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mouse anti human il 27ra mab (R&D Systems)

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R&D Systems mouse anti human il 27ra mab
FIGURE 1. <t>sIL-27Ra</t> is released from differ- ent primary human cell types. (A) Puriﬁed CD4+

Mouse Anti Human Il 27ra Mab, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+human+il+27ra+mab/pm24771852-51-10-15?v=R%26D+Systems
Average 90 stars, based on 5 article reviews

mouse anti human il 27ra mab - by Bioz Stars, 2026-08

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1) Product Images from "A soluble form of IL-27Rα is a natural IL-27 antagonist."

Article Title: A soluble form of IL-27Rα is a natural IL-27 antagonist.

Journal: Journal of immunology (Baltimore, Md. : 1950)

doi: 10.4049/jimmunol.1303435

Figure Legend Snippet: FIGURE 1. sIL-27Ra is released from differ- ent primary human cell types. (A) Puriﬁed CD4+

Techniques Used:

FIGURE 2. ELISA analysis of sIL-27Ra in the sera of healthy indi- viduals. (A) Levels of sIL-27Ra were measured by ELISA in the sera from healthy individuals. (B) The correlation between sIL-27Ra and IL-27 se- rum levels is shown. Although a logarithmic scale is used, linear regression was calculated using the actual values. (C) Sera from six pregnant women, collected at various times during pregnancy (6–10 sera per time point), were tested by sIL-27Ra ELISA. The mean values (6SEM) are represented. (D) Sera from four nonpregnant healthy individuals (Da–d) and four pregnant women (De–h) were tested in a sandwich ELISA using the indicated Abs as capture Abs and biotinylated anti-human IL-27 Ab as detection Ab.

Figure Legend Snippet: FIGURE 2. ELISA analysis of sIL-27Ra in the sera of healthy indi- viduals. (A) Levels of sIL-27Ra were measured by ELISA in the sera from healthy individuals. (B) The correlation between sIL-27Ra and IL-27 se- rum levels is shown. Although a logarithmic scale is used, linear regression was calculated using the actual values. (C) Sera from six pregnant women, collected at various times during pregnancy (6–10 sera per time point), were tested by sIL-27Ra ELISA. The mean values (6SEM) are represented. (D) Sera from four nonpregnant healthy individuals (Da–d) and four pregnant women (De–h) were tested in a sandwich ELISA using the indicated Abs as capture Abs and biotinylated anti-human IL-27 Ab as detection Ab.

Techniques Used: Enzyme-linked Immunosorbent Assay, Sandwich ELISA

FIGURE 3. Biochemical characterization of sIL- 27Ra. Lysates from COS7 cells transiently transfected with vector control or vector expressing IL-27RaV5His (A), and anti–IL-27Ra immunoprecipitates from the lysate of IL-27RaV5His–transfected COS7 cells before or after N-glycanase treatment (B), were analyzed by immunoblot using anti–IL-27Ra Ab. (C) Concentrated culture supernatant from KMH2 cells (left) or human sera (right) was submitted to immunoprecipitation with goat or mouse anti–IL-27Ra Abs, followed by protein G beads, or with anti–IL-27Ra beads, as indicated, and analyzed by anti–IL-27Ra immunoblot. (D) Treatment of anti–IL-27Ra immunoprecipitate from KMH2 cul- ture supernatant with N-glycanase causes a shift in the apparent molecular mass of sIL-27Ra from 90/70 to 60 kDa. Cross-reacting IgH is indicated by an asterisk. Kilodaltons of molecular size markers are reported on the left.

Figure Legend Snippet: FIGURE 3. Biochemical characterization of sIL- 27Ra. Lysates from COS7 cells transiently transfected with vector control or vector expressing IL-27RaV5His (A), and anti–IL-27Ra immunoprecipitates from the lysate of IL-27RaV5His–transfected COS7 cells before or after N-glycanase treatment (B), were analyzed by immunoblot using anti–IL-27Ra Ab. (C) Concentrated culture supernatant from KMH2 cells (left) or human sera (right) was submitted to immunoprecipitation with goat or mouse anti–IL-27Ra Abs, followed by protein G beads, or with anti–IL-27Ra beads, as indicated, and analyzed by anti–IL-27Ra immunoblot. (D) Treatment of anti–IL-27Ra immunoprecipitate from KMH2 cul- ture supernatant with N-glycanase causes a shift in the apparent molecular mass of sIL-27Ra from 90/70 to 60 kDa. Cross-reacting IgH is indicated by an asterisk. Kilodaltons of molecular size markers are reported on the left.

Techniques Used: Transfection, Plasmid Preparation, Control, Expressing, Western Blot, Immunoprecipitation

FIGURE 4. Role of metalloproteases in the production of sIL-27Ra. (A) COS7 cells were cotransfected with GFP vector and pcDNA3 control vector or pcDNA3 encoding IL-27RaV5His. Two days after transfection, cells were stained with isotype control (ﬁlled gray histogram) or anti–IL-27Ra (bold line) Abs and analyzed by FACS. Staining observed in GFP-positive cells is shown. (B) Cell culture supernatants from transfected COS7 cells were tested by Western blot for detection of sIL-27R. Only Abs recognizing the extracellular domain of IL-27Ra, but not its intracellular C terminus (V5 mAb), detected sIL-27Ra. (C) Cell culture supernatants from IL-27RaV5His–transfected COS7 cells, incubated for the indicated times with GM6001, TAPI-0 (both at 50 mM), or DMSO control, were tested by sIL-27Ra ELISA. No sIL-27Ra was detected in the culture supernatant from vector control-transfected COS7 cells. (D) Cell lysates from COS7 cells collected 48 h after transfection were analyzed by immunoblot with anti-V5 Ab to monitor IL-27RaV5His expression levels. On a longer exposure, a smaller band that was weaker in the presence of metalloprotease inhibitors and might correspond to the transmembrane and intracellular domains was observed (data not shown). One representative experiment of two to three is shown in (A)–(D). (E) KMH2 cells were incubated for 3 d with various con- centrations of GM6001, TAPI-0, or DMSO. Levels of sIL-27Ra measured by ELISA in the culture supernatants and cell numbers determined by trypan blue exclusion are shown as the mean 6 SEM of relative levels of three independent experiments. (F) Puriﬁed CD4+ T cells were stimulated for 5 d with CD2/CD3/ CD28 beads and IL-2 and various concentrations of GM6001, TAPI-0, or DMSO. Relative levels of sIL-27Ra and cell numbers observed in four independent experiments performed with different donors are shown. Inhibitor doses .25 mM were not used in CD4+ T cells because they resulted in cell toxicity. (G) Cell membrane IL-27Ra expression (mIL-27Ra) was analyzed by FACS in activated CD4+ T cells cultured for 5 d in the presence of GM6001, TAPI-0 (both at 25 mM), or DMSO. The mean ﬂuorescence intensity of mIL-27Ra staining is indicated. (H) The mean ﬂuorescence intensity of mIL-27Ra staining observed in GM6001 or TAPI-0–treated CD4+ T cells relative to that observed in the DMSO control is shown as mean 6 SEM of four independent experiments. *p , 0.05, **p , 0.01, ***p , 0.001.

Figure Legend Snippet: FIGURE 4. Role of metalloproteases in the production of sIL-27Ra. (A) COS7 cells were cotransfected with GFP vector and pcDNA3 control vector or pcDNA3 encoding IL-27RaV5His. Two days after transfection, cells were stained with isotype control (ﬁlled gray histogram) or anti–IL-27Ra (bold line) Abs and analyzed by FACS. Staining observed in GFP-positive cells is shown. (B) Cell culture supernatants from transfected COS7 cells were tested by Western blot for detection of sIL-27R. Only Abs recognizing the extracellular domain of IL-27Ra, but not its intracellular C terminus (V5 mAb), detected sIL-27Ra. (C) Cell culture supernatants from IL-27RaV5His–transfected COS7 cells, incubated for the indicated times with GM6001, TAPI-0 (both at 50 mM), or DMSO control, were tested by sIL-27Ra ELISA. No sIL-27Ra was detected in the culture supernatant from vector control-transfected COS7 cells. (D) Cell lysates from COS7 cells collected 48 h after transfection were analyzed by immunoblot with anti-V5 Ab to monitor IL-27RaV5His expression levels. On a longer exposure, a smaller band that was weaker in the presence of metalloprotease inhibitors and might correspond to the transmembrane and intracellular domains was observed (data not shown). One representative experiment of two to three is shown in (A)–(D). (E) KMH2 cells were incubated for 3 d with various con- centrations of GM6001, TAPI-0, or DMSO. Levels of sIL-27Ra measured by ELISA in the culture supernatants and cell numbers determined by trypan blue exclusion are shown as the mean 6 SEM of relative levels of three independent experiments. (F) Puriﬁed CD4+ T cells were stimulated for 5 d with CD2/CD3/ CD28 beads and IL-2 and various concentrations of GM6001, TAPI-0, or DMSO. Relative levels of sIL-27Ra and cell numbers observed in four independent experiments performed with different donors are shown. Inhibitor doses .25 mM were not used in CD4+ T cells because they resulted in cell toxicity. (G) Cell membrane IL-27Ra expression (mIL-27Ra) was analyzed by FACS in activated CD4+ T cells cultured for 5 d in the presence of GM6001, TAPI-0 (both at 25 mM), or DMSO. The mean ﬂuorescence intensity of mIL-27Ra staining is indicated. (H) The mean ﬂuorescence intensity of mIL-27Ra staining observed in GM6001 or TAPI-0–treated CD4+ T cells relative to that observed in the DMSO control is shown as mean 6 SEM of four independent experiments. *p , 0.05, **p , 0.01, ***p , 0.001.

Techniques Used: Plasmid Preparation, Control, Transfection, Staining, Cell Culture, Western Blot, Incubation, Enzyme-linked Immunosorbent Assay, Expressing, Membrane

$FIGURE 5. Natural sIL-27Ra antagonizes IL-27 signaling. (A) Concentrated cell culture supernatant of KMH2 cells was submitted to immuno- precipitation with control or anti–IL-27Ra Abs, in the absence or presence of 100 ng rIL-27. Immunoprecipitates (lanes 1–4) and a fraction of su- pernatant before immunoprecipitation (lane 5) were analyzed by anti–IL-27Ra and anti-EBI3 immunoblots. (B and C) rIL-27 was preincubated for 15 min at 37˚C with various concentrations of rIL-27R-Fc or gp130-Fc fusion proteins, or puriﬁed natural sIL-27Ra, before addition to BL2 cells for 15 min. Cell lysates were analyzed for STAT1 activation with anti–phospho-STAT1 Ab and subsequently with STAT1 Ab to monitor STAT1 levels. (D) Similar experiment was conducted using IFN-g in place of IL-27. (E) Inhibition of IL-27 binding to BL2 cells. rIL-27 (2 ng) was preincubated or not with puriﬁed natural sIL-27Ra (2 ng) before incubation with BL2 cells. IL-27 binding was measured by FACS. One representative experiment of two to three is shown.$
Figure Legend Snippet: FIGURE 5. Natural sIL-27Ra antagonizes IL-27 signaling. (A) Concentrated cell culture supernatant of KMH2 cells was submitted to immuno- precipitation with control or anti–IL-27Ra Abs, in the absence or presence of 100 ng rIL-27. Immunoprecipitates (lanes 1–4) and a fraction of su- pernatant before immunoprecipitation (lane 5) were analyzed by anti–IL-27Ra and anti-EBI3 immunoblots. (B and C) rIL-27 was preincubated for 15 min at 37˚C with various concentrations of rIL-27R-Fc or gp130-Fc fusion proteins, or puriﬁed natural sIL-27Ra, before addition to BL2 cells for 15 min. Cell lysates were analyzed for STAT1 activation with anti–phospho-STAT1 Ab and subsequently with STAT1 Ab to monitor STAT1 levels. (D) Similar experiment was conducted using IFN-g in place of IL-27. (E) Inhibition of IL-27 binding to BL2 cells. rIL-27 (2 ng) was preincubated or not with puriﬁed natural sIL-27Ra (2 ng) before incubation with BL2 cells. IL-27 binding was measured by FACS. One representative experiment of two to three is shown.

Techniques Used: Cell Culture, Immunoprecipitation, Control, Western Blot, Activation Assay, Inhibition, Binding Assay, Incubation

FIGURE 6. Analysis of sIL-27Ra and IL-27 levels in the sera of CD patients. Serum levels of sIL-27Ra (A) and IL-27 (B) were determined by ELISA in 52 CD patients and 28 healthy individuals. The correlation between sIL-27Ra and IL-27 serum levels (C) and the molar ratio between IL-27 and sIL-27Ra serum values (D) are shown. Although a logarithmic scale is used in (C), linear regression was calculated using the actual values.

Figure Legend Snippet: FIGURE 6. Analysis of sIL-27Ra and IL-27 levels in the sera of CD patients. Serum levels of sIL-27Ra (A) and IL-27 (B) were determined by ELISA in 52 CD patients and 28 healthy individuals. The correlation between sIL-27Ra and IL-27 serum levels (C) and the molar ratio between IL-27 and sIL-27Ra serum values (D) are shown. Although a logarithmic scale is used in (C), linear regression was calculated using the actual values.

Techniques Used: Enzyme-linked Immunosorbent Assay

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Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: A soluble form of IL-27Rα is a natural IL-27 antagonist.

doi: 10.4049/jimmunol.1303435

Figure Lengend Snippet: FIGURE 1. sIL-27Ra is released from differ- ent primary human cell types. (A) Puriﬁed CD4+

Article Snippet: To detect sIL-27Ra, a sandwich ELISA was developed by using mouse anti-human IL-27Ra mAb (191106; R&D Systems) as coating Ab and goat biotinylated polyclonal anti-human IL-27Ra Ab (R&D Systems) as detection Ab.

Techniques:

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: A soluble form of IL-27Rα is a natural IL-27 antagonist.

doi: 10.4049/jimmunol.1303435

Figure Lengend Snippet: FIGURE 2. ELISA analysis of sIL-27Ra in the sera of healthy indi- viduals. (A) Levels of sIL-27Ra were measured by ELISA in the sera from healthy individuals. (B) The correlation between sIL-27Ra and IL-27 se- rum levels is shown. Although a logarithmic scale is used, linear regression was calculated using the actual values. (C) Sera from six pregnant women, collected at various times during pregnancy (6–10 sera per time point), were tested by sIL-27Ra ELISA. The mean values (6SEM) are represented. (D) Sera from four nonpregnant healthy individuals (Da–d) and four pregnant women (De–h) were tested in a sandwich ELISA using the indicated Abs as capture Abs and biotinylated anti-human IL-27 Ab as detection Ab.

Techniques: Enzyme-linked Immunosorbent Assay, Sandwich ELISA

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: A soluble form of IL-27Rα is a natural IL-27 antagonist.

doi: 10.4049/jimmunol.1303435

Figure Lengend Snippet: FIGURE 3. Biochemical characterization of sIL- 27Ra. Lysates from COS7 cells transiently transfected with vector control or vector expressing IL-27RaV5His (A), and anti–IL-27Ra immunoprecipitates from the lysate of IL-27RaV5His–transfected COS7 cells before or after N-glycanase treatment (B), were analyzed by immunoblot using anti–IL-27Ra Ab. (C) Concentrated culture supernatant from KMH2 cells (left) or human sera (right) was submitted to immunoprecipitation with goat or mouse anti–IL-27Ra Abs, followed by protein G beads, or with anti–IL-27Ra beads, as indicated, and analyzed by anti–IL-27Ra immunoblot. (D) Treatment of anti–IL-27Ra immunoprecipitate from KMH2 cul- ture supernatant with N-glycanase causes a shift in the apparent molecular mass of sIL-27Ra from 90/70 to 60 kDa. Cross-reacting IgH is indicated by an asterisk. Kilodaltons of molecular size markers are reported on the left.

Techniques: Transfection, Plasmid Preparation, Control, Expressing, Western Blot, Immunoprecipitation

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: A soluble form of IL-27Rα is a natural IL-27 antagonist.

doi: 10.4049/jimmunol.1303435

Figure Lengend Snippet: FIGURE 4. Role of metalloproteases in the production of sIL-27Ra. (A) COS7 cells were cotransfected with GFP vector and pcDNA3 control vector or pcDNA3 encoding IL-27RaV5His. Two days after transfection, cells were stained with isotype control (ﬁlled gray histogram) or anti–IL-27Ra (bold line) Abs and analyzed by FACS. Staining observed in GFP-positive cells is shown. (B) Cell culture supernatants from transfected COS7 cells were tested by Western blot for detection of sIL-27R. Only Abs recognizing the extracellular domain of IL-27Ra, but not its intracellular C terminus (V5 mAb), detected sIL-27Ra. (C) Cell culture supernatants from IL-27RaV5His–transfected COS7 cells, incubated for the indicated times with GM6001, TAPI-0 (both at 50 mM), or DMSO control, were tested by sIL-27Ra ELISA. No sIL-27Ra was detected in the culture supernatant from vector control-transfected COS7 cells. (D) Cell lysates from COS7 cells collected 48 h after transfection were analyzed by immunoblot with anti-V5 Ab to monitor IL-27RaV5His expression levels. On a longer exposure, a smaller band that was weaker in the presence of metalloprotease inhibitors and might correspond to the transmembrane and intracellular domains was observed (data not shown). One representative experiment of two to three is shown in (A)–(D). (E) KMH2 cells were incubated for 3 d with various con- centrations of GM6001, TAPI-0, or DMSO. Levels of sIL-27Ra measured by ELISA in the culture supernatants and cell numbers determined by trypan blue exclusion are shown as the mean 6 SEM of relative levels of three independent experiments. (F) Puriﬁed CD4+ T cells were stimulated for 5 d with CD2/CD3/ CD28 beads and IL-2 and various concentrations of GM6001, TAPI-0, or DMSO. Relative levels of sIL-27Ra and cell numbers observed in four independent experiments performed with different donors are shown. Inhibitor doses .25 mM were not used in CD4+ T cells because they resulted in cell toxicity. (G) Cell membrane IL-27Ra expression (mIL-27Ra) was analyzed by FACS in activated CD4+ T cells cultured for 5 d in the presence of GM6001, TAPI-0 (both at 25 mM), or DMSO. The mean ﬂuorescence intensity of mIL-27Ra staining is indicated. (H) The mean ﬂuorescence intensity of mIL-27Ra staining observed in GM6001 or TAPI-0–treated CD4+ T cells relative to that observed in the DMSO control is shown as mean 6 SEM of four independent experiments. *p , 0.05, **p , 0.01, ***p , 0.001.

Techniques: Plasmid Preparation, Control, Transfection, Staining, Cell Culture, Western Blot, Incubation, Enzyme-linked Immunosorbent Assay, Expressing, Membrane

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: A soluble form of IL-27Rα is a natural IL-27 antagonist.

doi: 10.4049/jimmunol.1303435

Figure Lengend Snippet: FIGURE 5. Natural sIL-27Ra antagonizes IL-27 signaling. (A) Concentrated cell culture supernatant of KMH2 cells was submitted to immuno- precipitation with control or anti–IL-27Ra Abs, in the absence or presence of 100 ng rIL-27. Immunoprecipitates (lanes 1–4) and a fraction of su- pernatant before immunoprecipitation (lane 5) were analyzed by anti–IL-27Ra and anti-EBI3 immunoblots. (B and C) rIL-27 was preincubated for 15 min at 37˚C with various concentrations of rIL-27R-Fc or gp130-Fc fusion proteins, or puriﬁed natural sIL-27Ra, before addition to BL2 cells for 15 min. Cell lysates were analyzed for STAT1 activation with anti–phospho-STAT1 Ab and subsequently with STAT1 Ab to monitor STAT1 levels. (D) Similar experiment was conducted using IFN-g in place of IL-27. (E) Inhibition of IL-27 binding to BL2 cells. rIL-27 (2 ng) was preincubated or not with puriﬁed natural sIL-27Ra (2 ng) before incubation with BL2 cells. IL-27 binding was measured by FACS. One representative experiment of two to three is shown.

Techniques: Cell Culture, Immunoprecipitation, Control, Western Blot, Activation Assay, Inhibition, Binding Assay, Incubation

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: A soluble form of IL-27Rα is a natural IL-27 antagonist.

doi: 10.4049/jimmunol.1303435

Figure Lengend Snippet: FIGURE 6. Analysis of sIL-27Ra and IL-27 levels in the sera of CD patients. Serum levels of sIL-27Ra (A) and IL-27 (B) were determined by ELISA in 52 CD patients and 28 healthy individuals. The correlation between sIL-27Ra and IL-27 serum levels (C) and the molar ratio between IL-27 and sIL-27Ra serum values (D) are shown. Although a logarithmic scale is used in (C), linear regression was calculated using the actual values.

Techniques: Enzyme-linked Immunosorbent Assay

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