rabbit anti nfkb2 p100 p52  (Cell Signaling Technology Inc)

Journal: Cancer Biology & Medicine

Article Title: Migration and invasion inhibitory protein inhibits M2 macrophage polarization to suppress colorectal cancer progression through the STING–NFκB2–IL10 axis

doi: 10.20892/j.issn.2095-3941.2025.0282

Figure Lengend Snippet: MIIP modulates the STING–NFκB2–IL10 signaling pathway in CRC cells. Immunofluorescence staining showing the effects of MIIP knockdown and MIIP overexpression on dsDNA levels (A) and the distribution and expression of STING (B) in SW480 and SW620 cells. (C) Western blots showing the effects of MIIP knockdown and overexpression on STING, TRAF3, p-p100, and p52 levels. (D) ELISA results showing the effects of MIIP knockdown and overexpression on IL10 levels in the cell culture medium. (E and F) Effects of MIIP knockdown and/or STING knockdown on p52 expression (E) and IL10 levels in the cell culture medium (F). All data are presented as the means ± SDs ( n = 3). * P < 0.05, ** P < 0.01, and *** P < 0.001; scale bar, 50 μm.

Article Snippet: The primary antibodies used included mouse anti-dsDNA (1:1000, ab270732; Abcam, Cambridge, MA, USA), rabbit anti-NFKB2/p52 (1:200, 15503-1-AP; Proteintech, Wuhan, Hubei, China), rabbit anti-TMEM173/STING (1:200, 19851-1-AP; Proteintech, Wuhan, Hubei, China), and rabbit anti-IL-10 antibodies (1:100, 20850-1-AP; Proteintech, Wuhan, Hubei, China).

Techniques: Immunofluorescence, Staining, Knockdown, Over Expression, Expressing, Western Blot, Enzyme-linked Immunosorbent Assay, Cell Culture

Journal: Cancer Biology & Medicine

Article Title: Migration and invasion inhibitory protein inhibits M2 macrophage polarization to suppress colorectal cancer progression through the STING–NFκB2–IL10 axis

doi: 10.20892/j.issn.2095-3941.2025.0282

Figure Lengend Snippet: MIIP inhibits tumor growth and metastasis and M2 macrophage infiltration in a syngeneic CRC mouse model through the STING–NFκB2–IL10 axis. (A) Tumors in situ (indicated by green arrows) and liver metastatic nodules (indicated by black arrows) were observed in a syngeneic CRC mouse model. Statistics for the size of tumors in situ (B) and the number of metastatic foci (C). (D) Statistical analysis of IL10 levels in mouse blood. (E) Representative images of HE and IHC staining for SATB2, MIIP, STING, IL10, p52, and CD163 (green arrows) in tumor tissues from the different groups. The bar graphs show the percentages of high/low STING (F), IL-10 (G), and p52 (H) expression in the different groups. (I) Comparison of the number of CD163-positive cells among the different groups. All data are presented as the means ± SDs ( n = 3). ns, not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; scale bar, 50 μm.

Article Snippet: The primary antibodies used included mouse anti-dsDNA (1:1000, ab270732; Abcam, Cambridge, MA, USA), rabbit anti-NFKB2/p52 (1:200, 15503-1-AP; Proteintech, Wuhan, Hubei, China), rabbit anti-TMEM173/STING (1:200, 19851-1-AP; Proteintech, Wuhan, Hubei, China), and rabbit anti-IL-10 antibodies (1:100, 20850-1-AP; Proteintech, Wuhan, Hubei, China).

Techniques: In Situ, Immunohistochemistry, Expressing, Comparison

Journal: Cancer Biology & Medicine

Article Title: Migration and invasion inhibitory protein inhibits M2 macrophage polarization to suppress colorectal cancer progression through the STING–NFκB2–IL10 axis

doi: 10.20892/j.issn.2095-3941.2025.0282

Figure Lengend Snippet: MIIP modulates the STING–NFκB2–IL10 signaling pathway in CRC cells. Immunofluorescence staining showing the effects of MIIP knockdown and MIIP overexpression on dsDNA levels (A) and the distribution and expression of STING (B) in SW480 and SW620 cells. (C) Western blots showing the effects of MIIP knockdown and overexpression on STING, TRAF3, p-p100, and p52 levels. (D) ELISA results showing the effects of MIIP knockdown and overexpression on IL10 levels in the cell culture medium. (E and F) Effects of MIIP knockdown and/or STING knockdown on p52 expression (E) and IL10 levels in the cell culture medium (F). All data are presented as the means ± SDs ( n = 3). * P < 0.05, ** P < 0.01, and *** P < 0.001; scale bar, 50 μm.

Article Snippet: The primary antibodies used included rabbit anti-MIIP (1:1000, HPA044948; Sigma-Aldrich, St. Louis, MO, USA), rabbit anti-MIIP (1:1000, orb537083; Biorbyt, Cambridge, UK), rabbit anti-STING (1:2000, 19851-1-AP; Proteintech, Wuhan, Hubei, China), mouse anti-TRAF3 (1:1000, 66310-1-Ig; Proteintech, Wuhan, Hubei, China), rabbit anti-p52 (1:1000, 4882S; Cell Signaling Technology, Danvers, MA, USA), rabbit anti-p52 (1:500, 15503-1-AP; Proteintech, Wuhan, Hubei, China), rabbit anti-p-p100 (1:1000, 4810T; Cell Signaling Technology, Danvers, MA, USA), rabbit anti-CD163 (1:1000, 68922; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-β-actin antibodies (1:1000, 3700S; Cell Signaling Technology, Danvers, MA, USA).

Techniques: Immunofluorescence, Staining, Knockdown, Over Expression, Expressing, Western Blot, Enzyme-linked Immunosorbent Assay, Cell Culture

Journal: Cancer Biology & Medicine

Article Title: Migration and invasion inhibitory protein inhibits M2 macrophage polarization to suppress colorectal cancer progression through the STING–NFκB2–IL10 axis

doi: 10.20892/j.issn.2095-3941.2025.0282

Figure Lengend Snippet: MIIP inhibits tumor growth and metastasis and M2 macrophage infiltration in a syngeneic CRC mouse model through the STING–NFκB2–IL10 axis. (A) Tumors in situ (indicated by green arrows) and liver metastatic nodules (indicated by black arrows) were observed in a syngeneic CRC mouse model. Statistics for the size of tumors in situ (B) and the number of metastatic foci (C). (D) Statistical analysis of IL10 levels in mouse blood. (E) Representative images of HE and IHC staining for SATB2, MIIP, STING, IL10, p52, and CD163 (green arrows) in tumor tissues from the different groups. The bar graphs show the percentages of high/low STING (F), IL-10 (G), and p52 (H) expression in the different groups. (I) Comparison of the number of CD163-positive cells among the different groups. All data are presented as the means ± SDs ( n = 3). ns, not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; scale bar, 50 μm.

Article Snippet: The primary antibodies used included rabbit anti-MIIP (1:1000, HPA044948; Sigma-Aldrich, St. Louis, MO, USA), rabbit anti-MIIP (1:1000, orb537083; Biorbyt, Cambridge, UK), rabbit anti-STING (1:2000, 19851-1-AP; Proteintech, Wuhan, Hubei, China), mouse anti-TRAF3 (1:1000, 66310-1-Ig; Proteintech, Wuhan, Hubei, China), rabbit anti-p52 (1:1000, 4882S; Cell Signaling Technology, Danvers, MA, USA), rabbit anti-p52 (1:500, 15503-1-AP; Proteintech, Wuhan, Hubei, China), rabbit anti-p-p100 (1:1000, 4810T; Cell Signaling Technology, Danvers, MA, USA), rabbit anti-CD163 (1:1000, 68922; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-β-actin antibodies (1:1000, 3700S; Cell Signaling Technology, Danvers, MA, USA).

Techniques: In Situ, Immunohistochemistry, Expressing, Comparison