anti mouse c1q  (Hycult Biotech)


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    Hycult Biotech anti mouse c1q
    Deposition of components of the mouse complement system on PNPs. The proteins adsorbed on PNPs were analyzed by LC-MS/MS and Western blot (WB) analyses. Immunoglobulins were quantified by LC-MS/MS ( A ) and the deposition of mouse IgG ( B ) and IgM ( C ) was also analyzed by WB (attended band at 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ); the corresponding bands of <t>C1q</t> chains were visualized by WB ( E , attended bands height: ~26 and 27 kDa). Proteins of the alternative pathway ( F ) deposited on particles were detected by LC-MS/MS analysis. LC-MS/MS data (n=4) are presented as abundance values (arbitrary values generated by mass spec peak integration) and are shown as boxplot with median value. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; MS: mouse serum; empty: empty well
    Anti Mouse C1q, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti mouse c1q/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti mouse c1q - by Bioz Stars, 2024-04
    93/100 stars

    Images

    1) Product Images from "Surface antibody changes protein corona both in human and mouse serum but not final opsonization and elimination of targeted polymeric nanoparticles"

    Article Title: Surface antibody changes protein corona both in human and mouse serum but not final opsonization and elimination of targeted polymeric nanoparticles

    Journal: Journal of Nanobiotechnology

    doi: 10.1186/s12951-023-02134-4

    Deposition of components of the mouse complement system on PNPs. The proteins adsorbed on PNPs were analyzed by LC-MS/MS and Western blot (WB) analyses. Immunoglobulins were quantified by LC-MS/MS ( A ) and the deposition of mouse IgG ( B ) and IgM ( C ) was also analyzed by WB (attended band at 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ); the corresponding bands of C1q chains were visualized by WB ( E , attended bands height: ~26 and 27 kDa). Proteins of the alternative pathway ( F ) deposited on particles were detected by LC-MS/MS analysis. LC-MS/MS data (n=4) are presented as abundance values (arbitrary values generated by mass spec peak integration) and are shown as boxplot with median value. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; MS: mouse serum; empty: empty well
    Figure Legend Snippet: Deposition of components of the mouse complement system on PNPs. The proteins adsorbed on PNPs were analyzed by LC-MS/MS and Western blot (WB) analyses. Immunoglobulins were quantified by LC-MS/MS ( A ) and the deposition of mouse IgG ( B ) and IgM ( C ) was also analyzed by WB (attended band at 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ); the corresponding bands of C1q chains were visualized by WB ( E , attended bands height: ~26 and 27 kDa). Proteins of the alternative pathway ( F ) deposited on particles were detected by LC-MS/MS analysis. LC-MS/MS data (n=4) are presented as abundance values (arbitrary values generated by mass spec peak integration) and are shown as boxplot with median value. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; MS: mouse serum; empty: empty well

    Techniques Used: Liquid Chromatography with Mass Spectroscopy, Western Blot, Activation Assay, Generated, Mass Spectrometry

    Deposition of proteins of the human complement system on PNPs. The adsorbed proteins were analyzed by LC-MS/MS and Western blot (WB) analyses. A. Adsorbed immunoglobulins such as IgG (i.e., IgG1, IgG2, IgG3) and IgM were detected by LC-MS/MS. The deposition of human IgG ( B ) and IgM ( C ) was also analyzed by WB analysis (attended band: 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ) and the bands corresponding to C1q chains were visualized by WB ( E , attended bands of C1q at ~ 23, 27 and 29 kDa). Proteins of the alternative ( F ) pathway were detected by LC-MS/MS analysis. LC-MS/MS data are shown as boxplots with median value. * p-value < 0.05; ** p-value < 0.01. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; HS: human serum; HP: human plasma; empty: empty well
    Figure Legend Snippet: Deposition of proteins of the human complement system on PNPs. The adsorbed proteins were analyzed by LC-MS/MS and Western blot (WB) analyses. A. Adsorbed immunoglobulins such as IgG (i.e., IgG1, IgG2, IgG3) and IgM were detected by LC-MS/MS. The deposition of human IgG ( B ) and IgM ( C ) was also analyzed by WB analysis (attended band: 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ) and the bands corresponding to C1q chains were visualized by WB ( E , attended bands of C1q at ~ 23, 27 and 29 kDa). Proteins of the alternative ( F ) pathway were detected by LC-MS/MS analysis. LC-MS/MS data are shown as boxplots with median value. * p-value < 0.05; ** p-value < 0.01. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; HS: human serum; HP: human plasma; empty: empty well

    Techniques Used: Liquid Chromatography with Mass Spectroscopy, Western Blot, Activation Assay

    anti mouse c1q  (Hycult Biotech)


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    Structured Review

    Hycult Biotech anti mouse c1q
    Deposition of components of the mouse complement system on PNPs. The proteins adsorbed on PNPs were analyzed by LC-MS/MS and Western blot (WB) analyses. Immunoglobulins were quantified by LC-MS/MS ( A ) and the deposition of mouse IgG ( B ) and IgM ( C ) was also analyzed by WB (attended band at 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ); the corresponding bands of <t>C1q</t> chains were visualized by WB ( E , attended bands height: ~26 and 27 kDa). Proteins of the alternative pathway ( F ) deposited on particles were detected by LC-MS/MS analysis. LC-MS/MS data (n=4) are presented as abundance values (arbitrary values generated by mass spec peak integration) and are shown as boxplot with median value. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; MS: mouse serum; empty: empty well
    Anti Mouse C1q, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti mouse c1q/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti mouse c1q - by Bioz Stars, 2024-04
    93/100 stars

    Images

    1) Product Images from "Surface antibody changes protein corona both in human and mouse serum but not final opsonization and elimination of targeted polymeric nanoparticles"

    Article Title: Surface antibody changes protein corona both in human and mouse serum but not final opsonization and elimination of targeted polymeric nanoparticles

    Journal: Journal of Nanobiotechnology

    doi: 10.1186/s12951-023-02134-4

    Deposition of components of the mouse complement system on PNPs. The proteins adsorbed on PNPs were analyzed by LC-MS/MS and Western blot (WB) analyses. Immunoglobulins were quantified by LC-MS/MS ( A ) and the deposition of mouse IgG ( B ) and IgM ( C ) was also analyzed by WB (attended band at 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ); the corresponding bands of C1q chains were visualized by WB ( E , attended bands height: ~26 and 27 kDa). Proteins of the alternative pathway ( F ) deposited on particles were detected by LC-MS/MS analysis. LC-MS/MS data (n=4) are presented as abundance values (arbitrary values generated by mass spec peak integration) and are shown as boxplot with median value. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; MS: mouse serum; empty: empty well
    Figure Legend Snippet: Deposition of components of the mouse complement system on PNPs. The proteins adsorbed on PNPs were analyzed by LC-MS/MS and Western blot (WB) analyses. Immunoglobulins were quantified by LC-MS/MS ( A ) and the deposition of mouse IgG ( B ) and IgM ( C ) was also analyzed by WB (attended band at 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ); the corresponding bands of C1q chains were visualized by WB ( E , attended bands height: ~26 and 27 kDa). Proteins of the alternative pathway ( F ) deposited on particles were detected by LC-MS/MS analysis. LC-MS/MS data (n=4) are presented as abundance values (arbitrary values generated by mass spec peak integration) and are shown as boxplot with median value. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; MS: mouse serum; empty: empty well

    Techniques Used: Liquid Chromatography with Mass Spectroscopy, Western Blot, Activation Assay, Generated, Mass Spectrometry

    Deposition of proteins of the human complement system on PNPs. The adsorbed proteins were analyzed by LC-MS/MS and Western blot (WB) analyses. A. Adsorbed immunoglobulins such as IgG (i.e., IgG1, IgG2, IgG3) and IgM were detected by LC-MS/MS. The deposition of human IgG ( B ) and IgM ( C ) was also analyzed by WB analysis (attended band: 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ) and the bands corresponding to C1q chains were visualized by WB ( E , attended bands of C1q at ~ 23, 27 and 29 kDa). Proteins of the alternative ( F ) pathway were detected by LC-MS/MS analysis. LC-MS/MS data are shown as boxplots with median value. * p-value < 0.05; ** p-value < 0.01. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; HS: human serum; HP: human plasma; empty: empty well
    Figure Legend Snippet: Deposition of proteins of the human complement system on PNPs. The adsorbed proteins were analyzed by LC-MS/MS and Western blot (WB) analyses. A. Adsorbed immunoglobulins such as IgG (i.e., IgG1, IgG2, IgG3) and IgM were detected by LC-MS/MS. The deposition of human IgG ( B ) and IgM ( C ) was also analyzed by WB analysis (attended band: 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ) and the bands corresponding to C1q chains were visualized by WB ( E , attended bands of C1q at ~ 23, 27 and 29 kDa). Proteins of the alternative ( F ) pathway were detected by LC-MS/MS analysis. LC-MS/MS data are shown as boxplots with median value. * p-value < 0.05; ** p-value < 0.01. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; HS: human serum; HP: human plasma; empty: empty well

    Techniques Used: Liquid Chromatography with Mass Spectroscopy, Western Blot, Activation Assay

    c1q  (Hycult Biotech)


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    Hycult Biotech c1q
    Complement component 1, Q subcomponent <t>(C1q)</t> and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.
    C1q, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/c1q/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    c1q - by Bioz Stars, 2024-04
    93/100 stars

    Images

    1) Product Images from "Complement Factor D protects mice from ethanol-induced inflammation and liver injury"

    Article Title: Complement Factor D protects mice from ethanol-induced inflammation and liver injury

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    doi: 10.1152/ajpgi.00334.2017

    Complement component 1, Q subcomponent (C1q) and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.
    Figure Legend Snippet: Complement component 1, Q subcomponent (C1q) and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.

    Techniques Used: Immunodetection, Staining, Software, Expressing, Real-time Polymerase Chain Reaction

    Hepatic complement component 1, Q subcomponent (C1q) deposition was increased in wild-type (WT) and complement factor D-deficient (FD−/−) mice after short-term and chronic ethanol (EtOH) feeding. WT and FD−/− mice were allowed free access to EtOH [11%, day (d) 4 and 32%, day 25] or pair-fed control diets. A: frozen liver sections were immunostained for C1q deposition. Representative images for C1q deposition in pair-fed controls for chronic 25-day studies were similar to 4 days (data not shown). All images were acquired using a ×40 oil immersion objective. Positive immunofluorescence after short-term (B) and chronic (C) EtOH feeding was quantified from at least three images per slide using Image-Pro Plus software. Values represent means ± SE; values with different superscripts were significantly different from each other (P < 0.05); n = 4 pair-fed and 6 EtOH-fed mice.
    Figure Legend Snippet: Hepatic complement component 1, Q subcomponent (C1q) deposition was increased in wild-type (WT) and complement factor D-deficient (FD−/−) mice after short-term and chronic ethanol (EtOH) feeding. WT and FD−/− mice were allowed free access to EtOH [11%, day (d) 4 and 32%, day 25] or pair-fed control diets. A: frozen liver sections were immunostained for C1q deposition. Representative images for C1q deposition in pair-fed controls for chronic 25-day studies were similar to 4 days (data not shown). All images were acquired using a ×40 oil immersion objective. Positive immunofluorescence after short-term (B) and chronic (C) EtOH feeding was quantified from at least three images per slide using Image-Pro Plus software. Values represent means ± SE; values with different superscripts were significantly different from each other (P < 0.05); n = 4 pair-fed and 6 EtOH-fed mice.

    Techniques Used: Immunofluorescence, Software

    Complement activation and involvement during alcoholic liver disease. In mouse models of ALD, ethanol (EtOH) induces the activation of complement via complement component 1, Q subcomponent (C1q), leading to the cleavage of complement protein 3 (C3) into the anaphylatoxin fragment of C3 (C3a) and C3b. The potent anaphylatoxins C3a and C5a act on cognate receptors (C3aR and C5aR) on resident hepatic macrophages (Kupffer cells) to initiate the transcription of proinflammatory mediators. During chronic EtOH, amplification of complement via the alternative pathway is required to provide essential opsonins (C3b/iC3b/C3c) on the surface of damaged cells in the liver, facilitating clearance of debris and allowing for resolution and repair. TNF-α, tumor necrosis factor-α; IL-6, interleukin-6; MCP-1, macrophage chemoattractant protein-1; FB, complement factor B; FD, complement factor D; C4, complement protein 4; C2, complement protein 2; C4b, 2a, C3 convertase; fBb, FB activation fragment b; fBa, FB activation fragment a. Reprinted with permission, Cleveland Clinic Center for Medical Art & Photography © 2018. All Rights Reserved.
    Figure Legend Snippet: Complement activation and involvement during alcoholic liver disease. In mouse models of ALD, ethanol (EtOH) induces the activation of complement via complement component 1, Q subcomponent (C1q), leading to the cleavage of complement protein 3 (C3) into the anaphylatoxin fragment of C3 (C3a) and C3b. The potent anaphylatoxins C3a and C5a act on cognate receptors (C3aR and C5aR) on resident hepatic macrophages (Kupffer cells) to initiate the transcription of proinflammatory mediators. During chronic EtOH, amplification of complement via the alternative pathway is required to provide essential opsonins (C3b/iC3b/C3c) on the surface of damaged cells in the liver, facilitating clearance of debris and allowing for resolution and repair. TNF-α, tumor necrosis factor-α; IL-6, interleukin-6; MCP-1, macrophage chemoattractant protein-1; FB, complement factor B; FD, complement factor D; C4, complement protein 4; C2, complement protein 2; C4b, 2a, C3 convertase; fBb, FB activation fragment b; fBa, FB activation fragment a. Reprinted with permission, Cleveland Clinic Center for Medical Art & Photography © 2018. All Rights Reserved.

    Techniques Used: Activation Assay, Amplification

    c1q  (Hycult Biotech)


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    Hycult Biotech c1q
    Complement component 1, Q subcomponent <t>(C1q)</t> and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.
    C1q, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/c1q/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    c1q - by Bioz Stars, 2024-04
    93/100 stars

    Images

    1) Product Images from "Complement Factor D protects mice from ethanol-induced inflammation and liver injury"

    Article Title: Complement Factor D protects mice from ethanol-induced inflammation and liver injury

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    doi: 10.1152/ajpgi.00334.2017

    Complement component 1, Q subcomponent (C1q) and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.
    Figure Legend Snippet: Complement component 1, Q subcomponent (C1q) and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.

    Techniques Used: Immunodetection, Staining, Software, Expressing, Real-time Polymerase Chain Reaction

    Hepatic complement component 1, Q subcomponent (C1q) deposition was increased in wild-type (WT) and complement factor D-deficient (FD−/−) mice after short-term and chronic ethanol (EtOH) feeding. WT and FD−/− mice were allowed free access to EtOH [11%, day (d) 4 and 32%, day 25] or pair-fed control diets. A: frozen liver sections were immunostained for C1q deposition. Representative images for C1q deposition in pair-fed controls for chronic 25-day studies were similar to 4 days (data not shown). All images were acquired using a ×40 oil immersion objective. Positive immunofluorescence after short-term (B) and chronic (C) EtOH feeding was quantified from at least three images per slide using Image-Pro Plus software. Values represent means ± SE; values with different superscripts were significantly different from each other (P < 0.05); n = 4 pair-fed and 6 EtOH-fed mice.
    Figure Legend Snippet: Hepatic complement component 1, Q subcomponent (C1q) deposition was increased in wild-type (WT) and complement factor D-deficient (FD−/−) mice after short-term and chronic ethanol (EtOH) feeding. WT and FD−/− mice were allowed free access to EtOH [11%, day (d) 4 and 32%, day 25] or pair-fed control diets. A: frozen liver sections were immunostained for C1q deposition. Representative images for C1q deposition in pair-fed controls for chronic 25-day studies were similar to 4 days (data not shown). All images were acquired using a ×40 oil immersion objective. Positive immunofluorescence after short-term (B) and chronic (C) EtOH feeding was quantified from at least three images per slide using Image-Pro Plus software. Values represent means ± SE; values with different superscripts were significantly different from each other (P < 0.05); n = 4 pair-fed and 6 EtOH-fed mice.

    Techniques Used: Immunofluorescence, Software

    Complement activation and involvement during alcoholic liver disease. In mouse models of ALD, ethanol (EtOH) induces the activation of complement via complement component 1, Q subcomponent (C1q), leading to the cleavage of complement protein 3 (C3) into the anaphylatoxin fragment of C3 (C3a) and C3b. The potent anaphylatoxins C3a and C5a act on cognate receptors (C3aR and C5aR) on resident hepatic macrophages (Kupffer cells) to initiate the transcription of proinflammatory mediators. During chronic EtOH, amplification of complement via the alternative pathway is required to provide essential opsonins (C3b/iC3b/C3c) on the surface of damaged cells in the liver, facilitating clearance of debris and allowing for resolution and repair. TNF-α, tumor necrosis factor-α; IL-6, interleukin-6; MCP-1, macrophage chemoattractant protein-1; FB, complement factor B; FD, complement factor D; C4, complement protein 4; C2, complement protein 2; C4b, 2a, C3 convertase; fBb, FB activation fragment b; fBa, FB activation fragment a. Reprinted with permission, Cleveland Clinic Center for Medical Art & Photography © 2018. All Rights Reserved.
    Figure Legend Snippet: Complement activation and involvement during alcoholic liver disease. In mouse models of ALD, ethanol (EtOH) induces the activation of complement via complement component 1, Q subcomponent (C1q), leading to the cleavage of complement protein 3 (C3) into the anaphylatoxin fragment of C3 (C3a) and C3b. The potent anaphylatoxins C3a and C5a act on cognate receptors (C3aR and C5aR) on resident hepatic macrophages (Kupffer cells) to initiate the transcription of proinflammatory mediators. During chronic EtOH, amplification of complement via the alternative pathway is required to provide essential opsonins (C3b/iC3b/C3c) on the surface of damaged cells in the liver, facilitating clearance of debris and allowing for resolution and repair. TNF-α, tumor necrosis factor-α; IL-6, interleukin-6; MCP-1, macrophage chemoattractant protein-1; FB, complement factor B; FD, complement factor D; C4, complement protein 4; C2, complement protein 2; C4b, 2a, C3 convertase; fBb, FB activation fragment b; fBa, FB activation fragment a. Reprinted with permission, Cleveland Clinic Center for Medical Art & Photography © 2018. All Rights Reserved.

    Techniques Used: Activation Assay, Amplification

    monoclonal anti mouse c1q  (Hycult Biotech)


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    Hycult Biotech monoclonal anti mouse c1q
    Monoclonal Anti Mouse C1q, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/monoclonal anti mouse c1q/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    monoclonal anti mouse c1q - by Bioz Stars, 2024-04
    93/100 stars

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    monoclonal anti mouse c1q  (Hycult Biotech)


    Bioz Verified Symbol Hycult Biotech is a verified supplier
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    Hycult Biotech monoclonal anti mouse c1q
    Monoclonal Anti Mouse C1q, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/monoclonal anti mouse c1q/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    monoclonal anti mouse c1q - by Bioz Stars, 2024-04
    93/100 stars

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  • 93
    Hycult Biotech anti mouse c1q
    Deposition of components of the mouse complement system on PNPs. The proteins adsorbed on PNPs were analyzed by LC-MS/MS and Western blot (WB) analyses. Immunoglobulins were quantified by LC-MS/MS ( A ) and the deposition of mouse IgG ( B ) and IgM ( C ) was also analyzed by WB (attended band at 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ); the corresponding bands of <t>C1q</t> chains were visualized by WB ( E , attended bands height: ~26 and 27 kDa). Proteins of the alternative pathway ( F ) deposited on particles were detected by LC-MS/MS analysis. LC-MS/MS data (n=4) are presented as abundance values (arbitrary values generated by mass spec peak integration) and are shown as boxplot with median value. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; MS: mouse serum; empty: empty well
    Anti Mouse C1q, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti mouse c1q/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
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    anti mouse c1q - by Bioz Stars, 2024-04
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    93
    Hycult Biotech c1q
    Complement component 1, Q subcomponent <t>(C1q)</t> and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.
    C1q, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/c1q/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    c1q - by Bioz Stars, 2024-04
    93/100 stars
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    93
    Hycult Biotech monoclonal anti mouse c1q
    Complement component 1, Q subcomponent <t>(C1q)</t> and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.
    Monoclonal Anti Mouse C1q, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/monoclonal anti mouse c1q/product/Hycult Biotech
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    monoclonal anti mouse c1q - by Bioz Stars, 2024-04
    93/100 stars
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    Image Search Results


    Deposition of components of the mouse complement system on PNPs. The proteins adsorbed on PNPs were analyzed by LC-MS/MS and Western blot (WB) analyses. Immunoglobulins were quantified by LC-MS/MS ( A ) and the deposition of mouse IgG ( B ) and IgM ( C ) was also analyzed by WB (attended band at 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ); the corresponding bands of C1q chains were visualized by WB ( E , attended bands height: ~26 and 27 kDa). Proteins of the alternative pathway ( F ) deposited on particles were detected by LC-MS/MS analysis. LC-MS/MS data (n=4) are presented as abundance values (arbitrary values generated by mass spec peak integration) and are shown as boxplot with median value. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; MS: mouse serum; empty: empty well

    Journal: Journal of Nanobiotechnology

    Article Title: Surface antibody changes protein corona both in human and mouse serum but not final opsonization and elimination of targeted polymeric nanoparticles

    doi: 10.1186/s12951-023-02134-4

    Figure Lengend Snippet: Deposition of components of the mouse complement system on PNPs. The proteins adsorbed on PNPs were analyzed by LC-MS/MS and Western blot (WB) analyses. Immunoglobulins were quantified by LC-MS/MS ( A ) and the deposition of mouse IgG ( B ) and IgM ( C ) was also analyzed by WB (attended band at 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ); the corresponding bands of C1q chains were visualized by WB ( E , attended bands height: ~26 and 27 kDa). Proteins of the alternative pathway ( F ) deposited on particles were detected by LC-MS/MS analysis. LC-MS/MS data (n=4) are presented as abundance values (arbitrary values generated by mass spec peak integration) and are shown as boxplot with median value. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; MS: mouse serum; empty: empty well

    Article Snippet: Primary antibodies such as anti-mouse C1q (Hycult Biotech, The Netherlands, 1:400), anti-mouse C3 (Cappel, 1:5,000), and anti-mouse C9 (gift from Prof. Mohamed Daha, 1:250) were used to detect mouse C components.

    Techniques: Liquid Chromatography with Mass Spectroscopy, Western Blot, Activation Assay, Generated, Mass Spectrometry

    Deposition of proteins of the human complement system on PNPs. The adsorbed proteins were analyzed by LC-MS/MS and Western blot (WB) analyses. A. Adsorbed immunoglobulins such as IgG (i.e., IgG1, IgG2, IgG3) and IgM were detected by LC-MS/MS. The deposition of human IgG ( B ) and IgM ( C ) was also analyzed by WB analysis (attended band: 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ) and the bands corresponding to C1q chains were visualized by WB ( E , attended bands of C1q at ~ 23, 27 and 29 kDa). Proteins of the alternative ( F ) pathway were detected by LC-MS/MS analysis. LC-MS/MS data are shown as boxplots with median value. * p-value < 0.05; ** p-value < 0.01. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; HS: human serum; HP: human plasma; empty: empty well

    Journal: Journal of Nanobiotechnology

    Article Title: Surface antibody changes protein corona both in human and mouse serum but not final opsonization and elimination of targeted polymeric nanoparticles

    doi: 10.1186/s12951-023-02134-4

    Figure Lengend Snippet: Deposition of proteins of the human complement system on PNPs. The adsorbed proteins were analyzed by LC-MS/MS and Western blot (WB) analyses. A. Adsorbed immunoglobulins such as IgG (i.e., IgG1, IgG2, IgG3) and IgM were detected by LC-MS/MS. The deposition of human IgG ( B ) and IgM ( C ) was also analyzed by WB analysis (attended band: 50 kDa and 75 kDa, respectively). Components of the classical complement activation pathway were analyzed by LC-MS/MS analysis ( D ) and the bands corresponding to C1q chains were visualized by WB ( E , attended bands of C1q at ~ 23, 27 and 29 kDa). Proteins of the alternative ( F ) pathway were detected by LC-MS/MS analysis. LC-MS/MS data are shown as boxplots with median value. * p-value < 0.05; ** p-value < 0.01. uPNPs: untargeted nanoparticles; tPNPs: targeted nanoparticles; HS: human serum; HP: human plasma; empty: empty well

    Article Snippet: Primary antibodies such as anti-mouse C1q (Hycult Biotech, The Netherlands, 1:400), anti-mouse C3 (Cappel, 1:5,000), and anti-mouse C9 (gift from Prof. Mohamed Daha, 1:250) were used to detect mouse C components.

    Techniques: Liquid Chromatography with Mass Spectroscopy, Western Blot, Activation Assay

    Complement component 1, Q subcomponent (C1q) and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Complement Factor D protects mice from ethanol-induced inflammation and liver injury

    doi: 10.1152/ajpgi.00334.2017

    Figure Lengend Snippet: Complement component 1, Q subcomponent (C1q) and complement protein 4 (C4) contributed to, while complement factor D (FD) protected from, chronic ethanol (EtOH)-induced hepatic inflammation. Wild-type (WT), C1q-deficient (C1qa−/−), complement protein 4-deficient (C4−/−), complement factor D-deficient (FD−/−), and C1q/FD−/− were allowed free access to EtOH [32%, day (d) 25] or pair-fed control diets. A: paraffin-embedded liver sections were deparaffinized followed by immunodetection of tumor necrosis factor-α (TNF-α). Nuclei were counterstained with hematoxylin. All images were acquired using a ×20 objective. B: TNF-α-stained areas were quantified from at least three images per slide using Image-Pro Plus software. Expression of TNF-α (C) and macrophage chemoattractant protein-1 (MCP-1/CCR2, D) mRNA was detected in mouse livers using Quantitative Real-Time Polymerase Chain Reaction. Values with different alphabetical superscripts were significantly different from each other (P < 0.05). Values represent means ± SE; n = 4–8 pair-fed and 6–12 EtOH-fed mice.

    Article Snippet: Frozen liver sections were mounted on glass slides, fixed with paraformaldehyde, and stained for C3b/iC3b/C3c (catalog no. HM1065; Hycult Biotech, Plymouth Meeting, PA) and C1q (catalog no. HM1044; Hycult Biotech) or Oil Red O as previously described ( 41 , 47 ).

    Techniques: Immunodetection, Staining, Software, Expressing, Real-time Polymerase Chain Reaction

    Hepatic complement component 1, Q subcomponent (C1q) deposition was increased in wild-type (WT) and complement factor D-deficient (FD−/−) mice after short-term and chronic ethanol (EtOH) feeding. WT and FD−/− mice were allowed free access to EtOH [11%, day (d) 4 and 32%, day 25] or pair-fed control diets. A: frozen liver sections were immunostained for C1q deposition. Representative images for C1q deposition in pair-fed controls for chronic 25-day studies were similar to 4 days (data not shown). All images were acquired using a ×40 oil immersion objective. Positive immunofluorescence after short-term (B) and chronic (C) EtOH feeding was quantified from at least three images per slide using Image-Pro Plus software. Values represent means ± SE; values with different superscripts were significantly different from each other (P < 0.05); n = 4 pair-fed and 6 EtOH-fed mice.

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Complement Factor D protects mice from ethanol-induced inflammation and liver injury

    doi: 10.1152/ajpgi.00334.2017

    Figure Lengend Snippet: Hepatic complement component 1, Q subcomponent (C1q) deposition was increased in wild-type (WT) and complement factor D-deficient (FD−/−) mice after short-term and chronic ethanol (EtOH) feeding. WT and FD−/− mice were allowed free access to EtOH [11%, day (d) 4 and 32%, day 25] or pair-fed control diets. A: frozen liver sections were immunostained for C1q deposition. Representative images for C1q deposition in pair-fed controls for chronic 25-day studies were similar to 4 days (data not shown). All images were acquired using a ×40 oil immersion objective. Positive immunofluorescence after short-term (B) and chronic (C) EtOH feeding was quantified from at least three images per slide using Image-Pro Plus software. Values represent means ± SE; values with different superscripts were significantly different from each other (P < 0.05); n = 4 pair-fed and 6 EtOH-fed mice.

    Article Snippet: Frozen liver sections were mounted on glass slides, fixed with paraformaldehyde, and stained for C3b/iC3b/C3c (catalog no. HM1065; Hycult Biotech, Plymouth Meeting, PA) and C1q (catalog no. HM1044; Hycult Biotech) or Oil Red O as previously described ( 41 , 47 ).

    Techniques: Immunofluorescence, Software

    Complement activation and involvement during alcoholic liver disease. In mouse models of ALD, ethanol (EtOH) induces the activation of complement via complement component 1, Q subcomponent (C1q), leading to the cleavage of complement protein 3 (C3) into the anaphylatoxin fragment of C3 (C3a) and C3b. The potent anaphylatoxins C3a and C5a act on cognate receptors (C3aR and C5aR) on resident hepatic macrophages (Kupffer cells) to initiate the transcription of proinflammatory mediators. During chronic EtOH, amplification of complement via the alternative pathway is required to provide essential opsonins (C3b/iC3b/C3c) on the surface of damaged cells in the liver, facilitating clearance of debris and allowing for resolution and repair. TNF-α, tumor necrosis factor-α; IL-6, interleukin-6; MCP-1, macrophage chemoattractant protein-1; FB, complement factor B; FD, complement factor D; C4, complement protein 4; C2, complement protein 2; C4b, 2a, C3 convertase; fBb, FB activation fragment b; fBa, FB activation fragment a. Reprinted with permission, Cleveland Clinic Center for Medical Art & Photography © 2018. All Rights Reserved.

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Complement Factor D protects mice from ethanol-induced inflammation and liver injury

    doi: 10.1152/ajpgi.00334.2017

    Figure Lengend Snippet: Complement activation and involvement during alcoholic liver disease. In mouse models of ALD, ethanol (EtOH) induces the activation of complement via complement component 1, Q subcomponent (C1q), leading to the cleavage of complement protein 3 (C3) into the anaphylatoxin fragment of C3 (C3a) and C3b. The potent anaphylatoxins C3a and C5a act on cognate receptors (C3aR and C5aR) on resident hepatic macrophages (Kupffer cells) to initiate the transcription of proinflammatory mediators. During chronic EtOH, amplification of complement via the alternative pathway is required to provide essential opsonins (C3b/iC3b/C3c) on the surface of damaged cells in the liver, facilitating clearance of debris and allowing for resolution and repair. TNF-α, tumor necrosis factor-α; IL-6, interleukin-6; MCP-1, macrophage chemoattractant protein-1; FB, complement factor B; FD, complement factor D; C4, complement protein 4; C2, complement protein 2; C4b, 2a, C3 convertase; fBb, FB activation fragment b; fBa, FB activation fragment a. Reprinted with permission, Cleveland Clinic Center for Medical Art & Photography © 2018. All Rights Reserved.

    Article Snippet: Frozen liver sections were mounted on glass slides, fixed with paraformaldehyde, and stained for C3b/iC3b/C3c (catalog no. HM1065; Hycult Biotech, Plymouth Meeting, PA) and C1q (catalog no. HM1044; Hycult Biotech) or Oil Red O as previously described ( 41 , 47 ).

    Techniques: Activation Assay, Amplification