mouse anti human c7 monoclonal antibody  (Hycult Biotech)


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    Structured Review

    Hycult Biotech mouse anti human c7 monoclonal antibody
    The <t>C7</t> and clusterin association was confirmed with a native-restricted anti-C7 mAb. (A) The <t>M7-HB2H</t> mAb binding target is located in the C-terminal domains (highlighted in grey) of C7. These domains participate in the formation of the MAC via interaction with the C345C domain of C5, hence, the M7-HB2H antibody would likely bind to an exposed epitope in the native form of C7 (i.e. C7 that is not involved in the assembly of the MAC). The C7 gene contains 18 exons, each exon codes for a specific region of the C7 domain, which corresponds to the exon coding region displayed above. The boundary phase refers to the phase of the corresponding intron. (B) C7 purified from NHS-BioIVT with anti-C7 mAb, M7-HB2H, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with M7-HB2H. Protein composition of the bands visualized in (B) was analzyed by mass spectrometry and protein abundance was quantified for the (C) 100 kDa band and the (D) 75 kDa band. (E) The C7 aa residues detected in the 75 kDa band (3B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 47% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blot (B) is representative of at least three independent experiments. Images were taken using Proxima C16 Phi. Figure (A) modified from Massri et al., 2022 .
    Mouse Anti Human C7 Monoclonal Antibody, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti human c7 monoclonal antibody/product/Hycult Biotech
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse anti human c7 monoclonal antibody - by Bioz Stars, 2024-04
    94/100 stars

    Images

    1) Product Images from "Complement C7 and clusterin form a complex in circulation"

    Article Title: Complement C7 and clusterin form a complex in circulation

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2024.1330095

    The C7 and clusterin association was confirmed with a native-restricted anti-C7 mAb. (A) The M7-HB2H mAb binding target is located in the C-terminal domains (highlighted in grey) of C7. These domains participate in the formation of the MAC via interaction with the C345C domain of C5, hence, the M7-HB2H antibody would likely bind to an exposed epitope in the native form of C7 (i.e. C7 that is not involved in the assembly of the MAC). The C7 gene contains 18 exons, each exon codes for a specific region of the C7 domain, which corresponds to the exon coding region displayed above. The boundary phase refers to the phase of the corresponding intron. (B) C7 purified from NHS-BioIVT with anti-C7 mAb, M7-HB2H, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with M7-HB2H. Protein composition of the bands visualized in (B) was analzyed by mass spectrometry and protein abundance was quantified for the (C) 100 kDa band and the (D) 75 kDa band. (E) The C7 aa residues detected in the 75 kDa band (3B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 47% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blot (B) is representative of at least three independent experiments. Images were taken using Proxima C16 Phi. Figure (A) modified from Massri et al., 2022 .
    Figure Legend Snippet: The C7 and clusterin association was confirmed with a native-restricted anti-C7 mAb. (A) The M7-HB2H mAb binding target is located in the C-terminal domains (highlighted in grey) of C7. These domains participate in the formation of the MAC via interaction with the C345C domain of C5, hence, the M7-HB2H antibody would likely bind to an exposed epitope in the native form of C7 (i.e. C7 that is not involved in the assembly of the MAC). The C7 gene contains 18 exons, each exon codes for a specific region of the C7 domain, which corresponds to the exon coding region displayed above. The boundary phase refers to the phase of the corresponding intron. (B) C7 purified from NHS-BioIVT with anti-C7 mAb, M7-HB2H, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with M7-HB2H. Protein composition of the bands visualized in (B) was analzyed by mass spectrometry and protein abundance was quantified for the (C) 100 kDa band and the (D) 75 kDa band. (E) The C7 aa residues detected in the 75 kDa band (3B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 47% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blot (B) is representative of at least three independent experiments. Images were taken using Proxima C16 Phi. Figure (A) modified from Massri et al., 2022 .

    Techniques Used: Binding Assay, Purification, SDS Page, Western Blot, Mass Spectrometry, Modification

    Detection of a variant form of C7 and screening of C7 aa residues in the visualized variant. (A) C7 purified from NHS-MUI with the anti-C7 pAb, P7, was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with the anti-C7 mAb, M7-WU4-15. (B) C7 purified from NHS-MUI with M7-WU4-15 was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with M7-WU4-15. (C) Coomassie staining of C7 purified from NHS-MUI with the anti-C7 mAb, M7-WU4-15, and separated by SDS-PAGE gel under non-reducing conditions. (D) The C7 aa residues identified by LC-MS in the 100 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 76% of the total C7 polypeptide chain. (E) The C7 aa residues detected in the 75 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 37% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blots and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.
    Figure Legend Snippet: Detection of a variant form of C7 and screening of C7 aa residues in the visualized variant. (A) C7 purified from NHS-MUI with the anti-C7 pAb, P7, was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with the anti-C7 mAb, M7-WU4-15. (B) C7 purified from NHS-MUI with M7-WU4-15 was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with M7-WU4-15. (C) Coomassie staining of C7 purified from NHS-MUI with the anti-C7 mAb, M7-WU4-15, and separated by SDS-PAGE gel under non-reducing conditions. (D) The C7 aa residues identified by LC-MS in the 100 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 76% of the total C7 polypeptide chain. (E) The C7 aa residues detected in the 75 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 37% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blots and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.

    Techniques Used: Variant Assay, Purification, SDS Page, Western Blot, Staining, Liquid Chromatography with Mass Spectroscopy

    Clusterin is the most abundant protein detected in the 75 kDa band of purified C7. Protein composition of the bands visualized for C7 purified with pAb P7 ( <xref ref-type= Figure 2A ) was analzyed by mass spectrometry and protein abundance was quantified for the (A) 100 kDa band and the (B) 75 kDa band. Protein composition of the bands visualized for C7 purified with mAb M7-WU4-15 ( Figure 2B ) was analyzed by mass spectrometry and protein abundance was quantified in the (C) 100 kDa band and the (D) 75 kDa band. " title="... detected in the 75 kDa band of purified C7. Protein composition of the bands visualized for C7 ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Clusterin is the most abundant protein detected in the 75 kDa band of purified C7. Protein composition of the bands visualized for C7 purified with pAb P7 ( Figure 2A ) was analzyed by mass spectrometry and protein abundance was quantified for the (A) 100 kDa band and the (B) 75 kDa band. Protein composition of the bands visualized for C7 purified with mAb M7-WU4-15 ( Figure 2B ) was analyzed by mass spectrometry and protein abundance was quantified in the (C) 100 kDa band and the (D) 75 kDa band.

    Techniques Used: Purification, Mass Spectrometry

    Clusterin purified from NHS with polyclonal and monoclonal antibodies contained low levels of C7. (A) Clusterin purified from NHS-MUI with anti-clusterin pAb, PC, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with the anti-clusterin mAb, MC. The clusterin band on the left was from the 1 st eluate acquired from the antibody-coupled column, while the band on the right was from a 2 nd , consecutive elution step. (B) Coomassie staining of clusterin purified from NHS-MUI with the anti-clusterin pAb, PC, and separated by SDS-PAGE gel under non-reducing conditions. (C) Protein composition of the 75 kDa band visualized in (A) was analyzed by mass spectrometry and protein abundance was quantified. (D) Protein compostion of the 75 kDa band (not shown) from C7 purified with the anti-clusterin mAb, MC-2D5, was analyzed by mass spectrometry and protein abundance was quantified. Results from purified clusterin in (B, C) were acquiered from the 1 st eluate. Western blot and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.
    Figure Legend Snippet: Clusterin purified from NHS with polyclonal and monoclonal antibodies contained low levels of C7. (A) Clusterin purified from NHS-MUI with anti-clusterin pAb, PC, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with the anti-clusterin mAb, MC. The clusterin band on the left was from the 1 st eluate acquired from the antibody-coupled column, while the band on the right was from a 2 nd , consecutive elution step. (B) Coomassie staining of clusterin purified from NHS-MUI with the anti-clusterin pAb, PC, and separated by SDS-PAGE gel under non-reducing conditions. (C) Protein composition of the 75 kDa band visualized in (A) was analyzed by mass spectrometry and protein abundance was quantified. (D) Protein compostion of the 75 kDa band (not shown) from C7 purified with the anti-clusterin mAb, MC-2D5, was analyzed by mass spectrometry and protein abundance was quantified. Results from purified clusterin in (B, C) were acquiered from the 1 st eluate. Western blot and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.

    Techniques Used: Purification, SDS Page, Western Blot, Staining, Mass Spectrometry

    Western blot analysis reveals strong association between C7 and clusterin. (A, B) Indicated proteins were separated by SDS-PAGE under (A) non-reducing or (B) reducing conditions and immunoblots were probed with the anti-C7 mAb, M7-HB2H. (C, D) Indicated proteins were separated by SDS-PAGE under (C) non-reducing or (D) reducing conditions and immunoblots were probed with the anti-clusterin mAb, MC-2D5. Western blots are representative of at least three independent experiments. Images were taken using Proxima C16 Phi.
    Figure Legend Snippet: Western blot analysis reveals strong association between C7 and clusterin. (A, B) Indicated proteins were separated by SDS-PAGE under (A) non-reducing or (B) reducing conditions and immunoblots were probed with the anti-C7 mAb, M7-HB2H. (C, D) Indicated proteins were separated by SDS-PAGE under (C) non-reducing or (D) reducing conditions and immunoblots were probed with the anti-clusterin mAb, MC-2D5. Western blots are representative of at least three independent experiments. Images were taken using Proxima C16 Phi.

    Techniques Used: Western Blot, SDS Page

    C7-CLU complex was detected in purified C7 and measured in healthy serum and plasma donors. (A) OD signal of C7-CLU complex measured in C7 purified from NHS-BioIVT with the anti-C7 mAb, M7-HB2H, at the indicated concentrations. (B) C7-CLU complex measured in indicated samples. Each data point denotes an independent measurement. (C) Concentration of C7-CLU complex measured zymosan-activated NHS at indicated time points. Asterisks denote statistically significant change from non-activated NHS. (D) Concentration of C7-CLU complex in EDTA plasma from healthy donors. Data are shown as mean ± SD. The CV values in all presented datasets were below 10%. Groups were compared using one-way ANOVA followed by Tukey’s multiple comparisons test. One-way ANOVA, followed by Dunnett’s multiple comparison test was used when comparing zymosan-activated NHS against non-activated control. *** p < 0.001, **** p < 0.0001. Some error bars cannot be shown because the SD is too small.
    Figure Legend Snippet: C7-CLU complex was detected in purified C7 and measured in healthy serum and plasma donors. (A) OD signal of C7-CLU complex measured in C7 purified from NHS-BioIVT with the anti-C7 mAb, M7-HB2H, at the indicated concentrations. (B) C7-CLU complex measured in indicated samples. Each data point denotes an independent measurement. (C) Concentration of C7-CLU complex measured zymosan-activated NHS at indicated time points. Asterisks denote statistically significant change from non-activated NHS. (D) Concentration of C7-CLU complex in EDTA plasma from healthy donors. Data are shown as mean ± SD. The CV values in all presented datasets were below 10%. Groups were compared using one-way ANOVA followed by Tukey’s multiple comparisons test. One-way ANOVA, followed by Dunnett’s multiple comparison test was used when comparing zymosan-activated NHS against non-activated control. *** p < 0.001, **** p < 0.0001. Some error bars cannot be shown because the SD is too small.

    Techniques Used: Purification, Concentration Assay, Comparison

    C7 and CLU co-elute in high molecular weight complexes. (A) Fractions of pooled NHS (F30-F62) were obtained by size exclusion chromatography and subsequently separated by SDS-PAGE under non-reducing conditions and immunoblots were probed with (B) anti-C7 mAb, M7-HB2H or (C) anti-clusterin mAb, MC-2D5. (D) Summary of (B, C) illustrating the fractions that were either positive or negative for C7 and clusterin. ± indicates fractions where a very faint band was detected due to minute amounts of the protein. (E) Concentration of the C7-CLU complex and native C7 in serum fractions. Note the difference between the y-axis scales, which translates to small concentrations of complexed C7, relative to native C7. NHS, normal human serum.
    Figure Legend Snippet: C7 and CLU co-elute in high molecular weight complexes. (A) Fractions of pooled NHS (F30-F62) were obtained by size exclusion chromatography and subsequently separated by SDS-PAGE under non-reducing conditions and immunoblots were probed with (B) anti-C7 mAb, M7-HB2H or (C) anti-clusterin mAb, MC-2D5. (D) Summary of (B, C) illustrating the fractions that were either positive or negative for C7 and clusterin. ± indicates fractions where a very faint band was detected due to minute amounts of the protein. (E) Concentration of the C7-CLU complex and native C7 in serum fractions. Note the difference between the y-axis scales, which translates to small concentrations of complexed C7, relative to native C7. NHS, normal human serum.

    Techniques Used: Molecular Weight, Size-exclusion Chromatography, SDS Page, Western Blot, Concentration Assay

    mouse anti human c7 monoclonal antibody  (Hycult Biotech)


    Bioz Verified Symbol Hycult Biotech is a verified supplier
    Bioz Manufacturer Symbol Hycult Biotech manufactures this product  
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  • Team
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  • 94

    Structured Review

    Hycult Biotech mouse anti human c7 monoclonal antibody
    The <t>C7</t> and clusterin association was confirmed with a native-restricted anti-C7 mAb. (A) The <t>M7-HB2H</t> mAb binding target is located in the C-terminal domains (highlighted in grey) of C7. These domains participate in the formation of the MAC via interaction with the C345C domain of C5, hence, the M7-HB2H antibody would likely bind to an exposed epitope in the native form of C7 (i.e. C7 that is not involved in the assembly of the MAC). The C7 gene contains 18 exons, each exon codes for a specific region of the C7 domain, which corresponds to the exon coding region displayed above. The boundary phase refers to the phase of the corresponding intron. (B) C7 purified from NHS-BioIVT with anti-C7 mAb, M7-HB2H, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with M7-HB2H. Protein composition of the bands visualized in (B) was analzyed by mass spectrometry and protein abundance was quantified for the (C) 100 kDa band and the (D) 75 kDa band. (E) The C7 aa residues detected in the 75 kDa band (3B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 47% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blot (B) is representative of at least three independent experiments. Images were taken using Proxima C16 Phi. Figure (A) modified from Massri et al., 2022 .
    Mouse Anti Human C7 Monoclonal Antibody, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti human c7 monoclonal antibody/product/Hycult Biotech
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse anti human c7 monoclonal antibody - by Bioz Stars, 2024-04
    94/100 stars

    Images

    1) Product Images from "Complement C7 and clusterin form a complex in circulation"

    Article Title: Complement C7 and clusterin form a complex in circulation

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2024.1330095

    The C7 and clusterin association was confirmed with a native-restricted anti-C7 mAb. (A) The M7-HB2H mAb binding target is located in the C-terminal domains (highlighted in grey) of C7. These domains participate in the formation of the MAC via interaction with the C345C domain of C5, hence, the M7-HB2H antibody would likely bind to an exposed epitope in the native form of C7 (i.e. C7 that is not involved in the assembly of the MAC). The C7 gene contains 18 exons, each exon codes for a specific region of the C7 domain, which corresponds to the exon coding region displayed above. The boundary phase refers to the phase of the corresponding intron. (B) C7 purified from NHS-BioIVT with anti-C7 mAb, M7-HB2H, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with M7-HB2H. Protein composition of the bands visualized in (B) was analzyed by mass spectrometry and protein abundance was quantified for the (C) 100 kDa band and the (D) 75 kDa band. (E) The C7 aa residues detected in the 75 kDa band (3B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 47% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blot (B) is representative of at least three independent experiments. Images were taken using Proxima C16 Phi. Figure (A) modified from Massri et al., 2022 .
    Figure Legend Snippet: The C7 and clusterin association was confirmed with a native-restricted anti-C7 mAb. (A) The M7-HB2H mAb binding target is located in the C-terminal domains (highlighted in grey) of C7. These domains participate in the formation of the MAC via interaction with the C345C domain of C5, hence, the M7-HB2H antibody would likely bind to an exposed epitope in the native form of C7 (i.e. C7 that is not involved in the assembly of the MAC). The C7 gene contains 18 exons, each exon codes for a specific region of the C7 domain, which corresponds to the exon coding region displayed above. The boundary phase refers to the phase of the corresponding intron. (B) C7 purified from NHS-BioIVT with anti-C7 mAb, M7-HB2H, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with M7-HB2H. Protein composition of the bands visualized in (B) was analzyed by mass spectrometry and protein abundance was quantified for the (C) 100 kDa band and the (D) 75 kDa band. (E) The C7 aa residues detected in the 75 kDa band (3B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 47% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blot (B) is representative of at least three independent experiments. Images were taken using Proxima C16 Phi. Figure (A) modified from Massri et al., 2022 .

    Techniques Used: Binding Assay, Purification, SDS Page, Western Blot, Mass Spectrometry, Modification

    Detection of a variant form of C7 and screening of C7 aa residues in the visualized variant. (A) C7 purified from NHS-MUI with the anti-C7 pAb, P7, was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with the anti-C7 mAb, M7-WU4-15. (B) C7 purified from NHS-MUI with M7-WU4-15 was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with M7-WU4-15. (C) Coomassie staining of C7 purified from NHS-MUI with the anti-C7 mAb, M7-WU4-15, and separated by SDS-PAGE gel under non-reducing conditions. (D) The C7 aa residues identified by LC-MS in the 100 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 76% of the total C7 polypeptide chain. (E) The C7 aa residues detected in the 75 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 37% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blots and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.
    Figure Legend Snippet: Detection of a variant form of C7 and screening of C7 aa residues in the visualized variant. (A) C7 purified from NHS-MUI with the anti-C7 pAb, P7, was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with the anti-C7 mAb, M7-WU4-15. (B) C7 purified from NHS-MUI with M7-WU4-15 was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with M7-WU4-15. (C) Coomassie staining of C7 purified from NHS-MUI with the anti-C7 mAb, M7-WU4-15, and separated by SDS-PAGE gel under non-reducing conditions. (D) The C7 aa residues identified by LC-MS in the 100 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 76% of the total C7 polypeptide chain. (E) The C7 aa residues detected in the 75 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 37% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blots and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.

    Techniques Used: Variant Assay, Purification, SDS Page, Western Blot, Staining, Liquid Chromatography with Mass Spectroscopy

    Clusterin is the most abundant protein detected in the 75 kDa band of purified C7. Protein composition of the bands visualized for C7 purified with pAb P7 ( <xref ref-type= Figure 2A ) was analzyed by mass spectrometry and protein abundance was quantified for the (A) 100 kDa band and the (B) 75 kDa band. Protein composition of the bands visualized for C7 purified with mAb M7-WU4-15 ( Figure 2B ) was analyzed by mass spectrometry and protein abundance was quantified in the (C) 100 kDa band and the (D) 75 kDa band. " title="... detected in the 75 kDa band of purified C7. Protein composition of the bands visualized for C7 ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Clusterin is the most abundant protein detected in the 75 kDa band of purified C7. Protein composition of the bands visualized for C7 purified with pAb P7 ( Figure 2A ) was analzyed by mass spectrometry and protein abundance was quantified for the (A) 100 kDa band and the (B) 75 kDa band. Protein composition of the bands visualized for C7 purified with mAb M7-WU4-15 ( Figure 2B ) was analyzed by mass spectrometry and protein abundance was quantified in the (C) 100 kDa band and the (D) 75 kDa band.

    Techniques Used: Purification, Mass Spectrometry

    Clusterin purified from NHS with polyclonal and monoclonal antibodies contained low levels of C7. (A) Clusterin purified from NHS-MUI with anti-clusterin pAb, PC, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with the anti-clusterin mAb, MC. The clusterin band on the left was from the 1 st eluate acquired from the antibody-coupled column, while the band on the right was from a 2 nd , consecutive elution step. (B) Coomassie staining of clusterin purified from NHS-MUI with the anti-clusterin pAb, PC, and separated by SDS-PAGE gel under non-reducing conditions. (C) Protein composition of the 75 kDa band visualized in (A) was analyzed by mass spectrometry and protein abundance was quantified. (D) Protein compostion of the 75 kDa band (not shown) from C7 purified with the anti-clusterin mAb, MC-2D5, was analyzed by mass spectrometry and protein abundance was quantified. Results from purified clusterin in (B, C) were acquiered from the 1 st eluate. Western blot and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.
    Figure Legend Snippet: Clusterin purified from NHS with polyclonal and monoclonal antibodies contained low levels of C7. (A) Clusterin purified from NHS-MUI with anti-clusterin pAb, PC, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with the anti-clusterin mAb, MC. The clusterin band on the left was from the 1 st eluate acquired from the antibody-coupled column, while the band on the right was from a 2 nd , consecutive elution step. (B) Coomassie staining of clusterin purified from NHS-MUI with the anti-clusterin pAb, PC, and separated by SDS-PAGE gel under non-reducing conditions. (C) Protein composition of the 75 kDa band visualized in (A) was analyzed by mass spectrometry and protein abundance was quantified. (D) Protein compostion of the 75 kDa band (not shown) from C7 purified with the anti-clusterin mAb, MC-2D5, was analyzed by mass spectrometry and protein abundance was quantified. Results from purified clusterin in (B, C) were acquiered from the 1 st eluate. Western blot and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.

    Techniques Used: Purification, SDS Page, Western Blot, Staining, Mass Spectrometry

    Western blot analysis reveals strong association between C7 and clusterin. (A, B) Indicated proteins were separated by SDS-PAGE under (A) non-reducing or (B) reducing conditions and immunoblots were probed with the anti-C7 mAb, M7-HB2H. (C, D) Indicated proteins were separated by SDS-PAGE under (C) non-reducing or (D) reducing conditions and immunoblots were probed with the anti-clusterin mAb, MC-2D5. Western blots are representative of at least three independent experiments. Images were taken using Proxima C16 Phi.
    Figure Legend Snippet: Western blot analysis reveals strong association between C7 and clusterin. (A, B) Indicated proteins were separated by SDS-PAGE under (A) non-reducing or (B) reducing conditions and immunoblots were probed with the anti-C7 mAb, M7-HB2H. (C, D) Indicated proteins were separated by SDS-PAGE under (C) non-reducing or (D) reducing conditions and immunoblots were probed with the anti-clusterin mAb, MC-2D5. Western blots are representative of at least three independent experiments. Images were taken using Proxima C16 Phi.

    Techniques Used: Western Blot, SDS Page

    C7-CLU complex was detected in purified C7 and measured in healthy serum and plasma donors. (A) OD signal of C7-CLU complex measured in C7 purified from NHS-BioIVT with the anti-C7 mAb, M7-HB2H, at the indicated concentrations. (B) C7-CLU complex measured in indicated samples. Each data point denotes an independent measurement. (C) Concentration of C7-CLU complex measured zymosan-activated NHS at indicated time points. Asterisks denote statistically significant change from non-activated NHS. (D) Concentration of C7-CLU complex in EDTA plasma from healthy donors. Data are shown as mean ± SD. The CV values in all presented datasets were below 10%. Groups were compared using one-way ANOVA followed by Tukey’s multiple comparisons test. One-way ANOVA, followed by Dunnett’s multiple comparison test was used when comparing zymosan-activated NHS against non-activated control. *** p < 0.001, **** p < 0.0001. Some error bars cannot be shown because the SD is too small.
    Figure Legend Snippet: C7-CLU complex was detected in purified C7 and measured in healthy serum and plasma donors. (A) OD signal of C7-CLU complex measured in C7 purified from NHS-BioIVT with the anti-C7 mAb, M7-HB2H, at the indicated concentrations. (B) C7-CLU complex measured in indicated samples. Each data point denotes an independent measurement. (C) Concentration of C7-CLU complex measured zymosan-activated NHS at indicated time points. Asterisks denote statistically significant change from non-activated NHS. (D) Concentration of C7-CLU complex in EDTA plasma from healthy donors. Data are shown as mean ± SD. The CV values in all presented datasets were below 10%. Groups were compared using one-way ANOVA followed by Tukey’s multiple comparisons test. One-way ANOVA, followed by Dunnett’s multiple comparison test was used when comparing zymosan-activated NHS against non-activated control. *** p < 0.001, **** p < 0.0001. Some error bars cannot be shown because the SD is too small.

    Techniques Used: Purification, Concentration Assay, Comparison

    C7 and CLU co-elute in high molecular weight complexes. (A) Fractions of pooled NHS (F30-F62) were obtained by size exclusion chromatography and subsequently separated by SDS-PAGE under non-reducing conditions and immunoblots were probed with (B) anti-C7 mAb, M7-HB2H or (C) anti-clusterin mAb, MC-2D5. (D) Summary of (B, C) illustrating the fractions that were either positive or negative for C7 and clusterin. ± indicates fractions where a very faint band was detected due to minute amounts of the protein. (E) Concentration of the C7-CLU complex and native C7 in serum fractions. Note the difference between the y-axis scales, which translates to small concentrations of complexed C7, relative to native C7. NHS, normal human serum.
    Figure Legend Snippet: C7 and CLU co-elute in high molecular weight complexes. (A) Fractions of pooled NHS (F30-F62) were obtained by size exclusion chromatography and subsequently separated by SDS-PAGE under non-reducing conditions and immunoblots were probed with (B) anti-C7 mAb, M7-HB2H or (C) anti-clusterin mAb, MC-2D5. (D) Summary of (B, C) illustrating the fractions that were either positive or negative for C7 and clusterin. ± indicates fractions where a very faint band was detected due to minute amounts of the protein. (E) Concentration of the C7-CLU complex and native C7 in serum fractions. Note the difference between the y-axis scales, which translates to small concentrations of complexed C7, relative to native C7. NHS, normal human serum.

    Techniques Used: Molecular Weight, Size-exclusion Chromatography, SDS Page, Western Blot, Concentration Assay

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    Hycult Biotech mouse anti human c7 monoclonal antibody
    The <t>C7</t> and clusterin association was confirmed with a native-restricted anti-C7 mAb. (A) The <t>M7-HB2H</t> mAb binding target is located in the C-terminal domains (highlighted in grey) of C7. These domains participate in the formation of the MAC via interaction with the C345C domain of C5, hence, the M7-HB2H antibody would likely bind to an exposed epitope in the native form of C7 (i.e. C7 that is not involved in the assembly of the MAC). The C7 gene contains 18 exons, each exon codes for a specific region of the C7 domain, which corresponds to the exon coding region displayed above. The boundary phase refers to the phase of the corresponding intron. (B) C7 purified from NHS-BioIVT with anti-C7 mAb, M7-HB2H, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with M7-HB2H. Protein composition of the bands visualized in (B) was analzyed by mass spectrometry and protein abundance was quantified for the (C) 100 kDa band and the (D) 75 kDa band. (E) The C7 aa residues detected in the 75 kDa band (3B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 47% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blot (B) is representative of at least three independent experiments. Images were taken using Proxima C16 Phi. Figure (A) modified from Massri et al., 2022 .
    Mouse Anti Human C7 Monoclonal Antibody, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    The C7 and clusterin association was confirmed with a native-restricted anti-C7 mAb. (A) The M7-HB2H mAb binding target is located in the C-terminal domains (highlighted in grey) of C7. These domains participate in the formation of the MAC via interaction with the C345C domain of C5, hence, the M7-HB2H antibody would likely bind to an exposed epitope in the native form of C7 (i.e. C7 that is not involved in the assembly of the MAC). The C7 gene contains 18 exons, each exon codes for a specific region of the C7 domain, which corresponds to the exon coding region displayed above. The boundary phase refers to the phase of the corresponding intron. (B) C7 purified from NHS-BioIVT with anti-C7 mAb, M7-HB2H, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with M7-HB2H. Protein composition of the bands visualized in (B) was analzyed by mass spectrometry and protein abundance was quantified for the (C) 100 kDa band and the (D) 75 kDa band. (E) The C7 aa residues detected in the 75 kDa band (3B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 47% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blot (B) is representative of at least three independent experiments. Images were taken using Proxima C16 Phi. Figure (A) modified from Massri et al., 2022 .

    Journal: Frontiers in Immunology

    Article Title: Complement C7 and clusterin form a complex in circulation

    doi: 10.3389/fimmu.2024.1330095

    Figure Lengend Snippet: The C7 and clusterin association was confirmed with a native-restricted anti-C7 mAb. (A) The M7-HB2H mAb binding target is located in the C-terminal domains (highlighted in grey) of C7. These domains participate in the formation of the MAC via interaction with the C345C domain of C5, hence, the M7-HB2H antibody would likely bind to an exposed epitope in the native form of C7 (i.e. C7 that is not involved in the assembly of the MAC). The C7 gene contains 18 exons, each exon codes for a specific region of the C7 domain, which corresponds to the exon coding region displayed above. The boundary phase refers to the phase of the corresponding intron. (B) C7 purified from NHS-BioIVT with anti-C7 mAb, M7-HB2H, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with M7-HB2H. Protein composition of the bands visualized in (B) was analzyed by mass spectrometry and protein abundance was quantified for the (C) 100 kDa band and the (D) 75 kDa band. (E) The C7 aa residues detected in the 75 kDa band (3B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 47% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blot (B) is representative of at least three independent experiments. Images were taken using Proxima C16 Phi. Figure (A) modified from Massri et al., 2022 .

    Article Snippet: Antibodies: goat anti-human C7 polyclonal antibody [P7] ( ); mouse anti-human C7 monoclonal antibody [M7-WU4-15] (cat# HM2277, Hycult Biotech, Uden, Netherlands); mouse anti-human C7 monoclonal antibody [M7-HB2H] (cat# HM2421, Hycult Biotech), goat anti-human clusterin polyclonal antibody [PC] (Sigma-Aldrich, St. Louis, MO, USA); mouse anti-human clusterin monoclonal antibody [MC] (Sinobiological, Beijing, China), mouse anti-human clusterin monoclonal antibody [MC-2D5] (cat# HM2435, Hycult Biotech); goat anti-mouse HRP-conjugated IgG antibody (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Binding Assay, Purification, SDS Page, Western Blot, Mass Spectrometry, Modification

    Detection of a variant form of C7 and screening of C7 aa residues in the visualized variant. (A) C7 purified from NHS-MUI with the anti-C7 pAb, P7, was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with the anti-C7 mAb, M7-WU4-15. (B) C7 purified from NHS-MUI with M7-WU4-15 was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with M7-WU4-15. (C) Coomassie staining of C7 purified from NHS-MUI with the anti-C7 mAb, M7-WU4-15, and separated by SDS-PAGE gel under non-reducing conditions. (D) The C7 aa residues identified by LC-MS in the 100 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 76% of the total C7 polypeptide chain. (E) The C7 aa residues detected in the 75 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 37% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blots and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.

    Journal: Frontiers in Immunology

    Article Title: Complement C7 and clusterin form a complex in circulation

    doi: 10.3389/fimmu.2024.1330095

    Figure Lengend Snippet: Detection of a variant form of C7 and screening of C7 aa residues in the visualized variant. (A) C7 purified from NHS-MUI with the anti-C7 pAb, P7, was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with the anti-C7 mAb, M7-WU4-15. (B) C7 purified from NHS-MUI with M7-WU4-15 was separated by SDS-PAGE under non-reducing conditions and immunoblot was probed with M7-WU4-15. (C) Coomassie staining of C7 purified from NHS-MUI with the anti-C7 mAb, M7-WU4-15, and separated by SDS-PAGE gel under non-reducing conditions. (D) The C7 aa residues identified by LC-MS in the 100 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 76% of the total C7 polypeptide chain. (E) The C7 aa residues detected in the 75 kDa band (1B) are in bold and underlined, along with an illustration of the screened residues in the C7 polypeptide chain highlighted in grey. The screened aa residues are 37% of the total C7 polypeptide chain. Black arrows indicate the exon/intron boundaries. Western blots and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.

    Article Snippet: Antibodies: goat anti-human C7 polyclonal antibody [P7] ( ); mouse anti-human C7 monoclonal antibody [M7-WU4-15] (cat# HM2277, Hycult Biotech, Uden, Netherlands); mouse anti-human C7 monoclonal antibody [M7-HB2H] (cat# HM2421, Hycult Biotech), goat anti-human clusterin polyclonal antibody [PC] (Sigma-Aldrich, St. Louis, MO, USA); mouse anti-human clusterin monoclonal antibody [MC] (Sinobiological, Beijing, China), mouse anti-human clusterin monoclonal antibody [MC-2D5] (cat# HM2435, Hycult Biotech); goat anti-mouse HRP-conjugated IgG antibody (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Variant Assay, Purification, SDS Page, Western Blot, Staining, Liquid Chromatography with Mass Spectroscopy

    Clusterin is the most abundant protein detected in the 75 kDa band of purified C7. Protein composition of the bands visualized for C7 purified with pAb P7 ( <xref ref-type= Figure 2A ) was analzyed by mass spectrometry and protein abundance was quantified for the (A) 100 kDa band and the (B) 75 kDa band. Protein composition of the bands visualized for C7 purified with mAb M7-WU4-15 ( Figure 2B ) was analyzed by mass spectrometry and protein abundance was quantified in the (C) 100 kDa band and the (D) 75 kDa band. " width="100%" height="100%">

    Journal: Frontiers in Immunology

    Article Title: Complement C7 and clusterin form a complex in circulation

    doi: 10.3389/fimmu.2024.1330095

    Figure Lengend Snippet: Clusterin is the most abundant protein detected in the 75 kDa band of purified C7. Protein composition of the bands visualized for C7 purified with pAb P7 ( Figure 2A ) was analzyed by mass spectrometry and protein abundance was quantified for the (A) 100 kDa band and the (B) 75 kDa band. Protein composition of the bands visualized for C7 purified with mAb M7-WU4-15 ( Figure 2B ) was analyzed by mass spectrometry and protein abundance was quantified in the (C) 100 kDa band and the (D) 75 kDa band.

    Article Snippet: Antibodies: goat anti-human C7 polyclonal antibody [P7] ( ); mouse anti-human C7 monoclonal antibody [M7-WU4-15] (cat# HM2277, Hycult Biotech, Uden, Netherlands); mouse anti-human C7 monoclonal antibody [M7-HB2H] (cat# HM2421, Hycult Biotech), goat anti-human clusterin polyclonal antibody [PC] (Sigma-Aldrich, St. Louis, MO, USA); mouse anti-human clusterin monoclonal antibody [MC] (Sinobiological, Beijing, China), mouse anti-human clusterin monoclonal antibody [MC-2D5] (cat# HM2435, Hycult Biotech); goat anti-mouse HRP-conjugated IgG antibody (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Purification, Mass Spectrometry

    Clusterin purified from NHS with polyclonal and monoclonal antibodies contained low levels of C7. (A) Clusterin purified from NHS-MUI with anti-clusterin pAb, PC, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with the anti-clusterin mAb, MC. The clusterin band on the left was from the 1 st eluate acquired from the antibody-coupled column, while the band on the right was from a 2 nd , consecutive elution step. (B) Coomassie staining of clusterin purified from NHS-MUI with the anti-clusterin pAb, PC, and separated by SDS-PAGE gel under non-reducing conditions. (C) Protein composition of the 75 kDa band visualized in (A) was analyzed by mass spectrometry and protein abundance was quantified. (D) Protein compostion of the 75 kDa band (not shown) from C7 purified with the anti-clusterin mAb, MC-2D5, was analyzed by mass spectrometry and protein abundance was quantified. Results from purified clusterin in (B, C) were acquiered from the 1 st eluate. Western blot and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.

    Journal: Frontiers in Immunology

    Article Title: Complement C7 and clusterin form a complex in circulation

    doi: 10.3389/fimmu.2024.1330095

    Figure Lengend Snippet: Clusterin purified from NHS with polyclonal and monoclonal antibodies contained low levels of C7. (A) Clusterin purified from NHS-MUI with anti-clusterin pAb, PC, was separated by SDS-PAGE under non-reducing conditions and the immunoblot was probed with the anti-clusterin mAb, MC. The clusterin band on the left was from the 1 st eluate acquired from the antibody-coupled column, while the band on the right was from a 2 nd , consecutive elution step. (B) Coomassie staining of clusterin purified from NHS-MUI with the anti-clusterin pAb, PC, and separated by SDS-PAGE gel under non-reducing conditions. (C) Protein composition of the 75 kDa band visualized in (A) was analyzed by mass spectrometry and protein abundance was quantified. (D) Protein compostion of the 75 kDa band (not shown) from C7 purified with the anti-clusterin mAb, MC-2D5, was analyzed by mass spectrometry and protein abundance was quantified. Results from purified clusterin in (B, C) were acquiered from the 1 st eluate. Western blot and coomassie staining are representative of at least three independent experiments. Images were taken using the ImageQuant™ LAS 400 camera system.

    Article Snippet: Antibodies: goat anti-human C7 polyclonal antibody [P7] ( ); mouse anti-human C7 monoclonal antibody [M7-WU4-15] (cat# HM2277, Hycult Biotech, Uden, Netherlands); mouse anti-human C7 monoclonal antibody [M7-HB2H] (cat# HM2421, Hycult Biotech), goat anti-human clusterin polyclonal antibody [PC] (Sigma-Aldrich, St. Louis, MO, USA); mouse anti-human clusterin monoclonal antibody [MC] (Sinobiological, Beijing, China), mouse anti-human clusterin monoclonal antibody [MC-2D5] (cat# HM2435, Hycult Biotech); goat anti-mouse HRP-conjugated IgG antibody (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Purification, SDS Page, Western Blot, Staining, Mass Spectrometry

    Western blot analysis reveals strong association between C7 and clusterin. (A, B) Indicated proteins were separated by SDS-PAGE under (A) non-reducing or (B) reducing conditions and immunoblots were probed with the anti-C7 mAb, M7-HB2H. (C, D) Indicated proteins were separated by SDS-PAGE under (C) non-reducing or (D) reducing conditions and immunoblots were probed with the anti-clusterin mAb, MC-2D5. Western blots are representative of at least three independent experiments. Images were taken using Proxima C16 Phi.

    Journal: Frontiers in Immunology

    Article Title: Complement C7 and clusterin form a complex in circulation

    doi: 10.3389/fimmu.2024.1330095

    Figure Lengend Snippet: Western blot analysis reveals strong association between C7 and clusterin. (A, B) Indicated proteins were separated by SDS-PAGE under (A) non-reducing or (B) reducing conditions and immunoblots were probed with the anti-C7 mAb, M7-HB2H. (C, D) Indicated proteins were separated by SDS-PAGE under (C) non-reducing or (D) reducing conditions and immunoblots were probed with the anti-clusterin mAb, MC-2D5. Western blots are representative of at least three independent experiments. Images were taken using Proxima C16 Phi.

    Article Snippet: Antibodies: goat anti-human C7 polyclonal antibody [P7] ( ); mouse anti-human C7 monoclonal antibody [M7-WU4-15] (cat# HM2277, Hycult Biotech, Uden, Netherlands); mouse anti-human C7 monoclonal antibody [M7-HB2H] (cat# HM2421, Hycult Biotech), goat anti-human clusterin polyclonal antibody [PC] (Sigma-Aldrich, St. Louis, MO, USA); mouse anti-human clusterin monoclonal antibody [MC] (Sinobiological, Beijing, China), mouse anti-human clusterin monoclonal antibody [MC-2D5] (cat# HM2435, Hycult Biotech); goat anti-mouse HRP-conjugated IgG antibody (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Western Blot, SDS Page

    C7-CLU complex was detected in purified C7 and measured in healthy serum and plasma donors. (A) OD signal of C7-CLU complex measured in C7 purified from NHS-BioIVT with the anti-C7 mAb, M7-HB2H, at the indicated concentrations. (B) C7-CLU complex measured in indicated samples. Each data point denotes an independent measurement. (C) Concentration of C7-CLU complex measured zymosan-activated NHS at indicated time points. Asterisks denote statistically significant change from non-activated NHS. (D) Concentration of C7-CLU complex in EDTA plasma from healthy donors. Data are shown as mean ± SD. The CV values in all presented datasets were below 10%. Groups were compared using one-way ANOVA followed by Tukey’s multiple comparisons test. One-way ANOVA, followed by Dunnett’s multiple comparison test was used when comparing zymosan-activated NHS against non-activated control. *** p < 0.001, **** p < 0.0001. Some error bars cannot be shown because the SD is too small.

    Journal: Frontiers in Immunology

    Article Title: Complement C7 and clusterin form a complex in circulation

    doi: 10.3389/fimmu.2024.1330095

    Figure Lengend Snippet: C7-CLU complex was detected in purified C7 and measured in healthy serum and plasma donors. (A) OD signal of C7-CLU complex measured in C7 purified from NHS-BioIVT with the anti-C7 mAb, M7-HB2H, at the indicated concentrations. (B) C7-CLU complex measured in indicated samples. Each data point denotes an independent measurement. (C) Concentration of C7-CLU complex measured zymosan-activated NHS at indicated time points. Asterisks denote statistically significant change from non-activated NHS. (D) Concentration of C7-CLU complex in EDTA plasma from healthy donors. Data are shown as mean ± SD. The CV values in all presented datasets were below 10%. Groups were compared using one-way ANOVA followed by Tukey’s multiple comparisons test. One-way ANOVA, followed by Dunnett’s multiple comparison test was used when comparing zymosan-activated NHS against non-activated control. *** p < 0.001, **** p < 0.0001. Some error bars cannot be shown because the SD is too small.

    Article Snippet: Antibodies: goat anti-human C7 polyclonal antibody [P7] ( ); mouse anti-human C7 monoclonal antibody [M7-WU4-15] (cat# HM2277, Hycult Biotech, Uden, Netherlands); mouse anti-human C7 monoclonal antibody [M7-HB2H] (cat# HM2421, Hycult Biotech), goat anti-human clusterin polyclonal antibody [PC] (Sigma-Aldrich, St. Louis, MO, USA); mouse anti-human clusterin monoclonal antibody [MC] (Sinobiological, Beijing, China), mouse anti-human clusterin monoclonal antibody [MC-2D5] (cat# HM2435, Hycult Biotech); goat anti-mouse HRP-conjugated IgG antibody (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Purification, Concentration Assay, Comparison

    C7 and CLU co-elute in high molecular weight complexes. (A) Fractions of pooled NHS (F30-F62) were obtained by size exclusion chromatography and subsequently separated by SDS-PAGE under non-reducing conditions and immunoblots were probed with (B) anti-C7 mAb, M7-HB2H or (C) anti-clusterin mAb, MC-2D5. (D) Summary of (B, C) illustrating the fractions that were either positive or negative for C7 and clusterin. ± indicates fractions where a very faint band was detected due to minute amounts of the protein. (E) Concentration of the C7-CLU complex and native C7 in serum fractions. Note the difference between the y-axis scales, which translates to small concentrations of complexed C7, relative to native C7. NHS, normal human serum.

    Journal: Frontiers in Immunology

    Article Title: Complement C7 and clusterin form a complex in circulation

    doi: 10.3389/fimmu.2024.1330095

    Figure Lengend Snippet: C7 and CLU co-elute in high molecular weight complexes. (A) Fractions of pooled NHS (F30-F62) were obtained by size exclusion chromatography and subsequently separated by SDS-PAGE under non-reducing conditions and immunoblots were probed with (B) anti-C7 mAb, M7-HB2H or (C) anti-clusterin mAb, MC-2D5. (D) Summary of (B, C) illustrating the fractions that were either positive or negative for C7 and clusterin. ± indicates fractions where a very faint band was detected due to minute amounts of the protein. (E) Concentration of the C7-CLU complex and native C7 in serum fractions. Note the difference between the y-axis scales, which translates to small concentrations of complexed C7, relative to native C7. NHS, normal human serum.

    Article Snippet: Antibodies: goat anti-human C7 polyclonal antibody [P7] ( ); mouse anti-human C7 monoclonal antibody [M7-WU4-15] (cat# HM2277, Hycult Biotech, Uden, Netherlands); mouse anti-human C7 monoclonal antibody [M7-HB2H] (cat# HM2421, Hycult Biotech), goat anti-human clusterin polyclonal antibody [PC] (Sigma-Aldrich, St. Louis, MO, USA); mouse anti-human clusterin monoclonal antibody [MC] (Sinobiological, Beijing, China), mouse anti-human clusterin monoclonal antibody [MC-2D5] (cat# HM2435, Hycult Biotech); goat anti-mouse HRP-conjugated IgG antibody (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Molecular Weight, Size-exclusion Chromatography, SDS Page, Western Blot, Concentration Assay