mouse anti human clusterin monoclonal antibody (Hycult Biotech)


Structured Review

Mouse Anti Human Clusterin 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 clusterin monoclonal antibody/product/Hycult Biotech
Average 94 stars, based on 1 article reviews
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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

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

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 (
Techniques Used: Purification, Mass Spectrometry

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

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

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