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Actinonin ((-)-Actinonin) is a naturally occurring antibacterial agent produced by Actinomyces. Actinonin inhibits aminopeptidase M, aminopeptidase N and leucine aminopeptidase. Actinonin is a potent reversible peptide deformylase (PDF) inhibitor with a Ki of 0.28 nM. Actinonin also inhibits MMP-1, MMP-3, MMP-8, MMP-9, and hmeprin α with Ki values of 300 nM, 1,700 nM, 190 nM, 330 nM, and 20 nM, respectively. Actinonin is an apoptosis inducer. Actinonin has antiproliferative and antitumor activities .
AtPep1 is a plant elicitor peptide. AtPep1 activates transcription of the defensive gene defensin(PDF1.2) and activates the synthesis of H2O2, which are components of the innate immune response against pathogens. AtPep1 can be isolated from extracts of Arabidopsis leaves .
Lanopepden (GSK 1322322) is a peptidyl peptidase (PDF) inhibitor. Lanopepden inhibits PDF activity, preventing bacterial protein synthesis, thereby exerting antibacterial activity. Lanopepden is primarily effective against Gram-positive bacteria. Lanopepden is used in the study of acute bacterial skin and skin structure infections .
LBM-415 (NVP-PDF 713) is a peptide deformylase (PDF) inhibitor that exhibits inhibitory activity against various antimicrobial-resistant gram-positive cocci, with a MIC90 range of 0.12-8 µg/ml. Additionally, inhibiting efflux pump activity can enhance bacterial sensitivity to LBM415, thereby improving its antibacterial efficacy .
(S,S)-TAPI-0 is a matrix metalloproteinase (MMP) inhibitor that inhibits the growth of Chlamydia trachomatis by inhibiting PDF enzyme activity. (S,S)-TAPI-0 can be used to study Chlamydia infection .
BB-3497 is a potent, orally active and selective peptide deformylase (PDF) inhibitor. BB-3497 is highly selective for PDF (IC50 = 7 nM for E. coliPDF.Ni) over the other mammalian metalloenzymes (MMP-1/2/3/7 and enkephalinase). BB-3497 exhibits potent activity against gram-positive bacteria and some gram-negative pathogens. BB-3497 protects mice from infection in systemic models of Staphylococeus aureus. BB-3497 can be used for anti-bacterial infection research .
AtPep1 TFA is an endogenous inducer of innate immune responses. AtPep1 TFA can be isolated from Arabidopsis thaliana leaves. AtPep1 TFA activates the transcription of defensin (PDF1.2), the expression of PROPEP1, the synthesis of hydrogen peroxide (H2O2) near leaf veins, and the alkalization of Arabidopsis suspension cell culture medium. AtPep1 TFA induces the expression of genes encoding defensins and PR-1. AtPep1 TFA is applicable to studies related to Pythium irregulare infection and pathogen infection .
BB-83698 is a peptide deformylase (PDF) inhibitor. BB-83698 exhibits potent in vitro activity against Streptococcus pneumoniae, with a minimum inhibitory concentration (MIC) range of 0.06-0.25μg/mL. BB-83698 elevates the survival rate of mice regardless of whether the infecting strain carries resistance mechanisms. BB-83698 can be used for the study of diseases related to drug-resistant Streptococcus pneumoniae infections .
PDF-IN-2 is a peptidyl deformylase (PDF) inhibitor. PDF-IN-2 has average IC50 values of 0.25, 0.50 and 0.34 nM, and average MIC values of 0.16, 0.33 and 0.25 μg/mL for Streptococcus pneumoniaePDF WT, G70V and G70D, respectively. PDF-IN-2 can be used in the research of infectious diseases .
Pdf Rat Pre-designed siRNA Set A contains three designed siRNAs for Pdf gene (Rat), as well as a negative control, a positive control, and a FAM-labeled negative control.
PDF Human Pre-designed siRNA Set A contains three designed siRNAs for PDF gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
Actinonin (Standard) is the analytical standard of Actinonin. This product is intended for research and analytical applications. Actinonin ((-)-Actinonin) is a naturally occurring antibacterial agent produced by Actinomyces. Actinonin inhibits aminopeptidase M, aminopeptidase N and leucine aminopeptidase. Actinonin is a potent reversible peptide deformylase (PDF) inhibitor with a Ki of 0.28 nM. Actinonin also inhibits MMP-1, MMP-3, MMP-8, MMP-9, and hmeprin α with Ki values of 300 nM, 1,700 nM, 190 nM, 330 nM, and 20 nM, respectively. Actinonin is an apoptosis inducer. Actinonin has antiproliferative and antitumor activities[1][2][3][4][5].
Lanopepden mesylate (GSK 1322322 mesylate) is a peptide deformase (PDF) inhibitor. Lanopepden mesylate has antibacterial activity by inhibiting the activity of PDF, preventing the correct synthesis of bacterial proteins. Lanopepden mesylate mainly targets Gram-positive bacteria. Lanopepden mesylate can be used in the study of acute bacterial skin and skin structural infections .
FR198248 is an anti-influenza agent and peptide deformylase (PDF) inhibitor. FR198248 can be isolated from Aspergillus flavipes. FR198248 potently inhibits the PDF of Staphylococcus aureus with an IC50 of 3.6 µM. FR198248 can be used for antiviral and antibacterial research .
Antibacterial agent 261 (compound 43) is a potent inhibitor of peptidomimetic peptide deformylase (PDF), with IC50 of 2.5 and 10.6 nM for S. aureus and E. coli, respectively .
GDF15 Human Pre-designed siRNA Set A contains three designed siRNAs for GDF15 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
Pdf Mouse Pre-designed siRNA Set A contains three designed siRNAs for Pdf gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control.
AtPep1 is a plant elicitor peptide. AtPep1 activates transcription of the defensive gene defensin(PDF1.2) and activates the synthesis of H2O2, which are components of the innate immune response against pathogens. AtPep1 can be isolated from extracts of Arabidopsis leaves .
AtPep1 TFA is an endogenous inducer of innate immune responses. AtPep1 TFA can be isolated from Arabidopsis thaliana leaves. AtPep1 TFA activates the transcription of defensin (PDF1.2), the expression of PROPEP1, the synthesis of hydrogen peroxide (H2O2) near leaf veins, and the alkalization of Arabidopsis suspension cell culture medium. AtPep1 TFA induces the expression of genes encoding defensins and PR-1. AtPep1 TFA is applicable to studies related to Pythium irregulare infection and pathogen infection .
Actinonin ((-)-Actinonin) is a naturally occurring antibacterial agent produced by Actinomyces. Actinonin inhibits aminopeptidase M, aminopeptidase N and leucine aminopeptidase. Actinonin is a potent reversible peptide deformylase (PDF) inhibitor with a Ki of 0.28 nM. Actinonin also inhibits MMP-1, MMP-3, MMP-8, MMP-9, and hmeprin α with Ki values of 300 nM, 1,700 nM, 190 nM, 330 nM, and 20 nM, respectively. Actinonin is an apoptosis inducer. Actinonin has antiproliferative and antitumor activities .
Actinonin (Standard) is the analytical standard of Actinonin. This product is intended for research and analytical applications. Actinonin ((-)-Actinonin) is a naturally occurring antibacterial agent produced by Actinomyces. Actinonin inhibits aminopeptidase M, aminopeptidase N and leucine aminopeptidase. Actinonin is a potent reversible peptide deformylase (PDF) inhibitor with a Ki of 0.28 nM. Actinonin also inhibits MMP-1, MMP-3, MMP-8, MMP-9, and hmeprin α with Ki values of 300 nM, 1,700 nM, 190 nM, 330 nM, and 20 nM, respectively. Actinonin is an apoptosis inducer. Actinonin has antiproliferative and antitumor activities[1][2][3][4][5].
FR198248 is an anti-influenza agent and peptide deformylase (PDF) inhibitor. FR198248 can be isolated from Aspergillus flavipes. FR198248 potently inhibits the PDF of Staphylococcus aureus with an IC50 of 3.6 µM. FR198248 can be used for antiviral and antibacterial research .
Peptide deformylase, a crucial enzyme in protein biosynthesis, catalyzes the removal of the formyl group from the N-terminal methionine of newly synthesized proteins. Displaying broad specificity at positions beyond the N-terminal L-methionine, the enzyme ensures proper maturation and functionality of proteins, emphasizing its essential contribution to the intricate process of protein synthesis and modification. Peptide deformylase Protein, S. aureus (P.pastoris, His) is the recombinant Staphylococcus aureus-derived Peptide deformylase protein, expressed by P. pastoris , with N-6*His labeled tag.
Peptide deformylase, a crucial enzyme in protein biosynthesis, catalyzes the removal of the formyl group from the N-terminal methionine of newly synthesized proteins. Displaying broad specificity at positions beyond the N-terminal L-methionine, the enzyme ensures proper maturation and functionality of proteins, emphasizing its essential contribution to the intricate process of protein synthesis and modification. Peptide deformylase Protein, S. aureus (His, SUMO) is the recombinant staphylococcus aureus-derived Peptide deformylase protein, expressed by E. coli, with SUMO and N-6*His labeled tag.
The GDF-15 protein regulates food intake, energy balance, and body weight by binding to its receptor GFRAL. This activates GFRAL-expressing neurons in the brainstem, triggering "emergency circuits" in the central parabrachial nucleus and amygdala during stress. GDF-15 Protein, Mouse (His) is the recombinant mouse-derived GDF-15 protein, expressed by E. coli, with N-His labeled tag.
Growth differentiation factor 15 (GDF-15) is a polypeptide hormone belonging to the transforming growth factor β (TGF-β) superfamily. GDF-15 is also known as non-steroidal anti-inflammatory drug activating Gene-1 (NAG-1), placental transforming growth factor-β (PTGFB), prostate-derived factor (PDF), and placental bone morphogenetic protein (PLAB). GDF-15 binds to glial cell-derived neurotrophic factor (GDNF) family receptor alpha-like protein (GFRAL) and is involved in aging, cancer, and metabolic processes. GFRAL-GDF15 does not affect SMAD activity and activates intracellular signals including RET, AKT, ERK1/2, and phospholipase C (PLCγ). GDF-15 Protein, Mouse (HEK293, hFc) has 115 amino acids expressed by HEK293 cells with N-terminal hFc tag.
Growth differentiation factor 15 (GDF-15) is a polypeptide hormone belonging to the transforming growth factor β (TGF-β) superfamily. GDF-15 is also known as non-steroidal anti-inflammatory drug activating Gene-1 (NAG-1), placental transforming growth factor-β (PTGFB), prostate-derived factor (PDF), and placental bone morphogenetic protein (PLAB). GDF-15 binds to glial cell-derived neurotrophic factor (GDNF) family receptor alpha-like protein (GFRAL) and is involved in aging, cancer, and metabolic processes. GFRAL-GDF15 does not affect SMAD activity and activates intracellular signals including RET, AKT, ERK1/2, and phospholipase C (PLCγ). GDF-15 Protein, Mouse (HEK293, Fc) has 115 amino acids expressed by HEK293 cells with N-terminal hFc tag and Fc co-transfection.
Growth differentiation factor 15 (GDF-15) is a polypeptide hormone belonging to the transforming growth factor β (TGF-β) superfamily. GDF-15 is also known as non-steroidal anti-inflammatory drug activating Gene-1 (NAG-1), placental transforming growth factor-β (PTGFB), prostate-derived factor (PDF), and placental bone morphogenetic protein (PLAB). GDF-15 binds to glial cell-derived neurotrophic factor (GDNF) family receptor alpha-like protein (GFRAL) and is involved in aging, cancer, and metabolic processes. GFRAL-GDF15 does not affect SMAD activity and activates intracellular signals including RET, AKT, ERK1/2, and phospholipase C (PLCγ). GDF-15 Protein, Cynomolgus (HEK293, Fc) has 112 amino acids expressed by HEK293 cells with N-terminal hFc tag.
Growth differentiation factor 15 (GDF-15) is a polypeptide hormone belonging to the transforming growth factor β (TGF-β) superfamily. GDF-15 is also known as non-steroidal anti-inflammatory drug activating Gene-1 (NAG-1), placental transforming growth factor-β (PTGFB), prostate-derived factor (PDF), and placental bone morphogenetic protein (PLAB). GDF-15 binds to glial cell-derived neurotrophic factor (GDNF) family receptor alpha-like protein (GFRAL) and is involved in aging, cancer, and metabolic processes. GFRAL-GDF15 does not affect SMAD activity and activates intracellular signals including RET, AKT, ERK1/2, and phospholipase C (PLCγ). GDF-15 Protein, Cynomolgus (Biotinylated, HEK293, Fc) has 112 amino acids expressed by HEK293 cells with N-terminal hFc tag.
Growth differentiation factor 15 (GDF-15) is a polypeptide hormone belonging to the transforming growth factor β (TGF-β) superfamily. GDF-15 is also known as non-steroidal anti-inflammatory drug activating Gene-1 (NAG-1), placental transforming growth factor-β (PTGFB), prostate-derived factor (PDF), and placental bone morphogenetic protein (PLAB). GDF-15 binds to glial cell-derived neurotrophic factor (GDNF) family receptor alpha-like protein (GFRAL) and is involved in aging, cancer, and metabolic processes. GFRAL-GDF15 does not affect SMAD activity and activates intracellular signals including RET, AKT, ERK1/2, and phospholipase C (PLCγ). GDF-15 Protein, Mouse (Biotinylated, HEK293, Fc) has 115 amino acids expressed by HEK293 cells with N-terminal hFc tag.
GDF-15 protein is an important member of the TGF-β family and plays a crucial role in cell growth, differentiation and immune regulation. His research has enhanced our understanding of the signaling pathways associated with the TGF-β superfamily and provided insights into its unique contribution to cellular homeostasis. GDF-15 Protein, Canine (His) is the recombinant canine-derived GDF-15 protein, expressed by E. coli , with N-His labeled tag.
The GDF-15 protein regulates food intake, energy expenditure, and body weight in response to metabolic and toxin-induced stress. Binds to its receptor GFRAL and activates GFRAL-expressing neurons in the brainstem, triggering the "stress response circuit." GDF-15 Protein, Rat (His) is the recombinant rat-derived GDF-15 protein, expressed by E. coli , with N-His labeled tag.
GDF-15 Protein, a key regulator of food intake and energy balance, binds to its receptor GFRAL, activating neurons in the brainstem and forming an 'emergency circuit' for feeding responses during stress. Additionally, GDF-15 inhibits growth hormone signaling on hepatocytes, existing as a disulfide-linked homodimer. Interacting with GFRAL, it acts as a ligand, mediating GDF15 internalization and cellular signaling through RET. GDF-15 Protein, Cynomolgus (His) is the recombinant cynomolgus-derived GDF-15 protein, expressed by E. coli , with N-His labeled tag.
Growth differentiation factor 15 (GDF-15) is a polypeptide hormone belonging to the transforming growth factor β (TGF-β) superfamily. GDF-15 is also known as non-steroidal anti-inflammatory drug activating Gene-1 (NAG-1), placental transforming growth factor-β (PTGFB), prostate-derived factor (PDF), and placental bone morphogenetic protein (PLAB). GDF-15 binds to glial cell-derived neurotrophic factor (GDNF) family receptor alpha-like protein (GFRAL) and is involved in aging, cancer, and metabolic processes. GFRAL-GDF15 does not affect SMAD activity and activates intracellular signals including RET, AKT, ERK1/2, and phospholipase C (PLCγ). GDF-15 Protein, Human (Biotinylated, HEK293, Fc) has 112 amino acids expressed by HEK293 cells with N-terminal hFc tag.
The GDF-15 protein is critical for regulating food intake, energy expenditure, and body weight in response to metabolic and toxin-induced stress. It binds to its receptor GFRAL and activates GFRAL-expressing neurons in the brainstem. GDF-15 Protein, Human (Biotinylated, His-Avi) is the recombinant human-derived GDF-15 protein, expressed by E. coli , with C-Avi, N-His labeled tag.
Pdf Rat Pre-designed siRNA Set A contains three designed siRNAs for Pdf gene (Rat), as well as a negative control, a positive control, and a FAM-labeled negative control.
PDF Human Pre-designed siRNA Set A contains three designed siRNAs for PDF gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
GDF15 Human Pre-designed siRNA Set A contains three designed siRNAs for GDF15 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
Pdf Mouse Pre-designed siRNA Set A contains three designed siRNAs for Pdf gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control.
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Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
MedchemExpress Validation 03
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
MedchemExpress Validation 04
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
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