goat anti mouse antiserum Search Results


goat antibodies against mouse c3  (Valiant Co Ltd)
94
Valiant Co Ltd goat antibodies against mouse c3
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Goat Antibodies Against Mouse C3, supplied by Valiant Co Ltd, 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/product/goat+anti+mouse+antiserum/Anti-mouse+Complement+C3+goat+antiserum/pmc13088890-165-19-24
Average 94 stars, based on 1 article reviews
goat antibodies against mouse c3 - by Bioz Stars, 2026-10
94/100 stars
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polyclonal rabbit anti-mouse m heavy chain abs  (Biocan Diagnostics Inc)
90
Biocan Diagnostics Inc polyclonal rabbit anti-mouse m heavy chain abs
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Polyclonal Rabbit Anti Mouse M Heavy Chain Abs, supplied by Biocan Diagnostics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/biotin+conjugated+goat+anti+mouse+secondary+antiserum/pm10903747-64-0-11
Average 90 stars, based on 1 article reviews
polyclonal rabbit anti-mouse m heavy chain abs - by Bioz Stars, 2026-10
90/100 stars
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peroxidase conjugated goat anti-mouse igg antiserum  (Promega)
90
Promega peroxidase conjugated goat anti-mouse igg antiserum
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Peroxidase Conjugated Goat Anti Mouse Igg Antiserum, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/peroxidase+conjugated+goat+anti+mouse+igg+antiserum/pmc03407889-99-23-29
Average 90 stars, based on 1 article reviews
peroxidase conjugated goat anti-mouse igg antiserum - by Bioz Stars, 2026-10
90/100 stars
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goat-anti-mouse c3 antiserum  (GeneTex)
90
GeneTex goat-anti-mouse c3 antiserum
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Goat Anti Mouse C3 Antiserum, supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/goat+anti+mouse+c3+antiserum/pmc03723569-220-17-20
Average 90 stars, based on 1 article reviews
goat-anti-mouse c3 antiserum - by Bioz Stars, 2026-10
90/100 stars
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affinity-purified goat anti–mouse antiserum gam  (ICN Biomedicals)
90
ICN Biomedicals affinity-purified goat anti–mouse antiserum gam
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Affinity Purified Goat Anti–Mouse Antiserum Gam, supplied by ICN Biomedicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/affinity+purified+goat+anti+mouse+antiserum++gam+/pmc02195691-28-16-19
Average 90 stars, based on 1 article reviews
affinity-purified goat anti–mouse antiserum gam - by Bioz Stars, 2026-10
90/100 stars
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goat anti–mouse c3 antiserum  (Organon Teknika Corporation LLC)
90
Organon Teknika Corporation LLC goat anti–mouse c3 antiserum
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Goat Anti–Mouse C3 Antiserum, supplied by Organon Teknika Corporation LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/goat+anti+mouse+c3+antiserum/pmc02212415-17-59-54
Average 90 stars, based on 1 article reviews
goat anti–mouse c3 antiserum - by Bioz Stars, 2026-10
90/100 stars
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fluorescein isothiocyanateconjugated goat anti-mouse heavy chain-specific antiserum  (Asbach Medical Products GmbH)
90
Asbach Medical Products GmbH fluorescein isothiocyanateconjugated goat anti-mouse heavy chain-specific antiserum
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Fluorescein Isothiocyanateconjugated Goat Anti Mouse Heavy Chain Specific Antiserum, supplied by Asbach Medical Products GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/fluorescein+isothiocyanateconjugated+goat+anti+mouse+heavy+chain+specific+antiserum/pm09766506-79-12-20
Average 90 stars, based on 1 article reviews
fluorescein isothiocyanateconjugated goat anti-mouse heavy chain-specific antiserum - by Bioz Stars, 2026-10
90/100 stars
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fitc-conjugated goat anti-mouse igg- and igm-specific antiserum (1:20  (Becton Dickinson)
90
Becton Dickinson fitc-conjugated goat anti-mouse igg- and igm-specific antiserum (1:20
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Fitc Conjugated Goat Anti Mouse Igg And Igm Specific Antiserum (1:20, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/fitc+conjugated+goat+anti+mouse+igg++and+igm+specific+antiserum++1+20/pm21182079-161-25-28
Average 90 stars, based on 1 article reviews
fitc-conjugated goat anti-mouse igg- and igm-specific antiserum (1:20 - by Bioz Stars, 2026-10
90/100 stars
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hrp-conjugated goat anti-rabbit or anti-mouse antiserum  (Becton Dickinson)
90
Becton Dickinson hrp-conjugated goat anti-rabbit or anti-mouse antiserum
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Hrp Conjugated Goat Anti Rabbit Or Anti Mouse Antiserum, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/hrp+conjugated+goat+anti+rabbit+or+anti+mouse+antiserum/pmc05774619-52-23-27
Average 90 stars, based on 1 article reviews
hrp-conjugated goat anti-rabbit or anti-mouse antiserum - by Bioz Stars, 2026-10
90/100 stars
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alkaline phosphatase-conjugated goat anti-mouse igg antiserum  (Promega)
90
Promega alkaline phosphatase-conjugated goat anti-mouse igg antiserum
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Alkaline Phosphatase Conjugated Goat Anti Mouse Igg Antiserum, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/alkaline+phosphatase+conjugated+goat+anti+mouse+igg+antiserum/pmc03823488-80-63-69
Average 90 stars, based on 1 article reviews
alkaline phosphatase-conjugated goat anti-mouse igg antiserum - by Bioz Stars, 2026-10
90/100 stars
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goat anti-mouse antiserum  (Biozol Diagnostica Vertrieb GmbH)
90
Biozol Diagnostica Vertrieb GmbH goat anti-mouse antiserum
(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Goat Anti Mouse Antiserum, supplied by Biozol Diagnostica Vertrieb GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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goat-anti-mouse antiserum conjugated cy5  (Biozol Diagnostica Vertrieb GmbH)
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(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of <t>C3</t> activation were detected with <t>specific</t> <t>antibodies.</t> Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).
Goat Anti Mouse Antiserum Conjugated Cy5, supplied by Biozol Diagnostica Vertrieb GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+mouse+antiserum/goat+anti+mouse+antiserum+conjugated+cy5/pm32374034-67-14-20
Average 90 stars, based on 1 article reviews
goat-anti-mouse antiserum conjugated cy5 - by Bioz Stars, 2026-10
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(A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of C3 activation were detected with specific antibodies. Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).

Journal: Journal of Extracellular Vesicles

Article Title: Yersinia enterocolitica O:3 Outer Membrane Vesicles as a Platform for Complement Activation

doi: 10.1002/jev2.70270

Figure Lengend Snippet: (A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of C3 activation were detected with specific antibodies. Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).

Article Snippet: Depletion of functional C3 from serum was verified in Western blot [acc. to Younger et al. ( )], using goat antibodies against mouse C3 (MP Biomedicals, USA), HRP‐conjugated anti‐goat Ig (Dako) for detection of intact C3 α‐chain and ECL detection system.

Techniques: Activity Assay, Bacteria, Sterility, Cell Culture, Expressing, Activation Assay, Enzyme-linked Immunosorbent Assay, Incubation, Comparison, Binding Assay, Negative Control, SDS Page, Control