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Bio-Rad pbs t
Antigen screening using multi-antigen print immunoassay. Staining of antigen printed onto nitrocellulose by sera from 5 negative controls (Danish participants, no known TB exposure of TB risk factors) and 19 patients with confirmed TB, recruited from Danish hospitals. The nitrocellulose strips were incubated with sera diluted 1/50 in 1% non-fat skim milk in <t>PBS-T.</t>
Pbs T, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 99 stars, based on 75 article reviews
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pbs t - by Bioz Stars, 2020-07
99/100 stars

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1) Product Images from "Development of a proof of concept immunochromatographic lateral flow assay for point of care diagnosis of Mycobacterium tuberculosis"

Article Title: Development of a proof of concept immunochromatographic lateral flow assay for point of care diagnosis of Mycobacterium tuberculosis

Journal: BMC Research Notes

doi: 10.1186/1756-0500-6-202

Antigen screening using multi-antigen print immunoassay. Staining of antigen printed onto nitrocellulose by sera from 5 negative controls (Danish participants, no known TB exposure of TB risk factors) and 19 patients with confirmed TB, recruited from Danish hospitals. The nitrocellulose strips were incubated with sera diluted 1/50 in 1% non-fat skim milk in PBS-T.
Figure Legend Snippet: Antigen screening using multi-antigen print immunoassay. Staining of antigen printed onto nitrocellulose by sera from 5 negative controls (Danish participants, no known TB exposure of TB risk factors) and 19 patients with confirmed TB, recruited from Danish hospitals. The nitrocellulose strips were incubated with sera diluted 1/50 in 1% non-fat skim milk in PBS-T.

Techniques Used: Staining, Incubation

2) Product Images from "Arginine-Specific Mono ADP-Ribosylation In Vitro of Antimicrobial Peptides by ADP-Ribosylating Toxins"

Article Title: Arginine-Specific Mono ADP-Ribosylation In Vitro of Antimicrobial Peptides by ADP-Ribosylating Toxins

Journal: PLoS ONE

doi: 10.1371/journal.pone.0041417

Modification of HNP-1 by selected ADP-ribosyltransferases. ( A ) HNP-1 is ADP-ribosylated by CTA and LTA but only weakly by NarE. HNP-1 (3 µg, 43.56 µM) was incubated with CTA (2.5 U), LTA (8.9 U) or NarE (2 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate buffer, pH 7.5, at 30°C for 1 h (Toxin). The same reactions were performed with heat-inactivated toxins (HI-Toxin), in the presence of 2 mM NAD (Toxin + NAD), or 2 mM ADP-ribose (Toxin + ADP-ribose). The ADP-ribosylated peptides were resolved by SDS-PAGE in a 10% NuPAGE gel, using MES as running buffer and transferred to nitrocellulose. After blocking with 5% BSA in PBS containing 0.05% Tween-20 (PBS-T) for 1 h, the blot was incubated with streptavidin-HRP conjugated (1∶10000 dilution) for 1 h at RT in the same buffer. The biotin-ADP-ribose labeled bands were visualized by chemiluminescence. ( B ) ART1 ADP-ribosylated HNP-1. HNP-1 (3 µg, 43.56 µM) was incubated with ART1 (6.8 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate, pH 7.5 at 30°C for 1 h (ART1). A control reaction with heat-inactivated ART1 is also shown (HI-ART1). ( C ) SDS-PAGE analysis of the purification grade of 2 µg each of CTA, LTA and NarE. ( D ) HNP-1 is ADP-ribosylated in a dose and response dependent manner by CTA and LTA. HNP-1 at the concentration shown in the Figure was incubated with CTA (2.5 U), or LTA (8.9 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate buffer, pH 7.5, at 30°C for 1 h. ( E ) HNP-1 is ADP-ribosylated in time dependent fashion. HNP-1 (3 µg) was incubated with CTA (1.25 U) or LTA (4.45 U) using the same conditions above described for the times of incubation indicated in the Figure. Molecular markers are on the left. Data shown are representative of several experiments performed in the same conditions.
Figure Legend Snippet: Modification of HNP-1 by selected ADP-ribosyltransferases. ( A ) HNP-1 is ADP-ribosylated by CTA and LTA but only weakly by NarE. HNP-1 (3 µg, 43.56 µM) was incubated with CTA (2.5 U), LTA (8.9 U) or NarE (2 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate buffer, pH 7.5, at 30°C for 1 h (Toxin). The same reactions were performed with heat-inactivated toxins (HI-Toxin), in the presence of 2 mM NAD (Toxin + NAD), or 2 mM ADP-ribose (Toxin + ADP-ribose). The ADP-ribosylated peptides were resolved by SDS-PAGE in a 10% NuPAGE gel, using MES as running buffer and transferred to nitrocellulose. After blocking with 5% BSA in PBS containing 0.05% Tween-20 (PBS-T) for 1 h, the blot was incubated with streptavidin-HRP conjugated (1∶10000 dilution) for 1 h at RT in the same buffer. The biotin-ADP-ribose labeled bands were visualized by chemiluminescence. ( B ) ART1 ADP-ribosylated HNP-1. HNP-1 (3 µg, 43.56 µM) was incubated with ART1 (6.8 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate, pH 7.5 at 30°C for 1 h (ART1). A control reaction with heat-inactivated ART1 is also shown (HI-ART1). ( C ) SDS-PAGE analysis of the purification grade of 2 µg each of CTA, LTA and NarE. ( D ) HNP-1 is ADP-ribosylated in a dose and response dependent manner by CTA and LTA. HNP-1 at the concentration shown in the Figure was incubated with CTA (2.5 U), or LTA (8.9 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate buffer, pH 7.5, at 30°C for 1 h. ( E ) HNP-1 is ADP-ribosylated in time dependent fashion. HNP-1 (3 µg) was incubated with CTA (1.25 U) or LTA (4.45 U) using the same conditions above described for the times of incubation indicated in the Figure. Molecular markers are on the left. Data shown are representative of several experiments performed in the same conditions.

Techniques Used: Modification, Incubation, TNKS1 Histone Ribosylation Assay, SDS Page, Blocking Assay, Labeling, Purification, Concentration Assay

Related Articles

Electrophoresis:

Article Title: A fractionation method to identify qauntitative changes in protein expression mediated by IGF-1 on the proteome of murine C2C12 myoblasts
Article Snippet: .. Two-dimensional electrophoresis Samples containing 75–200 μg of fractionated cytoplasmic proteins were diluted in 2D electrophoresis buffer (2 M thiourea, 5 M urea, 0.25% CHAPS, 0.25% Tween-20, 0.25% SB-3, 10% isopropanol, and 12.5% water-saturated butanol) containing 15 mg DTT and 0.5% ampholytes (pI ranges 3–10 or 5–8; Bio-Rad; Hercules, CA) to a final volume of 0.2 ml, and passively absorbed onto immobilized pH gradient strips (pI ranges 5–8 or 3–10 NL (non-linear); Bio-Rad) for 4 hours at 20°C followed by active rehydration (50 V at 20°C) for 8 hours. .. Isoelectric focusing was performed for 35,000 V-h on a Protean IEF System (Bio-Rad), electrophoresis with the Criterion gel system (Bio-Rad).

Incubation:

Article Title: In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae
Article Snippet: .. Membranes were incubated with polyclonal antisera against EpsG (1:150,000 in Tris-buffered saline with 0.1% Tween-20) or EpsL (1:40,000 in Tris buffered saline with 0.1% Tween-20), followed by horseradish peroxidase-conjugated goat anti-rabbit immunoglobulin G (BioRad) diluted 1:15,000 in Tris-buffered saline containing 0.1% Tween-20. .. Blots were developed with ECL Plus Western blotting detection reagent (GE Healthcare) and protein was visualized using a Typhoon Trio variable mode imager system and Image Quant software.

Article Title: Regulatory landscape of AGE-RAGE-oxidative stress axis and its modulation by PPARγ activation in high fructose diet-induced metabolic syndrome
Article Snippet: .. The blots were incubated in immunoblotting buffer (TBST: 20 mM Tris-HCl, pH 7.4, 0.15 M NaCl, 0.05% Tween-20) (Bio-Rad) containing 5% (w/v) Skim Milk Powder at room temperature, followed by washing with TBST. .. Blots were then incubated overnight at 4 °C with either anti-CML antibodies (1:800) in TBST containing 5% milk, or Anti-HNE polyclonal antibody (1:800) or anti-RAGE antibodies (1:400) both in TBST containing 3% milk.

other:

Article Title: Crystal Structures of Major Envelope Proteins VP26 and VP28 from White Spot Syndrome Virus Shed Light on Their Evolutionary Relationship ▿
Article Snippet: Nevertheless, when treated with Tween 20, VP26 may become accessible.

Article Title: Crystal Structures of Major Envelope Proteins VP26 and VP28 from White Spot Syndrome Virus Shed Light on Their Evolutionary Relationship ▿
Article Snippet: To clarify the location of VP26 in the virion, virus treatment with Tween 20 gave a mixture of partial and complete separation of the viral envelope from the nucleocapsid to reveal the location of the bound gold particles.

Labeling:

Article Title: Crystal Structures of Major Envelope Proteins VP26 and VP28 from White Spot Syndrome Virus Shed Light on Their Evolutionary Relationship ▿
Article Snippet: .. Our result showed that 0.1% Tween 20 could gently separate the envelope from the nucleocapsid, but 0.1% Triton X-100 was too harsh, resulting in a complete loss of envelope during subsequent steps of immunogold labeling (data not shown). .. More interestingly, surface protrusions were visible in the outer surface of the envelope after the Tween 20 treatment, possibly indicating that as the envelope structure becomes loosely packed, some inner structures and binding sites for both VP26 and VP28 are well exposed, giving high labeling efficiency.

Two-Dimensional Gel Electrophoresis:

Article Title: A fractionation method to identify qauntitative changes in protein expression mediated by IGF-1 on the proteome of murine C2C12 myoblasts
Article Snippet: .. Two-dimensional electrophoresis Samples containing 75–200 μg of fractionated cytoplasmic proteins were diluted in 2D electrophoresis buffer (2 M thiourea, 5 M urea, 0.25% CHAPS, 0.25% Tween-20, 0.25% SB-3, 10% isopropanol, and 12.5% water-saturated butanol) containing 15 mg DTT and 0.5% ampholytes (pI ranges 3–10 or 5–8; Bio-Rad; Hercules, CA) to a final volume of 0.2 ml, and passively absorbed onto immobilized pH gradient strips (pI ranges 5–8 or 3–10 NL (non-linear); Bio-Rad) for 4 hours at 20°C followed by active rehydration (50 V at 20°C) for 8 hours. .. Isoelectric focusing was performed for 35,000 V-h on a Protean IEF System (Bio-Rad), electrophoresis with the Criterion gel system (Bio-Rad).

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    Bio-Rad pbs t
    Antigen screening using multi-antigen print immunoassay. Staining of antigen printed onto nitrocellulose by sera from 5 negative controls (Danish participants, no known TB exposure of TB risk factors) and 19 patients with confirmed TB, recruited from Danish hospitals. The nitrocellulose strips were incubated with sera diluted 1/50 in 1% non-fat skim milk in <t>PBS-T.</t>
    Pbs T, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 90 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbs t/product/Bio-Rad
    Average 93 stars, based on 90 article reviews
    Price from $9.99 to $1999.99
    pbs t - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

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    Antigen screening using multi-antigen print immunoassay. Staining of antigen printed onto nitrocellulose by sera from 5 negative controls (Danish participants, no known TB exposure of TB risk factors) and 19 patients with confirmed TB, recruited from Danish hospitals. The nitrocellulose strips were incubated with sera diluted 1/50 in 1% non-fat skim milk in PBS-T.

    Journal: BMC Research Notes

    Article Title: Development of a proof of concept immunochromatographic lateral flow assay for point of care diagnosis of Mycobacterium tuberculosis

    doi: 10.1186/1756-0500-6-202

    Figure Lengend Snippet: Antigen screening using multi-antigen print immunoassay. Staining of antigen printed onto nitrocellulose by sera from 5 negative controls (Danish participants, no known TB exposure of TB risk factors) and 19 patients with confirmed TB, recruited from Danish hospitals. The nitrocellulose strips were incubated with sera diluted 1/50 in 1% non-fat skim milk in PBS-T.

    Article Snippet: The plates were washed with PBS-T and enzyme activity was assayed by incubation for 30 min at room temperature with 100 μl of tetramethylbenzidine peroxidase substrate (Bio-Rad, Hercules, Calif.) per well.

    Techniques: Staining, Incubation

    Modification of HNP-1 by selected ADP-ribosyltransferases. ( A ) HNP-1 is ADP-ribosylated by CTA and LTA but only weakly by NarE. HNP-1 (3 µg, 43.56 µM) was incubated with CTA (2.5 U), LTA (8.9 U) or NarE (2 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate buffer, pH 7.5, at 30°C for 1 h (Toxin). The same reactions were performed with heat-inactivated toxins (HI-Toxin), in the presence of 2 mM NAD (Toxin + NAD), or 2 mM ADP-ribose (Toxin + ADP-ribose). The ADP-ribosylated peptides were resolved by SDS-PAGE in a 10% NuPAGE gel, using MES as running buffer and transferred to nitrocellulose. After blocking with 5% BSA in PBS containing 0.05% Tween-20 (PBS-T) for 1 h, the blot was incubated with streptavidin-HRP conjugated (1∶10000 dilution) for 1 h at RT in the same buffer. The biotin-ADP-ribose labeled bands were visualized by chemiluminescence. ( B ) ART1 ADP-ribosylated HNP-1. HNP-1 (3 µg, 43.56 µM) was incubated with ART1 (6.8 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate, pH 7.5 at 30°C for 1 h (ART1). A control reaction with heat-inactivated ART1 is also shown (HI-ART1). ( C ) SDS-PAGE analysis of the purification grade of 2 µg each of CTA, LTA and NarE. ( D ) HNP-1 is ADP-ribosylated in a dose and response dependent manner by CTA and LTA. HNP-1 at the concentration shown in the Figure was incubated with CTA (2.5 U), or LTA (8.9 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate buffer, pH 7.5, at 30°C for 1 h. ( E ) HNP-1 is ADP-ribosylated in time dependent fashion. HNP-1 (3 µg) was incubated with CTA (1.25 U) or LTA (4.45 U) using the same conditions above described for the times of incubation indicated in the Figure. Molecular markers are on the left. Data shown are representative of several experiments performed in the same conditions.

    Journal: PLoS ONE

    Article Title: Arginine-Specific Mono ADP-Ribosylation In Vitro of Antimicrobial Peptides by ADP-Ribosylating Toxins

    doi: 10.1371/journal.pone.0041417

    Figure Lengend Snippet: Modification of HNP-1 by selected ADP-ribosyltransferases. ( A ) HNP-1 is ADP-ribosylated by CTA and LTA but only weakly by NarE. HNP-1 (3 µg, 43.56 µM) was incubated with CTA (2.5 U), LTA (8.9 U) or NarE (2 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate buffer, pH 7.5, at 30°C for 1 h (Toxin). The same reactions were performed with heat-inactivated toxins (HI-Toxin), in the presence of 2 mM NAD (Toxin + NAD), or 2 mM ADP-ribose (Toxin + ADP-ribose). The ADP-ribosylated peptides were resolved by SDS-PAGE in a 10% NuPAGE gel, using MES as running buffer and transferred to nitrocellulose. After blocking with 5% BSA in PBS containing 0.05% Tween-20 (PBS-T) for 1 h, the blot was incubated with streptavidin-HRP conjugated (1∶10000 dilution) for 1 h at RT in the same buffer. The biotin-ADP-ribose labeled bands were visualized by chemiluminescence. ( B ) ART1 ADP-ribosylated HNP-1. HNP-1 (3 µg, 43.56 µM) was incubated with ART1 (6.8 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate, pH 7.5 at 30°C for 1 h (ART1). A control reaction with heat-inactivated ART1 is also shown (HI-ART1). ( C ) SDS-PAGE analysis of the purification grade of 2 µg each of CTA, LTA and NarE. ( D ) HNP-1 is ADP-ribosylated in a dose and response dependent manner by CTA and LTA. HNP-1 at the concentration shown in the Figure was incubated with CTA (2.5 U), or LTA (8.9 U) and 10 µM of biotin-NAD in 50 mM potassium phosphate buffer, pH 7.5, at 30°C for 1 h. ( E ) HNP-1 is ADP-ribosylated in time dependent fashion. HNP-1 (3 µg) was incubated with CTA (1.25 U) or LTA (4.45 U) using the same conditions above described for the times of incubation indicated in the Figure. Molecular markers are on the left. Data shown are representative of several experiments performed in the same conditions.

    Article Snippet: After several washings with PBS-T, bound streptavidin was detected using an ECL immunoblotting detection system (Bio-Rad) according to the manufacturer's instructions.

    Techniques: Modification, Incubation, TNKS1 Histone Ribosylation Assay, SDS Page, Blocking Assay, Labeling, Purification, Concentration Assay

    Combination of MVA-CD40L and tumor-targeting antibodies enhances tumor growth control. a – d Enhanced tumor growth control when rMVA-CD40L immunization is combined with tumor-targeting antibodies. a , b B16.OVA tumor-bearing mice received PBS or were immunized with 5 × 10 7 TCID 50 of rMVA-CD40L (Day 0). Mice received 200 µg of either IgG2a or anti-TRP-1 antibody i.p. at days −2, 2, 6, and 10. a Tumor size follow-up ( n = 5 mice/group) and b overall survival. c , d Balb/c mice bearing 85–100 mm 3 CT26.HER2 received PBS or were immunized with 5 × 10 7 TCID 50 of MVA-HER2-CD40L (Day 0). Mice received 5 µg of either IgG1 or anti-HER2 antibody i.p. at days –2, 1, and 4. c Tumor size follow-up ( n = 5 mice/group) and d overall survival. Data in a and c are expressed as mean ± SEM, representative of at least two independent experiments. One-way ANOVA was performed on a . Log-rank test on mouse survival was performed for b . * p

    Journal: Nature Communications

    Article Title: Synergistic cancer immunotherapy combines MVA-CD40L induced innate and adaptive immunity with tumor targeting antibodies

    doi: 10.1038/s41467-019-12998-6

    Figure Lengend Snippet: Combination of MVA-CD40L and tumor-targeting antibodies enhances tumor growth control. a – d Enhanced tumor growth control when rMVA-CD40L immunization is combined with tumor-targeting antibodies. a , b B16.OVA tumor-bearing mice received PBS or were immunized with 5 × 10 7 TCID 50 of rMVA-CD40L (Day 0). Mice received 200 µg of either IgG2a or anti-TRP-1 antibody i.p. at days −2, 2, 6, and 10. a Tumor size follow-up ( n = 5 mice/group) and b overall survival. c , d Balb/c mice bearing 85–100 mm 3 CT26.HER2 received PBS or were immunized with 5 × 10 7 TCID 50 of MVA-HER2-CD40L (Day 0). Mice received 5 µg of either IgG1 or anti-HER2 antibody i.p. at days –2, 1, and 4. c Tumor size follow-up ( n = 5 mice/group) and d overall survival. Data in a and c are expressed as mean ± SEM, representative of at least two independent experiments. One-way ANOVA was performed on a . Log-rank test on mouse survival was performed for b . * p

    Article Snippet: Sera were diluted to 1:5000 in blocking buffer and incubated for 2 h at RT, then washed in T-PBS again, and sheep anti-mouse IgG H + L HRP conjugate (BioRad) diluted 1:10,000 in PBS + 1% bovine serum albumin was added to the plate for 2 h at RT.

    Techniques: Mouse Assay

    Role of CD8 + T cells during rMVA-CD40L-induced tumor growth control. a , b CD8 depletion in B16.OVA tumor-bearing mice. When B16.OVA tumors were above 50 mm 3 , mice received PBS or were immunized with 5 × 10 7 TCID 50 of either rMVA or rMVA-CD40L. Where indicated, mice received at days −2, 2, 6, and 10 after immunization 200 µg of either IgG2b or anti-CD8 antibody i.p. a Tumor size follow-up ( n = 5 mice/group) and b overall survival. a Representative growth of PBS and rMVA-CD40L-treated groups in at least two independent experiments. b Represents overall survival of one independent experiment. Data in a expressed as mean ± SEM. c – f C57BL/6 mice bearing 50 mm 3 B16.OVA tumors ( n = 5 mice/group) received PBS or were immunized with 5 × 10 7 TCID 50 of either rMVA, rMVA-CD40L, or rMVA-Profilin. c Quantitative expression of IL12p70 and IFN-γ in sera 6 h after systemic immunization. d Percentage of CD44 + OVA 257-264 -specific CD8 + T cells among peripheral blood leukocytes (PBL) 7 days after immunization. e Tumor size follow-up. f Overall survival. c – e Data representative of two independent experiments. f Survival of two merged independent experiments. Data in a , c , d , and e are expressed as mean ± SEM. One-way ANOVA was performed on figures a , c , d , and e . Log-rank test on mouse survival was performed for b and f . NS, nonsignificant; * p

    Journal: Nature Communications

    Article Title: Synergistic cancer immunotherapy combines MVA-CD40L induced innate and adaptive immunity with tumor targeting antibodies

    doi: 10.1038/s41467-019-12998-6

    Figure Lengend Snippet: Role of CD8 + T cells during rMVA-CD40L-induced tumor growth control. a , b CD8 depletion in B16.OVA tumor-bearing mice. When B16.OVA tumors were above 50 mm 3 , mice received PBS or were immunized with 5 × 10 7 TCID 50 of either rMVA or rMVA-CD40L. Where indicated, mice received at days −2, 2, 6, and 10 after immunization 200 µg of either IgG2b or anti-CD8 antibody i.p. a Tumor size follow-up ( n = 5 mice/group) and b overall survival. a Representative growth of PBS and rMVA-CD40L-treated groups in at least two independent experiments. b Represents overall survival of one independent experiment. Data in a expressed as mean ± SEM. c – f C57BL/6 mice bearing 50 mm 3 B16.OVA tumors ( n = 5 mice/group) received PBS or were immunized with 5 × 10 7 TCID 50 of either rMVA, rMVA-CD40L, or rMVA-Profilin. c Quantitative expression of IL12p70 and IFN-γ in sera 6 h after systemic immunization. d Percentage of CD44 + OVA 257-264 -specific CD8 + T cells among peripheral blood leukocytes (PBL) 7 days after immunization. e Tumor size follow-up. f Overall survival. c – e Data representative of two independent experiments. f Survival of two merged independent experiments. Data in a , c , d , and e are expressed as mean ± SEM. One-way ANOVA was performed on figures a , c , d , and e . Log-rank test on mouse survival was performed for b and f . NS, nonsignificant; * p

    Article Snippet: Sera were diluted to 1:5000 in blocking buffer and incubated for 2 h at RT, then washed in T-PBS again, and sheep anti-mouse IgG H + L HRP conjugate (BioRad) diluted 1:10,000 in PBS + 1% bovine serum albumin was added to the plate for 2 h at RT.

    Techniques: Mouse Assay, Expressing