to clot formation. FXa triggers an inflammatory pathway in the endothelial cells by activating PAR receptors, ICAM and VCAM adhesion molecule expression, ERK1/2 signaling, NF-κB signaling, secretion of inflammatory cytokines, and disruption of endothelial cell barrier permeability. Mosquito A. albopictus salivary gland protein Alboserpin, a highly specific, strong inhibitor of FXa, prevents cleavage of PAR-2 by FXa, resulting in strong anti-inflammatory activity in vitro and in vivo.
    Figure Legend Snippet: During a mosquito bite, tissue injury causes the initiation of signaling through the extrinsic and intrinsic pathways that leads to the formation of FXa. FXa further converts prothrombin to thrombin, leading to clot formation. FXa triggers an inflammatory pathway in the endothelial cells by activating PAR receptors, ICAM and VCAM adhesion molecule expression, ERK1/2 signaling, NF-κB signaling, secretion of inflammatory cytokines, and disruption of endothelial cell barrier permeability. Mosquito A. albopictus salivary gland protein Alboserpin, a highly specific, strong inhibitor of FXa, prevents cleavage of PAR-2 by FXa, resulting in strong anti-inflammatory activity in vitro and in vivo.

    Techniques Used: Expressing, Disruption, Permeability, Activity Assay, In Vitro, In Vivo



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    polyclonal abs against alboserpin  (Noble Life Sciences)
    90
    Noble Life Sciences polyclonal abs against alboserpin
    HDMVECns were left untreated (control), treated with <t>Alboserpin</t> (50 nM) or FXa (50 nM), or Alboserpin:FXa for 3 h. (A) Cell supernatants were used for cytokine and chemokine Luminex ELISA. (B) Gene expression of PARs in HDMVECns. Data are shown as relative quantification versus control (resting cells). (C) ERK1/2 protein expression was analyzed by Western blot. Cell lysates were analyzed for levels of p-ERK, and ERK (total ERK) and GAPDH was used as a loading control. ( D ) The ratio of p-ERK/ERK is presented in arbitrary units (A.U). ( E ) ERK1/2 protein expression was analyzed using In-Cell Western blots (ICW). ( F ) Intensity ratio (p-ERK/ERK). ( G and H ) NF-κB gene expression and protein expression were analyzed using RT-PCR and Western blots, respectively. (I and J) ICAM and VCAM gene expression were analyzed using RT-PCR. Data are shown as relative quantification versus control (resting cells). Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.
    Polyclonal Abs Against Alboserpin, supplied by Noble Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal abs against alboserpin/product/Noble Life Sciences
    Average 90 stars, based on 1 article reviews
    polyclonal abs against alboserpin - by Bioz Stars, 2026-04
    90/100 stars
    		  Buy from Supplier

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    HDMVECns were left untreated (control), treated with Alboserpin (50 nM) or FXa (50 nM), or Alboserpin:FXa for 3 h. (A) Cell supernatants were used for cytokine and chemokine Luminex ELISA. (B) Gene expression of PARs in HDMVECns. Data are shown as relative quantification versus control (resting cells). (C) ERK1/2 protein expression was analyzed by Western blot. Cell lysates were analyzed for levels of p-ERK, and ERK (total ERK) and GAPDH was used as a loading control. ( D ) The ratio of p-ERK/ERK is presented in arbitrary units (A.U). ( E ) ERK1/2 protein expression was analyzed using In-Cell Western blots (ICW). ( F ) Intensity ratio (p-ERK/ERK). ( G and H ) NF-κB gene expression and protein expression were analyzed using RT-PCR and Western blots, respectively. (I and J) ICAM and VCAM gene expression were analyzed using RT-PCR. Data are shown as relative quantification versus control (resting cells). Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Journal: ImmunoHorizons

    Article Title: Alboserpin, the Main Salivary Anticoagulant from the Disease Vector Aedes albopictus , Displays Anti–FXa-PAR Signaling In Vitro and In Vivo

    doi: 10.4049/immunohorizons.2200045

    Figure Lengend Snippet: HDMVECns were left untreated (control), treated with Alboserpin (50 nM) or FXa (50 nM), or Alboserpin:FXa for 3 h. (A) Cell supernatants were used for cytokine and chemokine Luminex ELISA. (B) Gene expression of PARs in HDMVECns. Data are shown as relative quantification versus control (resting cells). (C) ERK1/2 protein expression was analyzed by Western blot. Cell lysates were analyzed for levels of p-ERK, and ERK (total ERK) and GAPDH was used as a loading control. ( D ) The ratio of p-ERK/ERK is presented in arbitrary units (A.U). ( E ) ERK1/2 protein expression was analyzed using In-Cell Western blots (ICW). ( F ) Intensity ratio (p-ERK/ERK). ( G and H ) NF-κB gene expression and protein expression were analyzed using RT-PCR and Western blots, respectively. (I and J) ICAM and VCAM gene expression were analyzed using RT-PCR. Data are shown as relative quantification versus control (resting cells). Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Article Snippet: Polyclonal Abs against Alboserpin were raised in rabbits by Noble Life Sciences (Woodbine) using a standard protocol.

    Techniques: Control, Luminex, Enzyme-linked Immunosorbent Assay, Gene Expression, Quantitative Proteomics, Expressing, Western Blot, In-Cell ELISA, Reverse Transcription Polymerase Chain Reaction

    Representative data of FXa cleavage on PAR-2 peptide was investigated based on fluorescence resonance energy transfer (FRET) technology. Peptide sequence that spans the cleavage sites for mouse PAR-2 (NSKGRSLIGR) was synthesized with the fluorescent group Mca (7-methoxycoumarin-4-acetic acid) and the quenching group Dnp (2,4-DNP) at the N- and C-terminal ends, respectively. FXa (10 nM) was incubated with different concentrations of purified Alboserpin (0–200 nM) at 37°C in 20mMTris–HCl, 150 mM NaCl, Tween 20 0.01% (pH 7.4). After 15-min incubation, peptide was added in a 100 μl final reaction volume. The peptide hydrolysis rate was followed at 320 nm excitation and 420 nm emission in kinetic mode at 30°C in a microplate reader

    Journal: ImmunoHorizons

    Article Title: Alboserpin, the Main Salivary Anticoagulant from the Disease Vector Aedes albopictus , Displays Anti–FXa-PAR Signaling In Vitro and In Vivo

    doi: 10.4049/immunohorizons.2200045

    Figure Lengend Snippet: Representative data of FXa cleavage on PAR-2 peptide was investigated based on fluorescence resonance energy transfer (FRET) technology. Peptide sequence that spans the cleavage sites for mouse PAR-2 (NSKGRSLIGR) was synthesized with the fluorescent group Mca (7-methoxycoumarin-4-acetic acid) and the quenching group Dnp (2,4-DNP) at the N- and C-terminal ends, respectively. FXa (10 nM) was incubated with different concentrations of purified Alboserpin (0–200 nM) at 37°C in 20mMTris–HCl, 150 mM NaCl, Tween 20 0.01% (pH 7.4). After 15-min incubation, peptide was added in a 100 μl final reaction volume. The peptide hydrolysis rate was followed at 320 nm excitation and 420 nm emission in kinetic mode at 30°C in a microplate reader

    Article Snippet: Polyclonal Abs against Alboserpin were raised in rabbits by Noble Life Sciences (Woodbine) using a standard protocol.

    Techniques: Fluorescence, Förster Resonance Energy Transfer, Sequencing, Synthesized, Incubation, Purification

    Effect of Alboserpin in paw edema assay triggered by FXa. ( A ) Footpads of C3H/HeJ mice were intradermally injected with 30 μl of FXa (50 nM) alone or incubated along with 50 nM Alboserpin. As a control, 30 μl of PBS or 30 ml of 1 mg Alboserpin was injected. Formation of edema (increasein paw thickness in millimeters) was measured using a caliper before injection of FXa or after 15, 30, 45, and 60 min of injections. Data represent SEM of five footpads per experimental group. ( B ) Effect of Alboserpin in FXa-induced inflammatory cytokine and chemokine. Cytokine and chemokine levels in paw tissue extracts after 60 min of intradermal injection were determined by Luminex ELISA assay. Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM of eight footpads per experimental group. Error bars indicate SEM. ** p < 0.01, **** p < 0.0001. ns, not significant.

    Journal: ImmunoHorizons

    Article Title: Alboserpin, the Main Salivary Anticoagulant from the Disease Vector Aedes albopictus , Displays Anti–FXa-PAR Signaling In Vitro and In Vivo

    doi: 10.4049/immunohorizons.2200045

    Figure Lengend Snippet: Effect of Alboserpin in paw edema assay triggered by FXa. ( A ) Footpads of C3H/HeJ mice were intradermally injected with 30 μl of FXa (50 nM) alone or incubated along with 50 nM Alboserpin. As a control, 30 μl of PBS or 30 ml of 1 mg Alboserpin was injected. Formation of edema (increasein paw thickness in millimeters) was measured using a caliper before injection of FXa or after 15, 30, 45, and 60 min of injections. Data represent SEM of five footpads per experimental group. ( B ) Effect of Alboserpin in FXa-induced inflammatory cytokine and chemokine. Cytokine and chemokine levels in paw tissue extracts after 60 min of intradermal injection were determined by Luminex ELISA assay. Data from three independent experiments performed in triplicate are plotted. Error bars indicate SEM of eight footpads per experimental group. Error bars indicate SEM. ** p < 0.01, **** p < 0.0001. ns, not significant.

    Article Snippet: Polyclonal Abs against Alboserpin were raised in rabbits by Noble Life Sciences (Woodbine) using a standard protocol.

    Techniques: Injection, Incubation, Control, Luminex, Enzyme-linked Immunosorbent Assay

    Endothelial cell monolayer permeability assay using FITC-dextran. ( A ) Crystal violet staining of the HDMVECn monolayer pretreated with Alboserpin and FXa at 50 nM for 4 h. ( B ) The fluorescence intensity of FITC-conjugated dextran leaking from the upper to the lower chambers was measured at different time points after treatment of HDMVECns with either FXa alone, Alboserpin, or Alboserpin along with FXa. Data from three independent experiments performed in duplicate are plotted. Error bars indicate SEM. ( C and D ) Schematic representation of the sequential steps of the Miles assay in the mouse and corresponding inoculations in different locations in skin biopsies. ( E ) Spectrophotometric analysis (610 nm) of vascular leaked formamide-extracted Evans blue dye content in the skin injected with 50 μM Alboserpin, FXa, and both FXa-Alboserpin at the same concentration. PBS was used as a negative control. * p < 0.05, *** p < 0.001, **** p < 0.0001. ns, not significant.

    Journal: ImmunoHorizons

    Article Title: Alboserpin, the Main Salivary Anticoagulant from the Disease Vector Aedes albopictus , Displays Anti–FXa-PAR Signaling In Vitro and In Vivo

    doi: 10.4049/immunohorizons.2200045

    Figure Lengend Snippet: Endothelial cell monolayer permeability assay using FITC-dextran. ( A ) Crystal violet staining of the HDMVECn monolayer pretreated with Alboserpin and FXa at 50 nM for 4 h. ( B ) The fluorescence intensity of FITC-conjugated dextran leaking from the upper to the lower chambers was measured at different time points after treatment of HDMVECns with either FXa alone, Alboserpin, or Alboserpin along with FXa. Data from three independent experiments performed in duplicate are plotted. Error bars indicate SEM. ( C and D ) Schematic representation of the sequential steps of the Miles assay in the mouse and corresponding inoculations in different locations in skin biopsies. ( E ) Spectrophotometric analysis (610 nm) of vascular leaked formamide-extracted Evans blue dye content in the skin injected with 50 μM Alboserpin, FXa, and both FXa-Alboserpin at the same concentration. PBS was used as a negative control. * p < 0.05, *** p < 0.001, **** p < 0.0001. ns, not significant.

    Article Snippet: Polyclonal Abs against Alboserpin were raised in rabbits by Noble Life Sciences (Woodbine) using a standard protocol.

    Techniques: Permeability, Staining, Fluorescence, Injection, Concentration Assay, Negative Control

    During a mosquito bite, tissue injury causes the initiation of signaling through the extrinsic and intrinsic pathways that leads to the formation of FXa. FXa further converts prothrombin to thrombin, leading to clot formation. FXa triggers an inflammatory pathway in the endothelial cells by activating PAR receptors, ICAM and VCAM adhesion molecule expression, ERK1/2 signaling, NF-κB signaling, secretion of inflammatory cytokines, and disruption of endothelial cell barrier permeability. Mosquito A. albopictus salivary gland protein Alboserpin, a highly specific, strong inhibitor of FXa, prevents cleavage of PAR-2 by FXa, resulting in strong anti-inflammatory activity in vitro and in vivo.

    Journal: ImmunoHorizons

    Article Title: Alboserpin, the Main Salivary Anticoagulant from the Disease Vector Aedes albopictus , Displays Anti–FXa-PAR Signaling In Vitro and In Vivo

    doi: 10.4049/immunohorizons.2200045

    Figure Lengend Snippet: During a mosquito bite, tissue injury causes the initiation of signaling through the extrinsic and intrinsic pathways that leads to the formation of FXa. FXa further converts prothrombin to thrombin, leading to clot formation. FXa triggers an inflammatory pathway in the endothelial cells by activating PAR receptors, ICAM and VCAM adhesion molecule expression, ERK1/2 signaling, NF-κB signaling, secretion of inflammatory cytokines, and disruption of endothelial cell barrier permeability. Mosquito A. albopictus salivary gland protein Alboserpin, a highly specific, strong inhibitor of FXa, prevents cleavage of PAR-2 by FXa, resulting in strong anti-inflammatory activity in vitro and in vivo.

    Article Snippet: Polyclonal Abs against Alboserpin were raised in rabbits by Noble Life Sciences (Woodbine) using a standard protocol.

    Techniques: Expressing, Disruption, Permeability, Activity Assay, In Vitro, In Vivo