rabbit anti cd44  (Boster Bio)

Journal: Journal of Nanobiotechnology

Article Title: Low-dose X-ray-activated radiodynamic therapy via a lutetium-coordinated nanoplatform synergizing PARP inhibition and ferroptosis

doi: 10.1186/s12951-026-04027-8

Figure Lengend Snippet: Physicochemical characterization, stability, and drug release profile of BPNS@Lu 3+ /Lap-CMV. (a) Hydrodynamic size distribution of BPNS@Lu 3+ /Lap-CMV. (b) Zeta potential of BPNS, BPNS@Lu 3+ , BPNS@Lu 3+ /Lap, CMV, and BPNS@Lu 3+ /Lap-CMV ( n = 3). (c) UV–vis absorption spectra of Lap, BPNS/Lap, BPNS@Lu 3+ /Lap-CMV and BPNS. (d) Raman scattering spectra of BPNS, BPNS@Lu 3+ /Lap, BPNS@Lu 3+ /Lap-CMV. (e) Full-survey XPS spectrum and (f) high-resolution Lu 4 d XPS spectrum of BPNS@Lu 3+ /Lap-CMV. (g) Western blot analysis of the membrane marker CD44 and the nuclear protein histone H1t in (1) 4T1 cells, (2) CMs, (3) CMV, (4) BPNS@Lu 3+ /Lap, and (5) BPNS@Lu 3+ /Lap-CMV. (h) Protein concentration of CMV and BPNS@Lu 3+ /Lap-CMV by BCA assay. (i) CLSM images of cellular uptake of BPNS@Lu 3+ /Lap-CMV. Cy5 (red) represents the BPNS@Lu 3+ /Lap core, DiO (green) represents the tumor membrane shell, and DAPI (blue) stains the cell nuclei. (j) TEM images and elemental mapping images of BPNS, BPNS@Lu 3+ , BPNS@Lu 3+ /Lap, and BPNS@Lu 3+ /Lap-CMV (scale bar = 200 nm). (k) Colloidal stability of bare BPNS and (l) BPNS@Lu 3+ /Lap in aqueous solution over a 9-day period. (m) Cumulative release profiles of Lu 3+ and (n) Lap from BPNS@Lu 3+ /Lap-CMV under physiological (pH 7.4), acidic (pH6.0, pH 4.8), and chelating (with EDTA) conditions over 96 h (n = 3). Data are presented as mean ± standard deviation

Article Snippet: Rabbit anti-H1t antibody (catalog No. bs-1413R), and Rabbit anti-CD44 antibody (catalog No. bs-4916R) were purchased from Bioss (Beijing, China).

Techniques: Zeta Potential Analyzer, Western Blot, Membrane, Marker, Protein Concentration, BIA-KA, Standard Deviation

Journal: iScience

Article Title: pH-responsive CaCO 3 nanoplatform amplifies SDT via calcium overload-ROS loop for deep tumor therapy

doi: 10.1016/j.isci.2026.115082

Figure Lengend Snippet: Synthesis process and mechanism diagram of HA/CaCO 3 @Ce6 (A) Schematic of the functional pattern of HA/CaCO 3 @Ce6. (B) Tumor microenvironment-responsive calcium-based nanoplatform enables CD44-targeted modulation, improves acidic tumor niche, and amplifies mitochondrial Ca 2+ overload-mediated ROS production to trigger immunogenic cell death, thereby potentiating SDT efficacy.

Article Snippet: Anti-Mouse CD44 Rabbit Recombinant Antibody , Sanying Biotechnology , Cat No. 15675-1-AP; RRID: AB_2076198.

Techniques: Functional Assay

Journal: iScience

Article Title: pH-responsive CaCO 3 nanoplatform amplifies SDT via calcium overload-ROS loop for deep tumor therapy

doi: 10.1016/j.isci.2026.115082

Figure Lengend Snippet: In vitro HA-mediated targeting performance and the antitumor effects of HA/CaCO 3 @Ce6 (A) Flow cytometry analysis of CD44 receptor expression on the membrane surface of the different liver cancer cells. (B) Quantitative analysis of CD44 receptor expression on the membrane surface of the different liver cancer cells. Data are expressed as the mean ± SD ( n = 3), ∗∗∗p < 0.001 by Student’s t test. (C) CLSM images of Hepa1-6 cells stained with Fluo-4 after incubations with PBS, CaCO 3 , CaCO 3 @Ce6, and HA/CaCO 3 @Ce6 for 6 h. Scale bars, 100 μm. (D) Quantitative analysis of fluorescence intensity of Hepa1-6 cells stained with Fluo-4 after incubations with PBS, CaCO 3 , CaCO 3 @Ce6, and HA/CaCO 3 @Ce6 (G1–G4) for 6 h, respectively. Data are expressed as the mean ± SD ( n = 3). ∗∗∗p < 0.001 by Student’s t test. (E) Cell viability of Hepa1-6 cells treated with PBS, CaCO 3 , CaCO 3 @Ce6, and HA/CaCO 3 @Ce6 with different concentrations for 24 h. Data are expressed as the mean ± SD ( n = 3). ∗∗∗p < 0.001 by Student’s t test. (F) Cell viability of Hepa1-6 cells incubated with PBS, CaCO 3 , CaCO 3 @Ce6, and HA/CaCO 3 @Ce6 for 6 h and irradiated with different US intensity for 3 min. Data are expressed as the mean ± SD ( n = 3), ∗∗∗p < 0.001 by Student’s t test. (G) FCM patterns of apoptotic cells in Hepa1-6 cells with different treatments. (H) Quantitative analysis of apoptotic cells in Hepa1-6 cells with different treatments. G1–G6 represent PBS, CaCO 3 , CaCO 3 @Ce6, CaCO 3 @Ce6 + US, HA/CaCO 3 @Ce6 + US, and Ce6 + US, respectively. Data are expressed as the mean ± SD ( n = 3), ∗∗p ˂ 0.05; ∗∗∗p < 0.001 by Student’s t test. CLSM, confocal laser scanning microscopy; US, ultrasound.

Article Snippet: Anti-Mouse CD44 Rabbit Recombinant Antibody , Sanying Biotechnology , Cat No. 15675-1-AP; RRID: AB_2076198.

Techniques: In Vitro, Flow Cytometry, Expressing, Membrane, Staining, Fluorescence, Incubation, Irradiation, Confocal Laser Scanning Microscopy

Journal: Redox Biology

Article Title: Tumor-intrinsic redox programming drives an SPP1-CD44 axis of immune suppression in uveal melanoma

doi: 10.1016/j.redox.2026.104011

Figure Lengend Snippet: Intercellular communication networks between melanoma cells and T cells. (A, B) Number (A) and strength (B) of interactions among annotated tumor and T cell types. (C) Scatter plots illustrating the incoming and outgoing interaction strengths of the indicated cell types. (D) Heatmaps displaying representative outgoing (left) and incoming (right) signaling patterns among 14 cell types. (E) Hierarchical plot showing the inferred intracellular communication network of SPP1 signaling between annotated tumor and T cell types. (F) Violin plots comparing SPP1 expression level among five melanoma subtypes; ∗∗∗∗P < 0.0001. (G) Bar plot showing the major ligand-receptor pairs involved in SPP1 signaling. (H) Representative immunofluorescence images showing SPP1-CD44 ligand-receptor pairs in UM cohort (n = 7). HMB45 (green), SPP1 (yellow), CD8 (magenta), and CD44 (pink). Scale bar, 20 μm.

Article Snippet: After blocked with 3 % BSA, the 4 μm serial sections were incubated with primary antibody at 4 °C overnight: SPP1 (Proteintech, 22952-1-AP), HMB45 (Abcam, ab787), CD8 (CST, 98941), and CD44 (CST, 37259).

Techniques: Expressing, Immunofluorescence

Journal: Redox Biology

Article Title: Tumor-intrinsic redox programming drives an SPP1-CD44 axis of immune suppression in uveal melanoma

doi: 10.1016/j.redox.2026.104011

Figure Lengend Snippet: Redox-dependent SPP1 secretion drives immune suppression (A) ELISA measurement of SPP1 levels in conditioned medium from indicated UM cell lines. ∗P < 0.05, ∗∗∗∗P < 0.0001. (B) Immunoblot validation of SPP1 overexpression in UM cells. (C) ELISA analysis of secreted SPP1 following SPP1 overexpression. ∗∗∗∗P < 0.0001. (D) CCK-8 assay measuring proliferation of UM cells upon SPP1 overexpression. (E) Colony formation (top) and trans well assays (bottom) evaluating the clonogenic growth and invasive potential of UM cells upon SPP1 overexpression. (F) Schematic overview of the UM-CD8 + T cell coculture system. (G) Flow cytometry analysis of Ki-67 and IFN-γ expression levels in CD8 + T cells under different coculture conditions. ∗P < 0.05, ∗∗P < 0.01. (H) Proposed model of the SPP1-CD44 signaling axis in UM progression. (I) CCK-8 assay showing inhibitory effects of Mito-LND on MP46 cell viability. ∗∗P < 0.01. (J) OCR analysis assessing mitochondrial respiration in MP46 cells following Mito-LND treatment. ∗∗∗P < 0.001, ∗∗∗∗P < 0.0001. (K) ROS levels in UM cells after Mito-LND treatment. Scale bar, 200 μm. ∗P < 0.05. (L) Immunoblot analysis of SPP1 expression under oxidative stress induced by Tert -Butyl hydroperoxide solution (TBHP) or Mito-LND. (M) ELISA quantification of secreted SPP1 levels after Mito-LND treatment. ∗∗P < 0.01. (N) Immunoblot analysis of ER stress markers CHOP in UM cells treated with Mito-LND.

Article Snippet: After blocked with 3 % BSA, the 4 μm serial sections were incubated with primary antibody at 4 °C overnight: SPP1 (Proteintech, 22952-1-AP), HMB45 (Abcam, ab787), CD8 (CST, 98941), and CD44 (CST, 37259).

Techniques: Enzyme-linked Immunosorbent Assay, Western Blot, Biomarker Discovery, Over Expression, CCK-8 Assay, Flow Cytometry, Expressing

Journal: Biomolecules

Article Title: Induced Tumor-Suppressing (iTS) Cell-Based Approach for Protecting the Bone from Advanced Prostate Cancer

doi: 10.3390/biom16020240

Figure Lengend Snippet: Tumor selectivity and anti-tumor action of extracellular moesin. MSN = moesin, CN = control, CM = conditioned medium, MSC = mesenchymal stem cells, siFN1 = fibronectin 1 siRNA, siCD44 = CD44 siRNA, A5 = MLO-A5 osteocytes, EO = EO771 mammary tumor cells, and Lrp5 = Lrp5 overexpression. The double and triple asterisks indicate p < 0.01 and p < 0.001. Scale bar: 10 µm. ( a ) Tumor selectivity, λ, of A5 CM, A5 Lrp5 CM, and moesin. A value λ larger than 1 indicates that the MTT-based inhibition is greater in tumor cells (TRAMP prostate tumor cells and EO771 mammary tumor cells) than in non-tumor cells (MSCs and MC3T3 osteoblasts). ( b ) MSN immunoprecipitated CD44 from TRAMP protein extracts and FN1 from TRAMP ECM protein extracts. ( c , d ) Suppression of MSN-driven inhibition of MTT-based viability of TRAMP cells by silencing CD44 and FN1. ( e ) Suppression of the downregulation of MMP9, TGFβ, and Snail in TRAMP cells by silencing CD44 and FN1. ( f ) Decrease in Src activity and β-catenin nuclear localization in response to MSN in TRAMP cells, and the blockage of their MSN-driven inhibition by silencing CD44.

Article Snippet: We used antibodies against CD44 (37259T), cleaved caspase 3 (9661S), Lrp5 (5731S), MSN (3726T), Snail (3879S), TGFβ (3711S), Vimentin (5741T) (Cell Signaling), Fibronectin 1 (sc-271098), cathepsin K (sc-48353), MMP9 (sc-393859), NFATc1 (sc-7294) (Santa Cruz Biotechnology), LIMA1 (Nbp1-87947), TRAIL (NB500-220) (Novus, Centennial, CO, USA), ANXA6 (ab199422) (Abcam, Cambridge, UK), p53 (MA5-12557) (Invitrogen, Carlsbad, CA, USA), and β-actin (Sigma).

Techniques: Control, Over Expression, Inhibition, Immunoprecipitation, Activity Assay

Journal: Biomolecules

Article Title: Induced Tumor-Suppressing (iTS) Cell-Based Approach for Protecting the Bone from Advanced Prostate Cancer

doi: 10.3390/biom16020240

Figure Lengend Snippet: FRET-based analysis of the MSN-CD44 regulatory axis. MSN = moesin, CN = control. The double asterisks indicate p < 0.01. ( a ) Significant reduction in the overall survival rate for patients with a high level of MSN. ( b ) MSN-driven stimulation of MTT-based proliferation of PC3 prostate cancer cells and MDA-MB-231 breast cancer cells. ( c ) Downregulation of MTT-based viability of PC3 cells and MDA-MB-231 cells in response to MSN-overexpressing Jurkat-derived CM. ( d ) Downregulation of PDL1 and p-Src by the application of 5 µg/mL recombinant MSN proteins. ( e ) The putative mechanism of the anti-tumor action of Lrp5/β-catenin-overexpressing osteocyte-derived CM, which inhibits the progression of tumors and the development of osteoclasts.

Article Snippet: We used antibodies against CD44 (37259T), cleaved caspase 3 (9661S), Lrp5 (5731S), MSN (3726T), Snail (3879S), TGFβ (3711S), Vimentin (5741T) (Cell Signaling), Fibronectin 1 (sc-271098), cathepsin K (sc-48353), MMP9 (sc-393859), NFATc1 (sc-7294) (Santa Cruz Biotechnology), LIMA1 (Nbp1-87947), TRAIL (NB500-220) (Novus, Centennial, CO, USA), ANXA6 (ab199422) (Abcam, Cambridge, UK), p53 (MA5-12557) (Invitrogen, Carlsbad, CA, USA), and β-actin (Sigma).

Techniques: Control, Derivative Assay, Recombinant