mouse anti c1q primary ab Search Results


93
Hycult Biotech biotinylated mouse anti mouse c1q
Biotinylated Mouse 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
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Danaher Inc monoclonal mouse anti c1q antibody
Monoclonal Mouse Anti C1q Antibody, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad horseradishperoxidase hrp conjugated sheep anti human c1q antibody
Horseradishperoxidase Hrp Conjugated Sheep Anti Human C1q Antibody, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems anti adiponectin protein antibodies
Anti Adiponectin Protein Antibodies, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology adiponectin goat anti mouse igg hrp
Patient characteristics.
Adiponectin Goat Anti Mouse Igg Hrp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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GeneTex anti-rabbit adiponectin primary antibody gtx112777
Patient characteristics.
Anti Rabbit Adiponectin Primary Antibody Gtx112777, supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Quidel mouse anti-human c1q
Patient characteristics.
Mouse Anti Human C1q, supplied by Quidel, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology monoclonal mouse anti adiponectin
Patient characteristics.
Monoclonal Mouse Anti Adiponectin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cedarlane c1q antibody
Preparation and characterization of Neu-ABs and eNABs. ( A ) Schematic shows the purification of Neu-ABs through apoptosis induction and serial centrifugations, as well as the generation of eNABs. The latter process was conducted using a liposome extruder and followed two steps: (i) NABM was generated by repeated extrusion through the first filter (pore diameter: 400 nm); (ii) eNABs were generated through repeated extrusion of the mixed suspension (NABM and MSNs) through a smaller filter (pore diameter: 200 nm). ( B ) Representative SEM image of ABs derived from neutrophils. Scale bars, 1 μm. ( C ) The Annexin V and <t>C1q</t> staining of Neu-ABs. Scale bars, 5 μm. ( D ) Western blotting analysis of neutrophil and Neu-ABs. ( E ) Representative TEM images of MSNs and eNABs. Scale bars, 50 nm. ( F ) Size distribution of NABM, MSNs, and eNABs measured by DLS. Average diameter ( G ) and surface zeta potential ( H ) of NABM, MSNs, and eNABs (n = 3). ( I ) Representative images of the fluorescence colocalization of PKH67-labeled NABM and rhodamine-labeled MSNs in eNABs. The pure rhodamine-labeled MSNs were used as a control. Scale bars, 10 μm. ( J ) SDS-PAGE protein analysis of NABM, MSNs, and eNABs with Coomassie Blue staining. ( K ) Western blot analysis for membrane-specific protein markers. The storage stability ( L ) and the serum stability ( M ) of eNABs (n = 3). Data are presented as means ± SD. Statistical analysis between two groups was performed using unpaired two-tailed t-tests for M (** P < 0.01).
C1q Antibody, supplied by Cedarlane, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Danaher Inc rabbit anti mouse adiponectin
FIG. 6. Circulating levels of SAA, insulin, leptin, and <t>adiponectin.</t> Plasma was collected from mice at 12 weeks after diet. A: SAA levels were measured in 12–15 mice from each group using enzyme-linked immunosorbent assay. B: Insulin levels were measured in 9–14 mice from each group using RIA. C: Leptin levels were measured in 9–11 mice from each group using RIA. D: Adiponectin levels were measured in six mice from each group by SDS-PAGE as described in RESEARCH DESIGN AND METHODS. The high–molecular weight (HMW) form of the protein was quantified using densitometric analysis and is expressed relative to the a/a;LDLR/ chow diet levels. Data are presented as means SE. Genotypes and statistics are indicated below graphs.
Rabbit Anti Mouse Adiponectin, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology c1q
Stomach tissue from 15 month V30M animal stained with Thioflavin-S, α-hTTR antibody and Congo red in consecutive sections ( Ai-Avi ). The area of Thioflavin-S and α-hTTR antibody co-localization which was included in measurements as TTR plaques is indicated in ( Avi ). Stomach tissue from 5 month V30M animal stained with stained with Thioflavin-S and α-hTTR antibody indicating solely the presence of pre-fibrillar hTTR (Bi- Biii ) ( A&B Scale bar = 75mm). C Quantification of the amyloid plaques found in the stomach measured through Thioflavin-S and α-hTTR antibody co-localization for both the V30M and V30M <t>C1q</t> KO mice (n = 15/age group/line). Data presented as mean ± 1SD.
C1q, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson mouse monoclonal anti- cr1
Stomach tissue from 15 month V30M animal stained with Thioflavin-S, α-hTTR antibody and Congo red in consecutive sections ( Ai-Avi ). The area of Thioflavin-S and α-hTTR antibody co-localization which was included in measurements as TTR plaques is indicated in ( Avi ). Stomach tissue from 5 month V30M animal stained with stained with Thioflavin-S and α-hTTR antibody indicating solely the presence of pre-fibrillar hTTR (Bi- Biii ) ( A&B Scale bar = 75mm). C Quantification of the amyloid plaques found in the stomach measured through Thioflavin-S and α-hTTR antibody co-localization for both the V30M and V30M <t>C1q</t> KO mice (n = 15/age group/line). Data presented as mean ± 1SD.
Mouse Monoclonal Anti Cr1, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Patient characteristics.

Journal: Journal of Clinical Medicine

Article Title: Serum and Adipose Dipeptidyl Peptidase 4 in Cardiovascular Surgery Patients: Influence of Dipeptidyl Peptidase 4 Inhibitors

doi: 10.3390/jcm11154333

Figure Lengend Snippet: Patient characteristics.

Article Snippet: Secondary antibody reactions were performed at room temperature for 1 h. The antibodies used in the assay were DPP-4 and adiponectin goat anti-mouse IgG-HRP (sc-2005, Santa Cruz Biotech-nology, Inc., Dallas, TX, USA).

Techniques: Biomarker Discovery, Activity Assay

Comparison of dipeptidyl peptidase 4 (DPP-4), adiponectin, and tumor necrosis factor α (TNFα) expression in subcutaneous and epicardial adipose tissue. ( a ) Expression of DPP-4 in subcutaneous and epicardial adipose tissue. ( b ) Expression of adiponectin in subcutaneous and epicardial adipose tissue. ( c ) Expression of TNFα in subcutaneous and epicardial adipose tissue.

Journal: Journal of Clinical Medicine

Article Title: Serum and Adipose Dipeptidyl Peptidase 4 in Cardiovascular Surgery Patients: Influence of Dipeptidyl Peptidase 4 Inhibitors

doi: 10.3390/jcm11154333

Figure Lengend Snippet: Comparison of dipeptidyl peptidase 4 (DPP-4), adiponectin, and tumor necrosis factor α (TNFα) expression in subcutaneous and epicardial adipose tissue. ( a ) Expression of DPP-4 in subcutaneous and epicardial adipose tissue. ( b ) Expression of adiponectin in subcutaneous and epicardial adipose tissue. ( c ) Expression of TNFα in subcutaneous and epicardial adipose tissue.

Article Snippet: Secondary antibody reactions were performed at room temperature for 1 h. The antibodies used in the assay were DPP-4 and adiponectin goat anti-mouse IgG-HRP (sc-2005, Santa Cruz Biotech-nology, Inc., Dallas, TX, USA).

Techniques: Comparison, Expressing

Correlation between DPP-4 and other parameters in serum, subcutaneous adipose tissue, and epicardial adipose tissue.

Journal: Journal of Clinical Medicine

Article Title: Serum and Adipose Dipeptidyl Peptidase 4 in Cardiovascular Surgery Patients: Influence of Dipeptidyl Peptidase 4 Inhibitors

doi: 10.3390/jcm11154333

Figure Lengend Snippet: Correlation between DPP-4 and other parameters in serum, subcutaneous adipose tissue, and epicardial adipose tissue.

Article Snippet: Secondary antibody reactions were performed at room temperature for 1 h. The antibodies used in the assay were DPP-4 and adiponectin goat anti-mouse IgG-HRP (sc-2005, Santa Cruz Biotech-nology, Inc., Dallas, TX, USA).

Techniques: Activity Assay

Correlations between ( a ) serum and SAT adiponectin, ( b ) serum and EAT adiponectin, and ( c ) SAT and EAT adiponectin.

Journal: Journal of Clinical Medicine

Article Title: Serum and Adipose Dipeptidyl Peptidase 4 in Cardiovascular Surgery Patients: Influence of Dipeptidyl Peptidase 4 Inhibitors

doi: 10.3390/jcm11154333

Figure Lengend Snippet: Correlations between ( a ) serum and SAT adiponectin, ( b ) serum and EAT adiponectin, and ( c ) SAT and EAT adiponectin.

Article Snippet: Secondary antibody reactions were performed at room temperature for 1 h. The antibodies used in the assay were DPP-4 and adiponectin goat anti-mouse IgG-HRP (sc-2005, Santa Cruz Biotech-nology, Inc., Dallas, TX, USA).

Techniques:

Correlation between  adiponectin  and other parameters in serum, subcutaneous adipose tissue, and epicardial adipose tissue.

Journal: Journal of Clinical Medicine

Article Title: Serum and Adipose Dipeptidyl Peptidase 4 in Cardiovascular Surgery Patients: Influence of Dipeptidyl Peptidase 4 Inhibitors

doi: 10.3390/jcm11154333

Figure Lengend Snippet: Correlation between adiponectin and other parameters in serum, subcutaneous adipose tissue, and epicardial adipose tissue.

Article Snippet: Secondary antibody reactions were performed at room temperature for 1 h. The antibodies used in the assay were DPP-4 and adiponectin goat anti-mouse IgG-HRP (sc-2005, Santa Cruz Biotech-nology, Inc., Dallas, TX, USA).

Techniques: Activity Assay

Characteristics of patient groups taking DPP-4 inhibitors and those not taking them.

Journal: Journal of Clinical Medicine

Article Title: Serum and Adipose Dipeptidyl Peptidase 4 in Cardiovascular Surgery Patients: Influence of Dipeptidyl Peptidase 4 Inhibitors

doi: 10.3390/jcm11154333

Figure Lengend Snippet: Characteristics of patient groups taking DPP-4 inhibitors and those not taking them.

Article Snippet: Secondary antibody reactions were performed at room temperature for 1 h. The antibodies used in the assay were DPP-4 and adiponectin goat anti-mouse IgG-HRP (sc-2005, Santa Cruz Biotech-nology, Inc., Dallas, TX, USA).

Techniques: Biomarker Discovery, Activity Assay

Preparation and characterization of Neu-ABs and eNABs. ( A ) Schematic shows the purification of Neu-ABs through apoptosis induction and serial centrifugations, as well as the generation of eNABs. The latter process was conducted using a liposome extruder and followed two steps: (i) NABM was generated by repeated extrusion through the first filter (pore diameter: 400 nm); (ii) eNABs were generated through repeated extrusion of the mixed suspension (NABM and MSNs) through a smaller filter (pore diameter: 200 nm). ( B ) Representative SEM image of ABs derived from neutrophils. Scale bars, 1 μm. ( C ) The Annexin V and C1q staining of Neu-ABs. Scale bars, 5 μm. ( D ) Western blotting analysis of neutrophil and Neu-ABs. ( E ) Representative TEM images of MSNs and eNABs. Scale bars, 50 nm. ( F ) Size distribution of NABM, MSNs, and eNABs measured by DLS. Average diameter ( G ) and surface zeta potential ( H ) of NABM, MSNs, and eNABs (n = 3). ( I ) Representative images of the fluorescence colocalization of PKH67-labeled NABM and rhodamine-labeled MSNs in eNABs. The pure rhodamine-labeled MSNs were used as a control. Scale bars, 10 μm. ( J ) SDS-PAGE protein analysis of NABM, MSNs, and eNABs with Coomassie Blue staining. ( K ) Western blot analysis for membrane-specific protein markers. The storage stability ( L ) and the serum stability ( M ) of eNABs (n = 3). Data are presented as means ± SD. Statistical analysis between two groups was performed using unpaired two-tailed t-tests for M (** P < 0.01).

Journal: Bioactive Materials

Article Title: Engineered neutrophil apoptotic bodies ameliorate myocardial infarction by promoting macrophage efferocytosis and inflammation resolution

doi: 10.1016/j.bioactmat.2021.08.008

Figure Lengend Snippet: Preparation and characterization of Neu-ABs and eNABs. ( A ) Schematic shows the purification of Neu-ABs through apoptosis induction and serial centrifugations, as well as the generation of eNABs. The latter process was conducted using a liposome extruder and followed two steps: (i) NABM was generated by repeated extrusion through the first filter (pore diameter: 400 nm); (ii) eNABs were generated through repeated extrusion of the mixed suspension (NABM and MSNs) through a smaller filter (pore diameter: 200 nm). ( B ) Representative SEM image of ABs derived from neutrophils. Scale bars, 1 μm. ( C ) The Annexin V and C1q staining of Neu-ABs. Scale bars, 5 μm. ( D ) Western blotting analysis of neutrophil and Neu-ABs. ( E ) Representative TEM images of MSNs and eNABs. Scale bars, 50 nm. ( F ) Size distribution of NABM, MSNs, and eNABs measured by DLS. Average diameter ( G ) and surface zeta potential ( H ) of NABM, MSNs, and eNABs (n = 3). ( I ) Representative images of the fluorescence colocalization of PKH67-labeled NABM and rhodamine-labeled MSNs in eNABs. The pure rhodamine-labeled MSNs were used as a control. Scale bars, 10 μm. ( J ) SDS-PAGE protein analysis of NABM, MSNs, and eNABs with Coomassie Blue staining. ( K ) Western blot analysis for membrane-specific protein markers. The storage stability ( L ) and the serum stability ( M ) of eNABs (n = 3). Data are presented as means ± SD. Statistical analysis between two groups was performed using unpaired two-tailed t-tests for M (** P < 0.01).

Article Snippet: Fluorescence staining and flow cytometry analysis of ABs was conducted using an Annexin V-FITC apoptosis assay kit (A005-2, 7 Sea Biotech, China) and anti -C1q antibody (CL7501F, CEDARLANE).

Techniques: Purification, Generated, Suspension, Derivative Assay, Staining, Western Blot, Zeta Potential Analyzer, Fluorescence, Labeling, Control, SDS Page, Membrane, Two Tailed Test

FIG. 6. Circulating levels of SAA, insulin, leptin, and adiponectin. Plasma was collected from mice at 12 weeks after diet. A: SAA levels were measured in 12–15 mice from each group using enzyme-linked immunosorbent assay. B: Insulin levels were measured in 9–14 mice from each group using RIA. C: Leptin levels were measured in 9–11 mice from each group using RIA. D: Adiponectin levels were measured in six mice from each group by SDS-PAGE as described in RESEARCH DESIGN AND METHODS. The high–molecular weight (HMW) form of the protein was quantified using densitometric analysis and is expressed relative to the a/a;LDLR/ chow diet levels. Data are presented as means SE. Genotypes and statistics are indicated below graphs.

Journal: Diabetes

Article Title: Diet-induced increases in adiposity, but not plasma lipids, promote macrophage infiltration into white adipose tissue.

doi: 10.2337/db06-1375

Figure Lengend Snippet: FIG. 6. Circulating levels of SAA, insulin, leptin, and adiponectin. Plasma was collected from mice at 12 weeks after diet. A: SAA levels were measured in 12–15 mice from each group using enzyme-linked immunosorbent assay. B: Insulin levels were measured in 9–14 mice from each group using RIA. C: Leptin levels were measured in 9–11 mice from each group using RIA. D: Adiponectin levels were measured in six mice from each group by SDS-PAGE as described in RESEARCH DESIGN AND METHODS. The high–molecular weight (HMW) form of the protein was quantified using densitometric analysis and is expressed relative to the a/a;LDLR/ chow diet levels. Data are presented as means SE. Genotypes and statistics are indicated below graphs.

Article Snippet: Protein was transferred to nitrocellulose membranes and probed with rabbit anti-mouse adiponectin (ABCAM, Cambridge, MA) at a 1:2,000 dilution.

Techniques: Clinical Proteomics, Enzyme-linked Immunosorbent Assay, SDS Page, High Molecular Weight

Stomach tissue from 15 month V30M animal stained with Thioflavin-S, α-hTTR antibody and Congo red in consecutive sections ( Ai-Avi ). The area of Thioflavin-S and α-hTTR antibody co-localization which was included in measurements as TTR plaques is indicated in ( Avi ). Stomach tissue from 5 month V30M animal stained with stained with Thioflavin-S and α-hTTR antibody indicating solely the presence of pre-fibrillar hTTR (Bi- Biii ) ( A&B Scale bar = 75mm). C Quantification of the amyloid plaques found in the stomach measured through Thioflavin-S and α-hTTR antibody co-localization for both the V30M and V30M C1q KO mice (n = 15/age group/line). Data presented as mean ± 1SD.

Journal: PLoS ONE

Article Title: C1q ablation exacerbates amyloid deposition: A study in a transgenic mouse model of ATTRV30M amyloid neuropathy

doi: 10.1371/journal.pone.0175767

Figure Lengend Snippet: Stomach tissue from 15 month V30M animal stained with Thioflavin-S, α-hTTR antibody and Congo red in consecutive sections ( Ai-Avi ). The area of Thioflavin-S and α-hTTR antibody co-localization which was included in measurements as TTR plaques is indicated in ( Avi ). Stomach tissue from 5 month V30M animal stained with stained with Thioflavin-S and α-hTTR antibody indicating solely the presence of pre-fibrillar hTTR (Bi- Biii ) ( A&B Scale bar = 75mm). C Quantification of the amyloid plaques found in the stomach measured through Thioflavin-S and α-hTTR antibody co-localization for both the V30M and V30M C1q KO mice (n = 15/age group/line). Data presented as mean ± 1SD.

Article Snippet: Further analysis was carried out using supplementary antibodies; Fas (Santa Cruz Biotechnology anti-rabbit sc-1023 1/1000) and activated Caspase-3 (Santa Cruz Biotechnology anti-goat sc-1225 1/500), CD68 Fitch conjugated (Abcam ab53444 1/100), GRP78 (Santa Cruz Biotechnology anti-rabbit sc-13968 1/1000), C5b-9 (EMD Millipore anti-rabbit 204903 1/4,000), Properdin (Santa Cruz Biotechnology anti-mouse sc-393723 1/500) and C1q (Santa Cruz Biotechnology anti-goat sc-27661 1/250).

Techniques: Staining

hTTR immunoblotting exhibiting a single band at 14KDa ( A ). hTTR levels measured via immunoblotting in serum of V30M and V30M C1q KO animals of all three age groups indicating higher hTTR in the V30M mice and a gradual decrease in the amount of hTTR present as the animals age ( B ). hTTR levels measured via immunoblotting in stomach tissue of the V30M and V30M C1q KO animals exhibit a severe decrease in the second age group ( C ). B&C n = 15/age group/line. Data presented as mean ± 1SD.

Journal: PLoS ONE

Article Title: C1q ablation exacerbates amyloid deposition: A study in a transgenic mouse model of ATTRV30M amyloid neuropathy

doi: 10.1371/journal.pone.0175767

Figure Lengend Snippet: hTTR immunoblotting exhibiting a single band at 14KDa ( A ). hTTR levels measured via immunoblotting in serum of V30M and V30M C1q KO animals of all three age groups indicating higher hTTR in the V30M mice and a gradual decrease in the amount of hTTR present as the animals age ( B ). hTTR levels measured via immunoblotting in stomach tissue of the V30M and V30M C1q KO animals exhibit a severe decrease in the second age group ( C ). B&C n = 15/age group/line. Data presented as mean ± 1SD.

Article Snippet: Further analysis was carried out using supplementary antibodies; Fas (Santa Cruz Biotechnology anti-rabbit sc-1023 1/1000) and activated Caspase-3 (Santa Cruz Biotechnology anti-goat sc-1225 1/500), CD68 Fitch conjugated (Abcam ab53444 1/100), GRP78 (Santa Cruz Biotechnology anti-rabbit sc-13968 1/1000), C5b-9 (EMD Millipore anti-rabbit 204903 1/4,000), Properdin (Santa Cruz Biotechnology anti-mouse sc-393723 1/500) and C1q (Santa Cruz Biotechnology anti-goat sc-27661 1/250).

Techniques: Western Blot

The expression of Properdin ( A ) and C5b-9 ( B ) measured via immunoblotting in both V30M and V30M C1q KO animals stomach tissue in all three age groups exhibiting an age related increase of both markers, as well as a higher expression in the V30M C1q KO animals (n = 15/age group/line, data presented as mean ± 1SD).

Journal: PLoS ONE

Article Title: C1q ablation exacerbates amyloid deposition: A study in a transgenic mouse model of ATTRV30M amyloid neuropathy

doi: 10.1371/journal.pone.0175767

Figure Lengend Snippet: The expression of Properdin ( A ) and C5b-9 ( B ) measured via immunoblotting in both V30M and V30M C1q KO animals stomach tissue in all three age groups exhibiting an age related increase of both markers, as well as a higher expression in the V30M C1q KO animals (n = 15/age group/line, data presented as mean ± 1SD).

Article Snippet: Further analysis was carried out using supplementary antibodies; Fas (Santa Cruz Biotechnology anti-rabbit sc-1023 1/1000) and activated Caspase-3 (Santa Cruz Biotechnology anti-goat sc-1225 1/500), CD68 Fitch conjugated (Abcam ab53444 1/100), GRP78 (Santa Cruz Biotechnology anti-rabbit sc-13968 1/1000), C5b-9 (EMD Millipore anti-rabbit 204903 1/4,000), Properdin (Santa Cruz Biotechnology anti-mouse sc-393723 1/500) and C1q (Santa Cruz Biotechnology anti-goat sc-27661 1/250).

Techniques: Expressing, Western Blot

The expression of Fas protein measured by immunoblotting ( A ) in stomach tissue of both V30M and V30M C1q KO animals in all three age groups indicating an age related steady increase, as well as a higher expression in the V30M C1q KO mice. The same was observed by immunofluorescence ( B ). Similarly, the expression of Caspase-3 was also measured by immunoblotting ( C ) again indicating an age related increase with a markedly increased expression in the V30M C1q KO mice. Similar observations were made through immunofluorescence ( D ). A&C n = 15/age group/line, data presented as mean ± 1SD. B&D Scale bar = 150mm.

Journal: PLoS ONE

Article Title: C1q ablation exacerbates amyloid deposition: A study in a transgenic mouse model of ATTRV30M amyloid neuropathy

doi: 10.1371/journal.pone.0175767

Figure Lengend Snippet: The expression of Fas protein measured by immunoblotting ( A ) in stomach tissue of both V30M and V30M C1q KO animals in all three age groups indicating an age related steady increase, as well as a higher expression in the V30M C1q KO mice. The same was observed by immunofluorescence ( B ). Similarly, the expression of Caspase-3 was also measured by immunoblotting ( C ) again indicating an age related increase with a markedly increased expression in the V30M C1q KO mice. Similar observations were made through immunofluorescence ( D ). A&C n = 15/age group/line, data presented as mean ± 1SD. B&D Scale bar = 150mm.

Article Snippet: Further analysis was carried out using supplementary antibodies; Fas (Santa Cruz Biotechnology anti-rabbit sc-1023 1/1000) and activated Caspase-3 (Santa Cruz Biotechnology anti-goat sc-1225 1/500), CD68 Fitch conjugated (Abcam ab53444 1/100), GRP78 (Santa Cruz Biotechnology anti-rabbit sc-13968 1/1000), C5b-9 (EMD Millipore anti-rabbit 204903 1/4,000), Properdin (Santa Cruz Biotechnology anti-mouse sc-393723 1/500) and C1q (Santa Cruz Biotechnology anti-goat sc-27661 1/250).

Techniques: Expressing, Western Blot, Immunofluorescence

The expression of BiP protein measured by immunoblotting ( A ) in stomach tissue of both V30M and V30M C1q KO animals in all three age groups depicting an increased expression in V30M C1q KO mice of all ages. The same was observed by immunofluorescence ( B ). Furthermore, the presence of the 4-HNE was quantified via immunoblotting ( C ) in stomach tissues of both V30M and V30M C1q KO animals in all three age groups, again indicating the higher expression of 4-HNE in V30M C1q KO mice. The same was observed by immunofluorescence ( D ). A&C n = 15/age group/line, data presented as mean ± 1SD. B&D Scale bar = 150mm.

Journal: PLoS ONE

Article Title: C1q ablation exacerbates amyloid deposition: A study in a transgenic mouse model of ATTRV30M amyloid neuropathy

doi: 10.1371/journal.pone.0175767

Figure Lengend Snippet: The expression of BiP protein measured by immunoblotting ( A ) in stomach tissue of both V30M and V30M C1q KO animals in all three age groups depicting an increased expression in V30M C1q KO mice of all ages. The same was observed by immunofluorescence ( B ). Furthermore, the presence of the 4-HNE was quantified via immunoblotting ( C ) in stomach tissues of both V30M and V30M C1q KO animals in all three age groups, again indicating the higher expression of 4-HNE in V30M C1q KO mice. The same was observed by immunofluorescence ( D ). A&C n = 15/age group/line, data presented as mean ± 1SD. B&D Scale bar = 150mm.

Article Snippet: Further analysis was carried out using supplementary antibodies; Fas (Santa Cruz Biotechnology anti-rabbit sc-1023 1/1000) and activated Caspase-3 (Santa Cruz Biotechnology anti-goat sc-1225 1/500), CD68 Fitch conjugated (Abcam ab53444 1/100), GRP78 (Santa Cruz Biotechnology anti-rabbit sc-13968 1/1000), C5b-9 (EMD Millipore anti-rabbit 204903 1/4,000), Properdin (Santa Cruz Biotechnology anti-mouse sc-393723 1/500) and C1q (Santa Cruz Biotechnology anti-goat sc-27661 1/250).

Techniques: Expressing, Western Blot, Immunofluorescence

Immunofluorescence indicating the absence of the pan-macrophage marker CD68 on hTTR positive plaques from the V30M C1q KO mice contrary to V30M mice where macrophages co-localize with C1q ( A ) n = 15/age group/line, data presented as mean ± 1SD. By Western blot expression of the marker CD68 was severely decreased in stomach tissue of the V30M C1q KO mice when compared to the V30M mice ( B ), Scale bar = 30mm.

Journal: PLoS ONE

Article Title: C1q ablation exacerbates amyloid deposition: A study in a transgenic mouse model of ATTRV30M amyloid neuropathy

doi: 10.1371/journal.pone.0175767

Figure Lengend Snippet: Immunofluorescence indicating the absence of the pan-macrophage marker CD68 on hTTR positive plaques from the V30M C1q KO mice contrary to V30M mice where macrophages co-localize with C1q ( A ) n = 15/age group/line, data presented as mean ± 1SD. By Western blot expression of the marker CD68 was severely decreased in stomach tissue of the V30M C1q KO mice when compared to the V30M mice ( B ), Scale bar = 30mm.

Article Snippet: Further analysis was carried out using supplementary antibodies; Fas (Santa Cruz Biotechnology anti-rabbit sc-1023 1/1000) and activated Caspase-3 (Santa Cruz Biotechnology anti-goat sc-1225 1/500), CD68 Fitch conjugated (Abcam ab53444 1/100), GRP78 (Santa Cruz Biotechnology anti-rabbit sc-13968 1/1000), C5b-9 (EMD Millipore anti-rabbit 204903 1/4,000), Properdin (Santa Cruz Biotechnology anti-mouse sc-393723 1/500) and C1q (Santa Cruz Biotechnology anti-goat sc-27661 1/250).

Techniques: Immunofluorescence, Marker, Western Blot, Expressing

The expression of the CD88 receptor ( A ) and its ligand C5a ( B ) were measured by immunoblotting in stomach tissues of both V30M and V30M C1q KO animals in all three age groups. Both markers exhibit an astounding reduction in the V30M C1q KO mice. A&B n = 15/age group/line, data presented as mean ± 1SD.

Journal: PLoS ONE

Article Title: C1q ablation exacerbates amyloid deposition: A study in a transgenic mouse model of ATTRV30M amyloid neuropathy

doi: 10.1371/journal.pone.0175767

Figure Lengend Snippet: The expression of the CD88 receptor ( A ) and its ligand C5a ( B ) were measured by immunoblotting in stomach tissues of both V30M and V30M C1q KO animals in all three age groups. Both markers exhibit an astounding reduction in the V30M C1q KO mice. A&B n = 15/age group/line, data presented as mean ± 1SD.

Article Snippet: Further analysis was carried out using supplementary antibodies; Fas (Santa Cruz Biotechnology anti-rabbit sc-1023 1/1000) and activated Caspase-3 (Santa Cruz Biotechnology anti-goat sc-1225 1/500), CD68 Fitch conjugated (Abcam ab53444 1/100), GRP78 (Santa Cruz Biotechnology anti-rabbit sc-13968 1/1000), C5b-9 (EMD Millipore anti-rabbit 204903 1/4,000), Properdin (Santa Cruz Biotechnology anti-mouse sc-393723 1/500) and C1q (Santa Cruz Biotechnology anti-goat sc-27661 1/250).

Techniques: Expressing, Western Blot

Classical and alternative pathway activation lead to the hydrolysis of C3 initiating the formation of the membrane attack complex (MAC) and production of the chemoattractant C5a. C1q and C5a recruit and activate phagocytic cells such as macrophages through receptors located on their surfaces ( A ). In the absence of C1q, properdin expression increases along with the entire alternative pathway and the terminal MAC complex. Concurrently, the presence of CD68 positive phagocytes was decreased along with the expression of C5a anaphylatoxin and its receptor CD88 ( B ). As a result, amyloid deposition increases following C1q ablation ( b ) versus the original transgenic model ( a ).

Journal: PLoS ONE

Article Title: C1q ablation exacerbates amyloid deposition: A study in a transgenic mouse model of ATTRV30M amyloid neuropathy

doi: 10.1371/journal.pone.0175767

Figure Lengend Snippet: Classical and alternative pathway activation lead to the hydrolysis of C3 initiating the formation of the membrane attack complex (MAC) and production of the chemoattractant C5a. C1q and C5a recruit and activate phagocytic cells such as macrophages through receptors located on their surfaces ( A ). In the absence of C1q, properdin expression increases along with the entire alternative pathway and the terminal MAC complex. Concurrently, the presence of CD68 positive phagocytes was decreased along with the expression of C5a anaphylatoxin and its receptor CD88 ( B ). As a result, amyloid deposition increases following C1q ablation ( b ) versus the original transgenic model ( a ).

Article Snippet: Further analysis was carried out using supplementary antibodies; Fas (Santa Cruz Biotechnology anti-rabbit sc-1023 1/1000) and activated Caspase-3 (Santa Cruz Biotechnology anti-goat sc-1225 1/500), CD68 Fitch conjugated (Abcam ab53444 1/100), GRP78 (Santa Cruz Biotechnology anti-rabbit sc-13968 1/1000), C5b-9 (EMD Millipore anti-rabbit 204903 1/4,000), Properdin (Santa Cruz Biotechnology anti-mouse sc-393723 1/500) and C1q (Santa Cruz Biotechnology anti-goat sc-27661 1/250).

Techniques: Activation Assay, Membrane, Expressing, Transgenic Assay