Review

asah2 recombinant protein (MedChemExpress)

MedChemExpress is a verified supplier

MedChemExpress manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

MedChemExpress asah2 recombinant protein

Fut2 deficiency in ISCs resulted in impairment of α1,2-fucosylation of mitochondrial-function-related proteins. (A) Volcano plot of differently expressed N-glycosylated proteins and sites in Fut2 knockout ISCs compared to WT. (B) Fold change of protein level and N-glycosylation level of mitochondrial-function-related proteins <t>Asah2,</t> Npc1, and Bsg. (C) IHC analysis of Asah2 in ileal sections of WT and Fut2 ΔISC mice. Scale bar, 100 μm. (D) The protein level of Npc1, Asah2, and Bsg in whole-cell lysate and UEA-I-enriched proteins of WT and Fut2 ΔISC ISCs. (E) Protein expression of mTOR and p-mTOR in WT and Fut2 ΔISC crypts. * P < 0.05, ** P < 0.01, and *** P < 0.001. ns, no significant.

Asah2 Recombinant Protein, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/asah2+recombinant+protein/BST2%2C+Human/pmc10976588-211-3-6
Average 93 stars, based on 4 article reviews

asah2 recombinant protein - by Bioz Stars, 2026-10

93/100 stars

Images

1) Product Images from "Fut2 Deficiency Promotes Intestinal Stem Cell Aging by Damaging Mitochondrial Functions via Down-Regulating α1,2-Fucosylation of Asah2 and Npc1"

Article Title: Fut2 Deficiency Promotes Intestinal Stem Cell Aging by Damaging Mitochondrial Functions via Down-Regulating α1,2-Fucosylation of Asah2 and Npc1

Journal: Research

doi: 10.34133/research.0343

Figure Legend Snippet: Fut2 deficiency in ISCs resulted in impairment of α1,2-fucosylation of mitochondrial-function-related proteins. (A) Volcano plot of differently expressed N-glycosylated proteins and sites in Fut2 knockout ISCs compared to WT. (B) Fold change of protein level and N-glycosylation level of mitochondrial-function-related proteins Asah2, Npc1, and Bsg. (C) IHC analysis of Asah2 in ileal sections of WT and Fut2 ΔISC mice. Scale bar, 100 μm. (D) The protein level of Npc1, Asah2, and Bsg in whole-cell lysate and UEA-I-enriched proteins of WT and Fut2 ΔISC ISCs. (E) Protein expression of mTOR and p-mTOR in WT and Fut2 ΔISC crypts. * P < 0.05, ** P < 0.01, and *** P < 0.001. ns, no significant.

Techniques Used: Knock-Out, Glycoproteomics, Expressing

$Loss of α1,2-fucosylation of Asah2 and Npc1 induced stemness impairment and mitochondrial dysfunction in ISCs. (A) The protein level of Npc1, Asah2, and Bsg in whole-cell lysate and UEA-I-enriched proteins of WT and corresponding SDM organoids. (B) Images of WT, Asah2-N444Q, and Npc1-N961Q organoids and IF analysis of EGFP-labeled ISCs. Scale bars, 100 μm. (C) EdU assays in WT, Asah2-N444Q, and Npc1-N961Q organoids. Scale bar, 100 μm. (D) qPCR results of stemness markers in WT, Asah2-N444Q, and Npc1-N961Q organoids. (E to G) SA-β-gal staining of senescent cells, MitoSOX-indicated mtROS, and JC-1-indicated MMP analysis in WT, Asah2-N444Q, and Npc1-N961Q organoids. Scale bars, 100 μm. (H) Activity assays of respiratory complexes I, III, IV, and V in WT and Asah2-N444Q organoids. (I) Protein expression of mTOR and p-mTOR in WT and Npc1-N961Q organoids. (J) Expression of mitochondrial and mitophagy proteins in the whole-cell lysate of WT and Npc1-N961Q organoids. CCCP was used to activate mitophagy. (K) Expression of mitochondrial and mitophagy proteins in lysosome fractions of WT and Npc1-N961Q organoids. * P < 0.05 and ** P < 0.01.$
Figure Legend Snippet: Loss of α1,2-fucosylation of Asah2 and Npc1 induced stemness impairment and mitochondrial dysfunction in ISCs. (A) The protein level of Npc1, Asah2, and Bsg in whole-cell lysate and UEA-I-enriched proteins of WT and corresponding SDM organoids. (B) Images of WT, Asah2-N444Q, and Npc1-N961Q organoids and IF analysis of EGFP-labeled ISCs. Scale bars, 100 μm. (C) EdU assays in WT, Asah2-N444Q, and Npc1-N961Q organoids. Scale bar, 100 μm. (D) qPCR results of stemness markers in WT, Asah2-N444Q, and Npc1-N961Q organoids. (E to G) SA-β-gal staining of senescent cells, MitoSOX-indicated mtROS, and JC-1-indicated MMP analysis in WT, Asah2-N444Q, and Npc1-N961Q organoids. Scale bars, 100 μm. (H) Activity assays of respiratory complexes I, III, IV, and V in WT and Asah2-N444Q organoids. (I) Protein expression of mTOR and p-mTOR in WT and Npc1-N961Q organoids. (J) Expression of mitochondrial and mitophagy proteins in the whole-cell lysate of WT and Npc1-N961Q organoids. CCCP was used to activate mitophagy. (K) Expression of mitochondrial and mitophagy proteins in lysosome fractions of WT and Npc1-N961Q organoids. * P < 0.05 and ** P < 0.01.

Techniques Used: Labeling, Staining, Activity Assay, Expressing

$Asah2 supplement and mTOR inhibition ameliorated stemness impairment and mitochondrial dysfunction in Fut2 ΔISC organoids. (A) Development of organoids derived from WT and Fut2 ΔISC mice, with or without Asah2 and Torin1 treatment. Scale bar, 100 μm. (B) Statistical analysis of surface areas and budding number of organoids. (C and D) IF analysis of EGFP and EdU in WT and Fut2 ΔISC organoids, with or without Asah2 and Torin1 treatment. Scale bars, 100 μm. (E and F) JC-1-indicated MMP and MitoSOX-indicated mtROS analysis in WT and Fut2 ΔISC organoids, with or without Asah2 and Torin1 treatment. Scale bars, 100 μm. (G) Activity of complexes I, III. IV, and V in WT, Fut2 ΔISC, and Fut2 ΔISC + Asah2 organoids. (H) Expression of mitochondrial and mitophagy proteins in whole-cell lysate of Fut2 ΔISC and Fut2 ΔISC + Torin1 organoids. CCCP was used to activate mitophagy. (I) Expression of mitochondrial and mitophagy proteins in lysosome fractions of Fut2 ΔISC and Fut2 ΔISC + Torin1 organoids. * P < 0.05, ** P < 0.01, and *** P < 0.001.$
Figure Legend Snippet: Asah2 supplement and mTOR inhibition ameliorated stemness impairment and mitochondrial dysfunction in Fut2 ΔISC organoids. (A) Development of organoids derived from WT and Fut2 ΔISC mice, with or without Asah2 and Torin1 treatment. Scale bar, 100 μm. (B) Statistical analysis of surface areas and budding number of organoids. (C and D) IF analysis of EGFP and EdU in WT and Fut2 ΔISC organoids, with or without Asah2 and Torin1 treatment. Scale bars, 100 μm. (E and F) JC-1-indicated MMP and MitoSOX-indicated mtROS analysis in WT and Fut2 ΔISC organoids, with or without Asah2 and Torin1 treatment. Scale bars, 100 μm. (G) Activity of complexes I, III. IV, and V in WT, Fut2 ΔISC, and Fut2 ΔISC + Asah2 organoids. (H) Expression of mitochondrial and mitophagy proteins in whole-cell lysate of Fut2 ΔISC and Fut2 ΔISC + Torin1 organoids. CCCP was used to activate mitophagy. (I) Expression of mitochondrial and mitophagy proteins in lysosome fractions of Fut2 ΔISC and Fut2 ΔISC + Torin1 organoids. * P < 0.05, ** P < 0.01, and *** P < 0.001.

Techniques Used: Inhibition, Derivative Assay, Activity Assay, Expressing

The mechanism of Fut2-deficiency-induced facilitation of ISC aging. Fut2 knockout resulted in loss of α1,2-fucosylation on Asah2 and Npc1, which impaired respiratory complexes and mitophagy, and therefore suppressed ATP production and promoted ROS production. These mitochondrial dysfunctions promoted stemness impairment and ISC aging. This figure is illustrated using BioRender ( www.biorender.com ).

Figure Legend Snippet: The mechanism of Fut2-deficiency-induced facilitation of ISC aging. Fut2 knockout resulted in loss of α1,2-fucosylation on Asah2 and Npc1, which impaired respiratory complexes and mitophagy, and therefore suppressed ATP production and promoted ROS production. These mitochondrial dysfunctions promoted stemness impairment and ISC aging. This figure is illustrated using BioRender ( www.biorender.com ).

Techniques Used: Knock-Out

Recombinant:

Article Title: Fut2 Deficiency Promotes Intestinal Stem Cell Aging by Damaging Mitochondrial Functions via Down-Regulating α1,2-Fucosylation of Asah2 and Npc1
Article Snippet: To establish an in vitro model of oxidative-stress-induced aging, organoids derived from 12-week-old mice were treated with 500 μM hydrogen peroxide (H 2 O 2 ; Sigma-Aldrich, 88597) for 12 h. CCCP (10 μM; Selleck, S6494) treatment for 4 h was used to activate mitophagy. .. Ten micrograms of Asah2 recombinant protein (MedChemExpress, HY-P76735) and 250 nM mTOR inhibitor Torin1 (MedChemExpress, HY-13003) were used to treat organoids to confirm the role of Asah2 and Npc1 fucosylation. ..

Image Search Results

Journal: Research

Article Title: Fut2 Deficiency Promotes Intestinal Stem Cell Aging by Damaging Mitochondrial Functions via Down-Regulating α1,2-Fucosylation of Asah2 and Npc1

doi: 10.34133/research.0343

Figure Lengend Snippet: Fut2 deficiency in ISCs resulted in impairment of α1,2-fucosylation of mitochondrial-function-related proteins. (A) Volcano plot of differently expressed N-glycosylated proteins and sites in Fut2 knockout ISCs compared to WT. (B) Fold change of protein level and N-glycosylation level of mitochondrial-function-related proteins Asah2, Npc1, and Bsg. (C) IHC analysis of Asah2 in ileal sections of WT and Fut2 ΔISC mice. Scale bar, 100 μm. (D) The protein level of Npc1, Asah2, and Bsg in whole-cell lysate and UEA-I-enriched proteins of WT and Fut2 ΔISC ISCs. (E) Protein expression of mTOR and p-mTOR in WT and Fut2 ΔISC crypts. * P < 0.05, ** P < 0.01, and *** P < 0.001. ns, no significant.

Article Snippet: Ten micrograms of Asah2 recombinant protein (MedChemExpress, HY-P76735) and 250 nM mTOR inhibitor Torin1 (MedChemExpress, HY-13003) were used to treat organoids to confirm the role of Asah2 and Npc1 fucosylation.

Techniques: Knock-Out, Glycoproteomics, Expressing

Journal: Research

Article Title: Fut2 Deficiency Promotes Intestinal Stem Cell Aging by Damaging Mitochondrial Functions via Down-Regulating α1,2-Fucosylation of Asah2 and Npc1

doi: 10.34133/research.0343

Figure Lengend Snippet: Loss of α1,2-fucosylation of Asah2 and Npc1 induced stemness impairment and mitochondrial dysfunction in ISCs. (A) The protein level of Npc1, Asah2, and Bsg in whole-cell lysate and UEA-I-enriched proteins of WT and corresponding SDM organoids. (B) Images of WT, Asah2-N444Q, and Npc1-N961Q organoids and IF analysis of EGFP-labeled ISCs. Scale bars, 100 μm. (C) EdU assays in WT, Asah2-N444Q, and Npc1-N961Q organoids. Scale bar, 100 μm. (D) qPCR results of stemness markers in WT, Asah2-N444Q, and Npc1-N961Q organoids. (E to G) SA-β-gal staining of senescent cells, MitoSOX-indicated mtROS, and JC-1-indicated MMP analysis in WT, Asah2-N444Q, and Npc1-N961Q organoids. Scale bars, 100 μm. (H) Activity assays of respiratory complexes I, III, IV, and V in WT and Asah2-N444Q organoids. (I) Protein expression of mTOR and p-mTOR in WT and Npc1-N961Q organoids. (J) Expression of mitochondrial and mitophagy proteins in the whole-cell lysate of WT and Npc1-N961Q organoids. CCCP was used to activate mitophagy. (K) Expression of mitochondrial and mitophagy proteins in lysosome fractions of WT and Npc1-N961Q organoids. * P < 0.05 and ** P < 0.01.

Techniques: Labeling, Staining, Activity Assay, Expressing

Journal: Research

Article Title: Fut2 Deficiency Promotes Intestinal Stem Cell Aging by Damaging Mitochondrial Functions via Down-Regulating α1,2-Fucosylation of Asah2 and Npc1

doi: 10.34133/research.0343

Figure Lengend Snippet: Asah2 supplement and mTOR inhibition ameliorated stemness impairment and mitochondrial dysfunction in Fut2 ΔISC organoids. (A) Development of organoids derived from WT and Fut2 ΔISC mice, with or without Asah2 and Torin1 treatment. Scale bar, 100 μm. (B) Statistical analysis of surface areas and budding number of organoids. (C and D) IF analysis of EGFP and EdU in WT and Fut2 ΔISC organoids, with or without Asah2 and Torin1 treatment. Scale bars, 100 μm. (E and F) JC-1-indicated MMP and MitoSOX-indicated mtROS analysis in WT and Fut2 ΔISC organoids, with or without Asah2 and Torin1 treatment. Scale bars, 100 μm. (G) Activity of complexes I, III. IV, and V in WT, Fut2 ΔISC, and Fut2 ΔISC + Asah2 organoids. (H) Expression of mitochondrial and mitophagy proteins in whole-cell lysate of Fut2 ΔISC and Fut2 ΔISC + Torin1 organoids. CCCP was used to activate mitophagy. (I) Expression of mitochondrial and mitophagy proteins in lysosome fractions of Fut2 ΔISC and Fut2 ΔISC + Torin1 organoids. * P < 0.05, ** P < 0.01, and *** P < 0.001.

Techniques: Inhibition, Derivative Assay, Activity Assay, Expressing

Journal: Research

Article Title: Fut2 Deficiency Promotes Intestinal Stem Cell Aging by Damaging Mitochondrial Functions via Down-Regulating α1,2-Fucosylation of Asah2 and Npc1

doi: 10.34133/research.0343

Figure Lengend Snippet: The mechanism of Fut2-deficiency-induced facilitation of ISC aging. Fut2 knockout resulted in loss of α1,2-fucosylation on Asah2 and Npc1, which impaired respiratory complexes and mitophagy, and therefore suppressed ATP production and promoted ROS production. These mitochondrial dysfunctions promoted stemness impairment and ISC aging. This figure is illustrated using BioRender ( www.biorender.com ).

Techniques: Knock-Out

Ambroxol prevents infection with SARS-CoV-2. A , Vero-E6 cells were pretreated with 10 μM or 25 μM ambroxol for 1 h or left untreated and were infected with pp-VSV-SARS-CoV-2 spike or pp-VSV-G for 24 h. Infection was measured by the expression of eGFP in the cells. Ambroxol blocked the infection of the cells with pp-VSV-SARS-CoV-2 spike ( closed symbols ) but had no influence on infection with pp-VSV-G ( open symbols ). Reconstitution of ceramide in Vero-E6 cells that had been treated with 25 μM ambroxol by the addition of 10 μM C16 ceramide or 0.2 U/ml acid sphingomyelinase (ASM) restored infection of the cells with pp-VSV-SARS-CoV-2 spike. Shown are the means ± SD of the percentage of infected cells from six independent experiments. ∗∗∗ p < 0.001, ANOVA, followed by post hoc Student's t tests. B , higher concentrations of the pp-VSV-SARS-CoV-2 spike result in a higher percentage of infected cells but do not alter the ability of ambroxol to dose dependently inhibit infection of Vero-E6 cells. Neutralization of surface ceramide with two different anti-ceramide antibodies, that is, a monoclonal IgM antibody and an IgG antibody, or treatment with a ceramidase also prevented infection with pp-VSV-SARS-CoV-2 spike. Addition of sphingomyelin (50 μM) was without effect on the infection. Given are the means ± SD of the percentage of infected cells from six independent experiments. ∗∗∗ p < 0.001, ANOVA, followed by post hoc Student's t tests. Black symbols are untreated and ambroxol-treated cells, and gray symbols represent cells constituted with anti-ceramide antibodies or sphingomyelin. C , treatment of Caco-2 cells with ambroxol dose dependently prevented infection with pp-VSV-SARS-CoV-2 spike. Likewise, transfection of Caco-2 cells with shRNA targeting the acid sphingomyelinase prevented infection, whereas a control shRNA had no effect on the infection. Addition of ambroxol to cells transfected with acid sphingomyelinase targeting shRNA had no additional effects. Displayed are the means ± SD of the percentage of infected cells from six independent experiments. ∗∗∗ p < 0.001, ANOVA, followed by post hoc Student's t tests. Closed symbols are untransfected cells, and open symbols represent transfected cells. eGFP, enhanced GFP; pp-VSV-SARS-CoV-2, vesicular stomatitis virus pseudoviral particles presenting SARS-CoV-2 spike protein on their surface; SARS-CoV-2, severe acute respiratory syndrome coronavirus 2.

Journal: The Journal of Biological Chemistry

Article Title: Inhibition of acid sphingomyelinase by ambroxol prevents SARS-CoV-2 entry into epithelial cells

doi: 10.1016/j.jbc.2021.100701

Figure Lengend Snippet: Ambroxol prevents infection with SARS-CoV-2. A , Vero-E6 cells were pretreated with 10 μM or 25 μM ambroxol for 1 h or left untreated and were infected with pp-VSV-SARS-CoV-2 spike or pp-VSV-G for 24 h. Infection was measured by the expression of eGFP in the cells. Ambroxol blocked the infection of the cells with pp-VSV-SARS-CoV-2 spike ( closed symbols ) but had no influence on infection with pp-VSV-G ( open symbols ). Reconstitution of ceramide in Vero-E6 cells that had been treated with 25 μM ambroxol by the addition of 10 μM C16 ceramide or 0.2 U/ml acid sphingomyelinase (ASM) restored infection of the cells with pp-VSV-SARS-CoV-2 spike. Shown are the means ± SD of the percentage of infected cells from six independent experiments. ∗∗∗ p < 0.001, ANOVA, followed by post hoc Student's t tests. B , higher concentrations of the pp-VSV-SARS-CoV-2 spike result in a higher percentage of infected cells but do not alter the ability of ambroxol to dose dependently inhibit infection of Vero-E6 cells. Neutralization of surface ceramide with two different anti-ceramide antibodies, that is, a monoclonal IgM antibody and an IgG antibody, or treatment with a ceramidase also prevented infection with pp-VSV-SARS-CoV-2 spike. Addition of sphingomyelin (50 μM) was without effect on the infection. Given are the means ± SD of the percentage of infected cells from six independent experiments. ∗∗∗ p < 0.001, ANOVA, followed by post hoc Student's t tests. Black symbols are untreated and ambroxol-treated cells, and gray symbols represent cells constituted with anti-ceramide antibodies or sphingomyelin. C , treatment of Caco-2 cells with ambroxol dose dependently prevented infection with pp-VSV-SARS-CoV-2 spike. Likewise, transfection of Caco-2 cells with shRNA targeting the acid sphingomyelinase prevented infection, whereas a control shRNA had no effect on the infection. Addition of ambroxol to cells transfected with acid sphingomyelinase targeting shRNA had no additional effects. Displayed are the means ± SD of the percentage of infected cells from six independent experiments. ∗∗∗ p < 0.001, ANOVA, followed by post hoc Student's t tests. Closed symbols are untransfected cells, and open symbols represent transfected cells. eGFP, enhanced GFP; pp-VSV-SARS-CoV-2, vesicular stomatitis virus pseudoviral particles presenting SARS-CoV-2 spike protein on their surface; SARS-CoV-2, severe acute respiratory syndrome coronavirus 2.

Article Snippet: Ceramide was neutralized in Vero-E6 cells by addition of 50 μg/ml of the anticeramide IgM antibody clone S85-9 (Glycobiotech; MAB_0014) or of 100 μg/ml of a mouse monoclonal anticeramide IgG (Antibody Research Corp; #111583), or 0.2 units/ml of neutral ceramidase (R&D; #3557 AH) to the cells.

Techniques: Infection, Expressing, Neutralization, Transfection, shRNA, Control, Virus

Review

asah2 recombinant protein (MedChemExpress)

Structured Review

Images

1) Product Images from "Fut2 Deficiency Promotes Intestinal Stem Cell Aging by Damaging Mitochondrial Functions via Down-Regulating α1,2-Fucosylation of Asah2 and Npc1"

Related Articles

Recombinant:

Similar Products

Image Search Results