SMC-116 Search Results


mouse anti human cd74  (StressMarq)
91
StressMarq mouse anti human cd74
Figure 1. Functional Characterization of CTSS Y132D Mutation in FL (A) Distribution of CTSS mutations in 299 FL patients. (B) The total number of FL and DLBCL patients and the frequency of the Y132D mutation in the reported studies. (C) Stacked barplot indicating the percentage of patients with CTSS WT and mutated (Y132D/N). (D) Schematic representation of tyrosine (Y) 132 amino acid localization on CTSS binding site, and tridimensional structure of the proteins, colored according to the amino acid electrostatic potential. (E) Western blot of recombinant of CTSS-His WT and mutated CTSS-His Y132D using an anti-His-tag antibody. M, marker. (F) Quantification of western blot signals of CTSS mature protein normalized to the pro-CTSS signal (n = 3). (G) Graphical representation of <t>CD74</t> sequence between amino acids 89 and 121 and fluorescence resonance energy transfer (FRET) experimental design. The CTSS substrate is highlighted in blue, the arrow indicates the exact cleavage site, and the CLIP sequence is shown in green. (H) Representative FRET experiment with recombinant CTSS-His-WT and CTSS-His-Y132D. Signal Intensity normalized to the background (n = 3). (I) Quantification FRET emission normalized to CTSS WT signals (n = 6). The p value was calculated using a paired t test. (F, H, and I) Data are presented as mean ± standard deviation. See also Figure S1 and Tables S1, S2, and S3.
Mouse Anti Human Cd74, supplied by StressMarq, 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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mouse anti human cd74 - by Bioz Stars, 2026-02
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Figure 1. Functional Characterization of CTSS Y132D Mutation in FL (A) Distribution of CTSS mutations in 299 FL patients. (B) The total number of FL and DLBCL patients and the frequency of the Y132D mutation in the reported studies. (C) Stacked barplot indicating the percentage of patients with CTSS WT and mutated (Y132D/N). (D) Schematic representation of tyrosine (Y) 132 amino acid localization on CTSS binding site, and tridimensional structure of the proteins, colored according to the amino acid electrostatic potential. (E) Western blot of recombinant of CTSS-His WT and mutated CTSS-His Y132D using an anti-His-tag antibody. M, marker. (F) Quantification of western blot signals of CTSS mature protein normalized to the pro-CTSS signal (n = 3). (G) Graphical representation of CD74 sequence between amino acids 89 and 121 and fluorescence resonance energy transfer (FRET) experimental design. The CTSS substrate is highlighted in blue, the arrow indicates the exact cleavage site, and the CLIP sequence is shown in green. (H) Representative FRET experiment with recombinant CTSS-His-WT and CTSS-His-Y132D. Signal Intensity normalized to the background (n = 3). (I) Quantification FRET emission normalized to CTSS WT signals (n = 6). The p value was calculated using a paired t test. (F, H, and I) Data are presented as mean ± standard deviation. See also Figure S1 and Tables S1, S2, and S3.

Journal: Cancer cell

Article Title: Cathepsin S Regulates Antigen Processing and T Cell Activity in Non-Hodgkin Lymphoma.

doi: 10.1016/j.ccell.2020.03.016

Figure Lengend Snippet: Figure 1. Functional Characterization of CTSS Y132D Mutation in FL (A) Distribution of CTSS mutations in 299 FL patients. (B) The total number of FL and DLBCL patients and the frequency of the Y132D mutation in the reported studies. (C) Stacked barplot indicating the percentage of patients with CTSS WT and mutated (Y132D/N). (D) Schematic representation of tyrosine (Y) 132 amino acid localization on CTSS binding site, and tridimensional structure of the proteins, colored according to the amino acid electrostatic potential. (E) Western blot of recombinant of CTSS-His WT and mutated CTSS-His Y132D using an anti-His-tag antibody. M, marker. (F) Quantification of western blot signals of CTSS mature protein normalized to the pro-CTSS signal (n = 3). (G) Graphical representation of CD74 sequence between amino acids 89 and 121 and fluorescence resonance energy transfer (FRET) experimental design. The CTSS substrate is highlighted in blue, the arrow indicates the exact cleavage site, and the CLIP sequence is shown in green. (H) Representative FRET experiment with recombinant CTSS-His-WT and CTSS-His-Y132D. Signal Intensity normalized to the background (n = 3). (I) Quantification FRET emission normalized to CTSS WT signals (n = 6). The p value was calculated using a paired t test. (F, H, and I) Data are presented as mean ± standard deviation. See also Figure S1 and Tables S1, S2, and S3.

Article Snippet: After blocking in 5% milk (Applichem, cat #A0830) in PBS-0.1%Tween (Fisher scientific, cat #BP337), membranes were incubated overnight in 5% milk in PBS-Tween with the following primary antibodies: goat anti-human Cathepsin S (RD, cat #AF1183, 1:2000), Cathepsin B (D1C7Y) XP Rabbit (Cell signaling mAb #31718), rabbit anti-mouse Cathepsin S (Sino Biological, cat #50769-R054, 1:1000), mouse anti-human CD74 (PIN.1, StressMarq, cat #SMC-116, diluted 1:1000), rat-anti-mouse CD74 (clone ln-1, BD biosciences, cat #555317, 1:1000), rabbit anti-his-Tag (Cell Signaling, cat #D3I10, dilute 1:1000), mouse anti-human alpha-Tubulin (clone B-5-1-2, Sigma Aldrich, cat#T6072, diluted 1:10000), anti-beta actin (clone 8H10D10, ThermoFisher Scientific, cat# MA5-15452, 1:1000).

Techniques: Functional Assay, Mutagenesis, Binding Assay, Western Blot, Recombinant, Marker, Sequencing, Förster Resonance Energy Transfer, Standard Deviation