Review

rabbit anti-human collagen iii antibody (Absolute Biotech Inc)

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Absolute Biotech Inc rabbit anti-human collagen iii antibody

( A–C ) Immunostaining <t>of</t> <t>collagen</t> <t>III</t> in E14.5 mouse brain sections of wild type, Col3a1 −/− , and Gpr56 −/− revealed an expression of collagen III (red) in the meninges and pial basement membrane of wild type and Gpr56 −/− brains. Deletion of Col3a1 completely abolished the expression of collagen III. Scale bar, 100 µm. ( D–F ) Strong GPR56 N binding was detected in meninges and pial basement membrane of wild type and Gpr56 −/− , but not Col3a1 −/− mouse brains. Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm.

Rabbit Anti Human Collagen Iii Antibody, supplied by Absolute Biotech Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit anti-human collagen iii antibody/product/Absolute Biotech Inc
Average 90 stars, based on 1 article reviews

rabbit anti-human collagen iii antibody - by Bioz Stars, 2026-03

90/100 stars

Images

1) Product Images from "Disease-Associated Mutations Prevent GPR56-Collagen III Interaction"

Article Title: Disease-Associated Mutations Prevent GPR56-Collagen III Interaction

Journal: PLoS ONE

doi: 10.1371/journal.pone.0029818

( A–C ) Immunostaining of collagen III in E14.5 mouse brain sections of wild type, Col3a1 −/− , and Gpr56 −/− revealed an expression of collagen III (red) in the meninges and pial basement membrane of wild type and Gpr56 −/− brains. Deletion of Col3a1 completely abolished the expression of collagen III. Scale bar, 100 µm. ( D–F ) Strong GPR56 N binding was detected in meninges and pial basement membrane of wild type and Gpr56 −/− , but not Col3a1 −/− mouse brains. Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm.

Figure Legend Snippet: ( A–C ) Immunostaining of collagen III in E14.5 mouse brain sections of wild type, Col3a1 −/− , and Gpr56 −/− revealed an expression of collagen III (red) in the meninges and pial basement membrane of wild type and Gpr56 −/− brains. Deletion of Col3a1 completely abolished the expression of collagen III. Scale bar, 100 µm. ( D–F ) Strong GPR56 N binding was detected in meninges and pial basement membrane of wild type and Gpr56 −/− , but not Col3a1 −/− mouse brains. Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm.

Techniques Used: Immunostaining, Expressing, Binding Assay

( A ) The truncated GPR56 N -hFc fusion protein constructs are schematically shown, as well as the full length GPR56 protein with its identified N-glycosylation sites. ( B ) The fusion constructs were transfected into HEK-293T cells. Secreted proteins in the conditioned media were collected, concentrated, and verified by western blot. ( C–J ) Putative ligand binding on E14.5 mouse cortex. The shortest fragment with a specific binding pattern (green) is the truncated GPR56 N -hFc fusion protein containing aa 27–160 (H). Nuclear counterstain was performed by Hoechst 33342 (blue). Scale bar, 200 µm. ( K ) The binding of collagen III and various truncated GPR56 N -hFc was confirmed by co-IP. Anti-hFc immunoblot served as a loading control.

Figure Legend Snippet: ( A ) The truncated GPR56 N -hFc fusion protein constructs are schematically shown, as well as the full length GPR56 protein with its identified N-glycosylation sites. ( B ) The fusion constructs were transfected into HEK-293T cells. Secreted proteins in the conditioned media were collected, concentrated, and verified by western blot. ( C–J ) Putative ligand binding on E14.5 mouse cortex. The shortest fragment with a specific binding pattern (green) is the truncated GPR56 N -hFc fusion protein containing aa 27–160 (H). Nuclear counterstain was performed by Hoechst 33342 (blue). Scale bar, 200 µm. ( K ) The binding of collagen III and various truncated GPR56 N -hFc was confirmed by co-IP. Anti-hFc immunoblot served as a loading control.

Techniques Used: Construct, Transfection, Western Blot, Ligand Binding Assay, Binding Assay, Co-Immunoprecipitation Assay

( A ) The schematic representation of two separate N-glycosylation mutations within the GPR56 ligand binding domain is shown. ( B ) Secreted fusion proteins in the conditioned media were collected, concentrated, and verified by western blot. ( C–E ) Putative ligand binding on E14.5 mouse cortex. The N-glycosylation mutation did not impair GPR56 ligand binding (green). Nuclear counterstain was performed by Hoechst 33342 (blue). Scale bar, 200 µm. ( F ) The binding ability of the two N-glycosylation mutants to collagen III was confirmed by co-IP. Anti-hFc immunoblot served as a loading control.

Figure Legend Snippet: ( A ) The schematic representation of two separate N-glycosylation mutations within the GPR56 ligand binding domain is shown. ( B ) Secreted fusion proteins in the conditioned media were collected, concentrated, and verified by western blot. ( C–E ) Putative ligand binding on E14.5 mouse cortex. The N-glycosylation mutation did not impair GPR56 ligand binding (green). Nuclear counterstain was performed by Hoechst 33342 (blue). Scale bar, 200 µm. ( F ) The binding ability of the two N-glycosylation mutants to collagen III was confirmed by co-IP. Anti-hFc immunoblot served as a loading control.

Techniques Used: Ligand Binding Assay, Western Blot, Mutagenesis, Binding Assay, Co-Immunoprecipitation Assay

( A ) GPR56 N -hFc aa 27–160 schematic. The positions of the disease-associated mutations within the ligand binding domain are shown. ( B ) Secreted fusion proteins in the conditioned media were collected, concentrated, and verified by a western blot. ( C–G ) Putative ligand binding on E14.5 mouse cortex. Each of the four disease-associated mutations completely killed the receptor-ligand binding ability in contrast to the strong binding signal (green) displayed by the wild type fusion protein ( C ). Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm. ( H ) The impaired binding of disease-associated mutants to collagen III was confirmed by co-IP. Anti-hFc immunoblot served as a loading control.

Figure Legend Snippet: ( A ) GPR56 N -hFc aa 27–160 schematic. The positions of the disease-associated mutations within the ligand binding domain are shown. ( B ) Secreted fusion proteins in the conditioned media were collected, concentrated, and verified by a western blot. ( C–G ) Putative ligand binding on E14.5 mouse cortex. Each of the four disease-associated mutations completely killed the receptor-ligand binding ability in contrast to the strong binding signal (green) displayed by the wild type fusion protein ( C ). Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm. ( H ) The impaired binding of disease-associated mutants to collagen III was confirmed by co-IP. Anti-hFc immunoblot served as a loading control.

Techniques Used: Ligand Binding Assay, Western Blot, Binding Assay, Co-Immunoprecipitation Assay

( A–G ) Neurospheres were generated and plated on PDL-coated dishes in regular neurosphere culture medium. After 20 h, the cultures were changed to experimental medium containing collagen III (84 nM) with or without wild type or mutant GPR56 proteins (90 nM), or carrier solution (acetic acid). Representative images are shown. Scale bar, 100 µm. ( H ) The degree of collagen III-mediated migration inhibition was quantified as a percentage of the migrating neurospheres. Data are presented as mean ± SD, n = 3 for each group. *P<0.01, Student t test.

Figure Legend Snippet: ( A–G ) Neurospheres were generated and plated on PDL-coated dishes in regular neurosphere culture medium. After 20 h, the cultures were changed to experimental medium containing collagen III (84 nM) with or without wild type or mutant GPR56 proteins (90 nM), or carrier solution (acetic acid). Representative images are shown. Scale bar, 100 µm. ( H ) The degree of collagen III-mediated migration inhibition was quantified as a percentage of the migrating neurospheres. Data are presented as mean ± SD, n = 3 for each group. *P<0.01, Student t test.

Techniques Used: Generated, Mutagenesis, Migration, Inhibition

( A ) Human GPR56 N -hFc aa 27–382 schematic. The positions of the disease-associated mutations are shown. ( B ) Co-IP of human GPR56 N and purified human collagen III. Collagen III was detected in GPR56 IP complex, but not in mutant GPR56 complexes. Anti-hFc immunoblot served as a loading control. ( C–F ) Putative ligand binding of human GPR56 N -hFc on E14.5 mouse cortex. Strong binding signal was detected (green) with wild type human GPR56 N -hFc protein staining, whereas a loss of signal occurred in mutant proteins. Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm.

Figure Legend Snippet: ( A ) Human GPR56 N -hFc aa 27–382 schematic. The positions of the disease-associated mutations are shown. ( B ) Co-IP of human GPR56 N and purified human collagen III. Collagen III was detected in GPR56 IP complex, but not in mutant GPR56 complexes. Anti-hFc immunoblot served as a loading control. ( C–F ) Putative ligand binding of human GPR56 N -hFc on E14.5 mouse cortex. Strong binding signal was detected (green) with wild type human GPR56 N -hFc protein staining, whereas a loss of signal occurred in mutant proteins. Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm.

Techniques Used: Co-Immunoprecipitation Assay, Purification, Mutagenesis, Western Blot, Ligand Binding Assay, Binding Assay, Staining

Image Search Results

Journal: PLoS ONE

Article Title: Disease-Associated Mutations Prevent GPR56-Collagen III Interaction

doi: 10.1371/journal.pone.0029818

Figure Lengend Snippet: ( A–C ) Immunostaining of collagen III in E14.5 mouse brain sections of wild type, Col3a1 −/− , and Gpr56 −/− revealed an expression of collagen III (red) in the meninges and pial basement membrane of wild type and Gpr56 −/− brains. Deletion of Col3a1 completely abolished the expression of collagen III. Scale bar, 100 µm. ( D–F ) Strong GPR56 N binding was detected in meninges and pial basement membrane of wild type and Gpr56 −/− , but not Col3a1 −/− mouse brains. Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm.

Article Snippet: Immunocomplexes were subjected to SDS-PAGE and western blot using rabbit anti-human collagen III antibody (Lifespan Biosciences), and rabbit anti-human IgG Fc antibody (Thermo Scientific) following standard protocols.

Techniques: Immunostaining, Expressing, Binding Assay

Journal: PLoS ONE

Article Title: Disease-Associated Mutations Prevent GPR56-Collagen III Interaction

doi: 10.1371/journal.pone.0029818

Figure Lengend Snippet: ( A ) The truncated GPR56 N -hFc fusion protein constructs are schematically shown, as well as the full length GPR56 protein with its identified N-glycosylation sites. ( B ) The fusion constructs were transfected into HEK-293T cells. Secreted proteins in the conditioned media were collected, concentrated, and verified by western blot. ( C–J ) Putative ligand binding on E14.5 mouse cortex. The shortest fragment with a specific binding pattern (green) is the truncated GPR56 N -hFc fusion protein containing aa 27–160 (H). Nuclear counterstain was performed by Hoechst 33342 (blue). Scale bar, 200 µm. ( K ) The binding of collagen III and various truncated GPR56 N -hFc was confirmed by co-IP. Anti-hFc immunoblot served as a loading control.

Techniques: Construct, Transfection, Western Blot, Ligand Binding Assay, Binding Assay, Co-Immunoprecipitation Assay

Journal: PLoS ONE

Article Title: Disease-Associated Mutations Prevent GPR56-Collagen III Interaction

doi: 10.1371/journal.pone.0029818

Figure Lengend Snippet: ( A ) The schematic representation of two separate N-glycosylation mutations within the GPR56 ligand binding domain is shown. ( B ) Secreted fusion proteins in the conditioned media were collected, concentrated, and verified by western blot. ( C–E ) Putative ligand binding on E14.5 mouse cortex. The N-glycosylation mutation did not impair GPR56 ligand binding (green). Nuclear counterstain was performed by Hoechst 33342 (blue). Scale bar, 200 µm. ( F ) The binding ability of the two N-glycosylation mutants to collagen III was confirmed by co-IP. Anti-hFc immunoblot served as a loading control.

Techniques: Ligand Binding Assay, Western Blot, Mutagenesis, Binding Assay, Co-Immunoprecipitation Assay

Journal: PLoS ONE

Article Title: Disease-Associated Mutations Prevent GPR56-Collagen III Interaction

doi: 10.1371/journal.pone.0029818

Figure Lengend Snippet: ( A ) GPR56 N -hFc aa 27–160 schematic. The positions of the disease-associated mutations within the ligand binding domain are shown. ( B ) Secreted fusion proteins in the conditioned media were collected, concentrated, and verified by a western blot. ( C–G ) Putative ligand binding on E14.5 mouse cortex. Each of the four disease-associated mutations completely killed the receptor-ligand binding ability in contrast to the strong binding signal (green) displayed by the wild type fusion protein ( C ). Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm. ( H ) The impaired binding of disease-associated mutants to collagen III was confirmed by co-IP. Anti-hFc immunoblot served as a loading control.

Techniques: Ligand Binding Assay, Western Blot, Binding Assay, Co-Immunoprecipitation Assay

Journal: PLoS ONE

Article Title: Disease-Associated Mutations Prevent GPR56-Collagen III Interaction

doi: 10.1371/journal.pone.0029818

Figure Lengend Snippet: ( A–G ) Neurospheres were generated and plated on PDL-coated dishes in regular neurosphere culture medium. After 20 h, the cultures were changed to experimental medium containing collagen III (84 nM) with or without wild type or mutant GPR56 proteins (90 nM), or carrier solution (acetic acid). Representative images are shown. Scale bar, 100 µm. ( H ) The degree of collagen III-mediated migration inhibition was quantified as a percentage of the migrating neurospheres. Data are presented as mean ± SD, n = 3 for each group. *P<0.01, Student t test.

Techniques: Generated, Mutagenesis, Migration, Inhibition

Journal: PLoS ONE

Article Title: Disease-Associated Mutations Prevent GPR56-Collagen III Interaction

doi: 10.1371/journal.pone.0029818

Figure Lengend Snippet: ( A ) Human GPR56 N -hFc aa 27–382 schematic. The positions of the disease-associated mutations are shown. ( B ) Co-IP of human GPR56 N and purified human collagen III. Collagen III was detected in GPR56 IP complex, but not in mutant GPR56 complexes. Anti-hFc immunoblot served as a loading control. ( C–F ) Putative ligand binding of human GPR56 N -hFc on E14.5 mouse cortex. Strong binding signal was detected (green) with wild type human GPR56 N -hFc protein staining, whereas a loss of signal occurred in mutant proteins. Nuclear counterstain was performed with Hoechst 33342 (blue). Scale bar, 200 µm.

Techniques: Co-Immunoprecipitation Assay, Purification, Mutagenesis, Western Blot, Ligand Binding Assay, Binding Assay, Staining

Review

Structured Review

Images

1) Product Images from "Disease-Associated Mutations Prevent GPR56-Collagen III Interaction"

Similar Products

Image Search Results