biotin-conjugated rabbit immunoglobulin Millipore Search Results


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  • 90
    Millipore monoclonal anti rabbit immunoglobulins biotin antibody
    Monoclonal Anti Rabbit Immunoglobulins Biotin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Millipore biotin conjugated anti rabbit immunoglobulins
    Evaluation of Candida- specific antibodies on Candida from infected mice. Candida recovered from lavage fluid of day-9-infected animals was incubated with <t>biotin-conjugated</t> <t>anti-mouse</t> <t>immunoglobulin</t> followed by incubation with avidin-fluorescein isothiocyanate. Shown are bright-field (A and C) and fluorescent (B and D) images of hyphae from a mouse lavage fluid sample representative of 20 tested from separate mice (A and B) and of the positive control ( Candida hyphae incubated with anti- Candida antibody) (C and D).
    Biotin Conjugated Anti Rabbit Immunoglobulins, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Millipore biotin conjugated rabbit immunoglobulin
    Evaluation of Candida- specific antibodies on Candida from infected mice. Candida recovered from lavage fluid of day-9-infected animals was incubated with <t>biotin-conjugated</t> <t>anti-mouse</t> <t>immunoglobulin</t> followed by incubation with avidin-fluorescein isothiocyanate. Shown are bright-field (A and C) and fluorescent (B and D) images of hyphae from a mouse lavage fluid sample representative of 20 tested from separate mice (A and B) and of the positive control ( Candida hyphae incubated with anti- Candida antibody) (C and D).
    Biotin Conjugated Rabbit Immunoglobulin, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Millipore biotin conjugated rabbit anti goat immunoglobulin antibody
    Evaluation of Candida- specific antibodies on Candida from infected mice. Candida recovered from lavage fluid of day-9-infected animals was incubated with <t>biotin-conjugated</t> <t>anti-mouse</t> <t>immunoglobulin</t> followed by incubation with avidin-fluorescein isothiocyanate. Shown are bright-field (A and C) and fluorescent (B and D) images of hyphae from a mouse lavage fluid sample representative of 20 tested from separate mice (A and B) and of the positive control ( Candida hyphae incubated with anti- Candida antibody) (C and D).
    Biotin Conjugated Rabbit Anti Goat Immunoglobulin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Millipore anti rabbit igg biotin conjugated
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Anti Rabbit Igg Biotin Conjugated, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore anti rabbit igg whole molecule biotin antibody
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Anti Rabbit Igg Whole Molecule Biotin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 240 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    Millipore biotin conjugated anti dinitrophenyl rabbit igg
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Biotin Conjugated Anti Dinitrophenyl Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 76/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Millipore avidin conjugated goat anti rabbit immunoglobulin g
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Avidin Conjugated Goat Anti Rabbit Immunoglobulin G, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Millipore anti rabbit igg γ specific biotin conjugated mab
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Anti Rabbit Igg γ Specific Biotin Conjugated Mab, supplied by Millipore, used in various techniques. Bioz Stars score: 81/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore goat anti rabbit igg biotin conjugate
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Goat Anti Rabbit Igg Biotin Conjugate, supplied by Millipore, 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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    80
    Millipore goat anti rabbit igg conjugated to biotin
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Goat Anti Rabbit Igg Conjugated To Biotin, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rabbit anti goat igg biotin conjugates
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Rabbit Anti Goat Igg Biotin Conjugates, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore biotin conjugated monoclonal antirabbit igg
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Biotin Conjugated Monoclonal Antirabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Millipore biotin conjugated donkey α rabbit igg
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Biotin Conjugated Donkey α Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 81/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Millipore biotin conjugated sheep anti rabbit igg f
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Biotin Conjugated Sheep Anti Rabbit Igg F, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti fd bacteriophage biotin antibody
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Anti Fd Bacteriophage Biotin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore fitc conjugated anti rabbit igg
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Fitc Conjugated Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 345 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore biotin conjugated goat anti rabbit igg pab
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Biotin Conjugated Goat Anti Rabbit Igg Pab, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore biotin conjugated affinity purified goat anti rabbit igg
    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
    Biotin Conjugated Affinity Purified Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
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    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
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    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
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    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
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    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
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    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and <t>anti-SARS</t> S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit <t>IgG</t> antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.
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    Tetraspanins support EWI-2- α 3 β 1 integrin association. (A) ∼10 7 A431 EWI-2 cells were labeled with sulfo-NHS biotin and lysed in 1% Brij 96. Equal portions of lysate were depleted three times with protein G alone (mock) or with protein G plus anti- tetraspanin or α2 integrin antibodies. Depletions are indicated at the top of the figure. Depleted lysates were further divided and immunoprecipitated with anti-CD81, anti-α3 integrin, or anti-α2 integrin antibodies conjugated to agarose followed by SDS-PAGE and blotting with HRP-ExtrAvidin ® . EWI-2* is a 50-kD EWI-2 cleavage fragment. Densitometry revealed that CD9 and CD81 depletion removed only ∼10% of total α3 integrin, but ∼85% of the α3-associated EWI-2. Densitometry of an independent experiment confirmed that only ∼10% of α3 is CD81-associated in A431 cells (not depicted). (B) U937 cells lacking CD9 and CD81 were transduced with CD81 and EWI-2 retroviral expression vectors and selected to obtain stable (CD81−, EWI-2+) or (CD81+, EWI-2+) cell lines. Then, both cell types were super-infected with an α3 integrin retroviral expression vector, to yield equivalent α3 expression levels, as confirmed by flow cytometry (not depicted). EWI-2 (M2 <t>anti-FLAG</t> mAb), CD81 (M38 mAb), or α3 integrin (A3X8 mAb) were immunoprecipitated from 1% Brij 96 lysates of CD81 − or CD81 + cells. Immunoprecipitates were blotted for EWI-2 (biotinylated M2 anti-FLAG mAb), α3 integrin (D23 <t>pAb),</t> or CD81 (M38 mAb). Apparent mature and immature forms of EWI-2 and α3 integrin are indicated with filled and open arrows, respectively. 6 × 10 6 cell equivalents were analyzed in EWI-2 and CD81 immunoprecipitations, and 4.8 × 10 7 cell equivalents in the α3 immunoprecipitations. (C) Biotinylated CD81 − or CD81 + cells were lysed in 1% Brij 96, and EWI-2 (FLAG), α3 integrin, or CD81 were immunoprecipitated as above. Cell surface–labeled proteins were revealed by HRP-ExtrAvidin ® blot. 1.7 × 10 6 cell equivalents were analyzed in each immunoprecipitation.
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    Tetraspanins support EWI-2- α 3 β 1 integrin association. (A) ∼10 7 A431 EWI-2 cells were labeled with sulfo-NHS biotin and lysed in 1% Brij 96. Equal portions of lysate were depleted three times with protein G alone (mock) or with protein G plus anti- tetraspanin or α2 integrin antibodies. Depletions are indicated at the top of the figure. Depleted lysates were further divided and immunoprecipitated with anti-CD81, anti-α3 integrin, or anti-α2 integrin antibodies conjugated to agarose followed by SDS-PAGE and blotting with HRP-ExtrAvidin ® . EWI-2* is a 50-kD EWI-2 cleavage fragment. Densitometry revealed that CD9 and CD81 depletion removed only ∼10% of total α3 integrin, but ∼85% of the α3-associated EWI-2. Densitometry of an independent experiment confirmed that only ∼10% of α3 is CD81-associated in A431 cells (not depicted). (B) U937 cells lacking CD9 and CD81 were transduced with CD81 and EWI-2 retroviral expression vectors and selected to obtain stable (CD81−, EWI-2+) or (CD81+, EWI-2+) cell lines. Then, both cell types were super-infected with an α3 integrin retroviral expression vector, to yield equivalent α3 expression levels, as confirmed by flow cytometry (not depicted). EWI-2 (M2 <t>anti-FLAG</t> mAb), CD81 (M38 mAb), or α3 integrin (A3X8 mAb) were immunoprecipitated from 1% Brij 96 lysates of CD81 − or CD81 + cells. Immunoprecipitates were blotted for EWI-2 (biotinylated M2 anti-FLAG mAb), α3 integrin (D23 <t>pAb),</t> or CD81 (M38 mAb). Apparent mature and immature forms of EWI-2 and α3 integrin are indicated with filled and open arrows, respectively. 6 × 10 6 cell equivalents were analyzed in EWI-2 and CD81 immunoprecipitations, and 4.8 × 10 7 cell equivalents in the α3 immunoprecipitations. (C) Biotinylated CD81 − or CD81 + cells were lysed in 1% Brij 96, and EWI-2 (FLAG), α3 integrin, or CD81 were immunoprecipitated as above. Cell surface–labeled proteins were revealed by HRP-ExtrAvidin ® blot. 1.7 × 10 6 cell equivalents were analyzed in each immunoprecipitation.
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    Tetraspanins support EWI-2- α 3 β 1 integrin association. (A) ∼10 7 A431 EWI-2 cells were labeled with sulfo-NHS biotin and lysed in 1% Brij 96. Equal portions of lysate were depleted three times with protein G alone (mock) or with protein G plus anti- tetraspanin or α2 integrin antibodies. Depletions are indicated at the top of the figure. Depleted lysates were further divided and immunoprecipitated with anti-CD81, anti-α3 integrin, or anti-α2 integrin antibodies conjugated to agarose followed by SDS-PAGE and blotting with HRP-ExtrAvidin ® . EWI-2* is a 50-kD EWI-2 cleavage fragment. Densitometry revealed that CD9 and CD81 depletion removed only ∼10% of total α3 integrin, but ∼85% of the α3-associated EWI-2. Densitometry of an independent experiment confirmed that only ∼10% of α3 is CD81-associated in A431 cells (not depicted). (B) U937 cells lacking CD9 and CD81 were transduced with CD81 and EWI-2 retroviral expression vectors and selected to obtain stable (CD81−, EWI-2+) or (CD81+, EWI-2+) cell lines. Then, both cell types were super-infected with an α3 integrin retroviral expression vector, to yield equivalent α3 expression levels, as confirmed by flow cytometry (not depicted). EWI-2 (M2 <t>anti-FLAG</t> mAb), CD81 (M38 mAb), or α3 integrin (A3X8 mAb) were immunoprecipitated from 1% Brij 96 lysates of CD81 − or CD81 + cells. Immunoprecipitates were blotted for EWI-2 (biotinylated M2 anti-FLAG mAb), α3 integrin (D23 <t>pAb),</t> or CD81 (M38 mAb). Apparent mature and immature forms of EWI-2 and α3 integrin are indicated with filled and open arrows, respectively. 6 × 10 6 cell equivalents were analyzed in EWI-2 and CD81 immunoprecipitations, and 4.8 × 10 7 cell equivalents in the α3 immunoprecipitations. (C) Biotinylated CD81 − or CD81 + cells were lysed in 1% Brij 96, and EWI-2 (FLAG), α3 integrin, or CD81 were immunoprecipitated as above. Cell surface–labeled proteins were revealed by HRP-ExtrAvidin ® blot. 1.7 × 10 6 cell equivalents were analyzed in each immunoprecipitation.
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    Image Search Results


    Evaluation of Candida- specific antibodies on Candida from infected mice. Candida recovered from lavage fluid of day-9-infected animals was incubated with biotin-conjugated anti-mouse immunoglobulin followed by incubation with avidin-fluorescein isothiocyanate. Shown are bright-field (A and C) and fluorescent (B and D) images of hyphae from a mouse lavage fluid sample representative of 20 tested from separate mice (A and B) and of the positive control ( Candida hyphae incubated with anti- Candida antibody) (C and D).

    Journal: Infection and Immunity

    Article Title: Candida-Specific Antibodies during Experimental Vaginal Candidiasis in Mice

    doi: 10.1128/IAI.70.10.5790-5799.2002

    Figure Lengend Snippet: Evaluation of Candida- specific antibodies on Candida from infected mice. Candida recovered from lavage fluid of day-9-infected animals was incubated with biotin-conjugated anti-mouse immunoglobulin followed by incubation with avidin-fluorescein isothiocyanate. Shown are bright-field (A and C) and fluorescent (B and D) images of hyphae from a mouse lavage fluid sample representative of 20 tested from separate mice (A and B) and of the positive control ( Candida hyphae incubated with anti- Candida antibody) (C and D).

    Article Snippet: The positive control included C. albicans hyphae incubated with purified rabbit anti- Candida IgG polyclonal antibody (Sigma) at a 1:10,000 dilution in PBS with 10% FBS for 1 h at room temperature followed by the same protocol using biotin-conjugated anti-rabbit immunoglobulins (Sigma) at a 1:10,000 dilution.

    Techniques: Infection, Mouse Assay, Incubation, Avidin-Biotin Assay, Positive Control

    Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and anti-SARS S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit IgG antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.

    Journal: Journal of Virology

    Article Title: Mucosal Immunization with Surface-Displayed Severe Acute Respiratory Syndrome Coronavirus Spike Protein on Lactobacillus casei Induces Neutralizing Antibodies in Mice

    doi: 10.1128/JVI.80.8.4079-4087.2006

    Figure Lengend Snippet: Construction and expression of chimeric S proteins. (A) A schematic diagram of pHAT:pgsA-SA and pHAT:pgsA-SB. (B) Western blot analyses of PgsA-SA (top) and PgsA-SB (bottom) expression in L. casei using anti-pgsA (left) and anti-SARS S (right) polyclonal antibodies. Lanes 1 and 2 show whole-cell lysates of wild-type (parental vector) and recombinant L. casei , respectively. Lanes 3 and 4 show cytoplasmic and membrane fractions of recombinant L. casei , respectively. Protein bands of ∼55 and 79 kDa, corresponding to the expected sizes of PgsA-SA and PgsA-SB, respectively, were detected in lanes 2 and 4. (C) Fluorescence-activated cell sorter histograms of wild-type (filled) and recombinant (open) L. casei cells. The cells were probed with either polyclonal rabbit anti-PgsA (top) or anti-SARS S (middle and bottom) polyclonal antibodies, followed by biotin-conjugated anti-rabbit IgG antibody and fluorescein isothiocyanate-conjugated streptavidin. (D) Representative immunofluorescence images of wild-type (control) and recombinant L. casei cells expressing PgsA-SA and PgsA-SB. Bright-field images are shown on the left.

    Article Snippet: The cell pellets were sequentially incubated with rabbit anti-SARS S polyclonal antibodies (1:1,000), biotin-conjugated anti-rabbit IgG secondary antibodies (1:1,000; Sigma, St. Louis, MO), and fluorescein-conjugated streptavidin (Vector Laboratories, Burlingame, CA).

    Techniques: Expressing, Western Blot, Plasmid Preparation, Recombinant, Fluorescence, Immunofluorescence

    SARS-CoV pseudovirus-neutralizing activity. Purified IgG from sera (A) and IgA from either intestinal or bronchoalveolar lavage fluids (B) were evaluated for SARS pseudovirus-neutralizing activities. Mice immunized either orally or intranasally were sampled at the indicated number of weeks after the first immunization. Approximately 100 infectious units of pseudovirus were used. Con., control; P.C., positive control. The assays were performed in duplicate, and the graphs are representative of two independent experiments. The error bars represent standard deviations.

    Journal: Journal of Virology

    Article Title: Mucosal Immunization with Surface-Displayed Severe Acute Respiratory Syndrome Coronavirus Spike Protein on Lactobacillus casei Induces Neutralizing Antibodies in Mice

    doi: 10.1128/JVI.80.8.4079-4087.2006

    Figure Lengend Snippet: SARS-CoV pseudovirus-neutralizing activity. Purified IgG from sera (A) and IgA from either intestinal or bronchoalveolar lavage fluids (B) were evaluated for SARS pseudovirus-neutralizing activities. Mice immunized either orally or intranasally were sampled at the indicated number of weeks after the first immunization. Approximately 100 infectious units of pseudovirus were used. Con., control; P.C., positive control. The assays were performed in duplicate, and the graphs are representative of two independent experiments. The error bars represent standard deviations.

    Article Snippet: The cell pellets were sequentially incubated with rabbit anti-SARS S polyclonal antibodies (1:1,000), biotin-conjugated anti-rabbit IgG secondary antibodies (1:1,000; Sigma, St. Louis, MO), and fluorescein-conjugated streptavidin (Vector Laboratories, Burlingame, CA).

    Techniques: Activity Assay, Purification, Mouse Assay, Positive Control

    Graphic representation showing correlation coefficients obtained by correlating the string of reactivity of serum IgG ofdifferent individuals to different microorganism, obtained in ELISA, at steady state. A) Professional athletes; B) Control group. Red colour–Pearson product-moment correlation coefficient, r = 1, Blue– r = -1.

    Journal: PLoS ONE

    Article Title: Profiling of microorganism-binding serum antibody specificities in professional athletes

    doi: 10.1371/journal.pone.0203665

    Figure Lengend Snippet: Graphic representation showing correlation coefficients obtained by correlating the string of reactivity of serum IgG ofdifferent individuals to different microorganism, obtained in ELISA, at steady state. A) Professional athletes; B) Control group. Red colour–Pearson product-moment correlation coefficient, r = 1, Blue– r = -1.

    Article Snippet: For IgG subclass analysis, Biotin Mouse Anti-Human IgG1, IgG2, IgG4 (BD Biosciences, CA, USA), and Monoclonal Anti-Human IgG3-Biotin antibody produced in mouse (Sigma Aldrich) were used.All secondary antibodies were incubated for 1 hour at RT.

    Techniques: Enzyme-linked Immunosorbent Assay

    Graphic representation showing correlation coefficients obtained by correlating the string of reactivity of serumtotal IgG and total IgA with IgG subclasses, for different microorganisms in professional athletes. A) Escherichia coli ATCC25922; B) Candida albicans ATCC 10259; C) Lactobacillus plantarum WCFS1; D) Salmonella typhimurium 2865; E) Lactobacillusrhamnosus LGG, F) LPS from E . coli O55:B5.

    Journal: PLoS ONE

    Article Title: Profiling of microorganism-binding serum antibody specificities in professional athletes

    doi: 10.1371/journal.pone.0203665

    Figure Lengend Snippet: Graphic representation showing correlation coefficients obtained by correlating the string of reactivity of serumtotal IgG and total IgA with IgG subclasses, for different microorganisms in professional athletes. A) Escherichia coli ATCC25922; B) Candida albicans ATCC 10259; C) Lactobacillus plantarum WCFS1; D) Salmonella typhimurium 2865; E) Lactobacillusrhamnosus LGG, F) LPS from E . coli O55:B5.

    Article Snippet: For IgG subclass analysis, Biotin Mouse Anti-Human IgG1, IgG2, IgG4 (BD Biosciences, CA, USA), and Monoclonal Anti-Human IgG3-Biotin antibody produced in mouse (Sigma Aldrich) were used.All secondary antibodies were incubated for 1 hour at RT.

    Techniques:

    Analysis of reactivity of serial dilutions of serum IgG in A) professional athletes; B) control group, and of serum IgA in C) professional athletes; D) control group to different microorganisms. Red colour– E . coli ATCC25922; black - C . albicans ATCC 10259; turquoise– L . plantarum WCFS1; green– S . typhimurium 2865; blue— L . rhamnosus LGG, violet—LPS from E . coli 055:B5.

    Journal: PLoS ONE

    Article Title: Profiling of microorganism-binding serum antibody specificities in professional athletes

    doi: 10.1371/journal.pone.0203665

    Figure Lengend Snippet: Analysis of reactivity of serial dilutions of serum IgG in A) professional athletes; B) control group, and of serum IgA in C) professional athletes; D) control group to different microorganisms. Red colour– E . coli ATCC25922; black - C . albicans ATCC 10259; turquoise– L . plantarum WCFS1; green– S . typhimurium 2865; blue— L . rhamnosus LGG, violet—LPS from E . coli 055:B5.

    Article Snippet: For IgG subclass analysis, Biotin Mouse Anti-Human IgG1, IgG2, IgG4 (BD Biosciences, CA, USA), and Monoclonal Anti-Human IgG3-Biotin antibody produced in mouse (Sigma Aldrich) were used.All secondary antibodies were incubated for 1 hour at RT.

    Techniques:

    The strings of reactivities (apsorbance) of IgG and IgA to bacteria from different individuals were correlated, and the Pearson product-moment correlation coefficientswereplotted for individual bacteria. Red colour- Professional athletes PA; Green colour–Control.

    Journal: PLoS ONE

    Article Title: Profiling of microorganism-binding serum antibody specificities in professional athletes

    doi: 10.1371/journal.pone.0203665

    Figure Lengend Snippet: The strings of reactivities (apsorbance) of IgG and IgA to bacteria from different individuals were correlated, and the Pearson product-moment correlation coefficientswereplotted for individual bacteria. Red colour- Professional athletes PA; Green colour–Control.

    Article Snippet: For IgG subclass analysis, Biotin Mouse Anti-Human IgG1, IgG2, IgG4 (BD Biosciences, CA, USA), and Monoclonal Anti-Human IgG3-Biotin antibody produced in mouse (Sigma Aldrich) were used.All secondary antibodies were incubated for 1 hour at RT.

    Techniques:

    Tetraspanins support EWI-2- α 3 β 1 integrin association. (A) ∼10 7 A431 EWI-2 cells were labeled with sulfo-NHS biotin and lysed in 1% Brij 96. Equal portions of lysate were depleted three times with protein G alone (mock) or with protein G plus anti- tetraspanin or α2 integrin antibodies. Depletions are indicated at the top of the figure. Depleted lysates were further divided and immunoprecipitated with anti-CD81, anti-α3 integrin, or anti-α2 integrin antibodies conjugated to agarose followed by SDS-PAGE and blotting with HRP-ExtrAvidin ® . EWI-2* is a 50-kD EWI-2 cleavage fragment. Densitometry revealed that CD9 and CD81 depletion removed only ∼10% of total α3 integrin, but ∼85% of the α3-associated EWI-2. Densitometry of an independent experiment confirmed that only ∼10% of α3 is CD81-associated in A431 cells (not depicted). (B) U937 cells lacking CD9 and CD81 were transduced with CD81 and EWI-2 retroviral expression vectors and selected to obtain stable (CD81−, EWI-2+) or (CD81+, EWI-2+) cell lines. Then, both cell types were super-infected with an α3 integrin retroviral expression vector, to yield equivalent α3 expression levels, as confirmed by flow cytometry (not depicted). EWI-2 (M2 anti-FLAG mAb), CD81 (M38 mAb), or α3 integrin (A3X8 mAb) were immunoprecipitated from 1% Brij 96 lysates of CD81 − or CD81 + cells. Immunoprecipitates were blotted for EWI-2 (biotinylated M2 anti-FLAG mAb), α3 integrin (D23 pAb), or CD81 (M38 mAb). Apparent mature and immature forms of EWI-2 and α3 integrin are indicated with filled and open arrows, respectively. 6 × 10 6 cell equivalents were analyzed in EWI-2 and CD81 immunoprecipitations, and 4.8 × 10 7 cell equivalents in the α3 immunoprecipitations. (C) Biotinylated CD81 − or CD81 + cells were lysed in 1% Brij 96, and EWI-2 (FLAG), α3 integrin, or CD81 were immunoprecipitated as above. Cell surface–labeled proteins were revealed by HRP-ExtrAvidin ® blot. 1.7 × 10 6 cell equivalents were analyzed in each immunoprecipitation.

    Journal: The Journal of Cell Biology

    Article Title: EWI-2 regulates ?3?1 integrin-dependent cell functions on laminin-5

    doi: 10.1083/jcb.200309113

    Figure Lengend Snippet: Tetraspanins support EWI-2- α 3 β 1 integrin association. (A) ∼10 7 A431 EWI-2 cells were labeled with sulfo-NHS biotin and lysed in 1% Brij 96. Equal portions of lysate were depleted three times with protein G alone (mock) or with protein G plus anti- tetraspanin or α2 integrin antibodies. Depletions are indicated at the top of the figure. Depleted lysates were further divided and immunoprecipitated with anti-CD81, anti-α3 integrin, or anti-α2 integrin antibodies conjugated to agarose followed by SDS-PAGE and blotting with HRP-ExtrAvidin ® . EWI-2* is a 50-kD EWI-2 cleavage fragment. Densitometry revealed that CD9 and CD81 depletion removed only ∼10% of total α3 integrin, but ∼85% of the α3-associated EWI-2. Densitometry of an independent experiment confirmed that only ∼10% of α3 is CD81-associated in A431 cells (not depicted). (B) U937 cells lacking CD9 and CD81 were transduced with CD81 and EWI-2 retroviral expression vectors and selected to obtain stable (CD81−, EWI-2+) or (CD81+, EWI-2+) cell lines. Then, both cell types were super-infected with an α3 integrin retroviral expression vector, to yield equivalent α3 expression levels, as confirmed by flow cytometry (not depicted). EWI-2 (M2 anti-FLAG mAb), CD81 (M38 mAb), or α3 integrin (A3X8 mAb) were immunoprecipitated from 1% Brij 96 lysates of CD81 − or CD81 + cells. Immunoprecipitates were blotted for EWI-2 (biotinylated M2 anti-FLAG mAb), α3 integrin (D23 pAb), or CD81 (M38 mAb). Apparent mature and immature forms of EWI-2 and α3 integrin are indicated with filled and open arrows, respectively. 6 × 10 6 cell equivalents were analyzed in EWI-2 and CD81 immunoprecipitations, and 4.8 × 10 7 cell equivalents in the α3 immunoprecipitations. (C) Biotinylated CD81 − or CD81 + cells were lysed in 1% Brij 96, and EWI-2 (FLAG), α3 integrin, or CD81 were immunoprecipitated as above. Cell surface–labeled proteins were revealed by HRP-ExtrAvidin ® blot. 1.7 × 10 6 cell equivalents were analyzed in each immunoprecipitation.

    Article Snippet: The M2 anti-FLAG epitope mAb, either biotinylated or conjugated to agarose, and a rabbit anti-FLAG pAb were purchased from Sigma-Aldrich.

    Techniques: Labeling, Immunoprecipitation, SDS Page, Transduction, Expressing, Infection, Plasmid Preparation, Flow Cytometry, Cytometry

    Biochemical analysis of the EW2xCD2c chimera. (A) Wild-type and mutant EWI proteins were immunoprecipitated using anti-FLAG antibody, and then samples were analyzed by blotting using anti-α3, anti-CD81 (M38), and anti-FLAG pAbs. CD81 coprecipitating with EWI-2 is indicated with a small black arrow (middle). On the bottom, dark arrows indicate mature EWI proteins, and white arrows indicate immature forms. (B) From Brij 96 lysates of 10 6 cell surface–biotinylated, transduced A431 cells, EWI proteins were immunoprecipitated using anti-FLAG antibody, and then analyzed by HRP-ExtrAvidin ® blotting. The locations of α3 integrin, intact EW2xCD2c, intact EWI-2, CD9, and CD81 are indicated. Two exposures of the same blot are presented to allow comparison of the relative amounts of α3, CD9, and CD81 that coprecipitate with each protein. Note that intact EW2xCD2 (∼78 kD) and intact EWI-2 (∼70 kD) are each accompanied by two smaller cleavage products. (C) 3.6 × 10 6 A431 cells expressing EW2xCD2c or EWI-2were lysed in Brij 96, and the indicated proteins were immunoprecipitated. Samples were then immunoblotted for FLAG (M2 anti-FLAG mAb) or CD81 as above. In all cases, small differences in total protein in the lysates were measured by amido black assay and corrected before immunoprecipitation. Lanes 1* and 2* represent shorter exposures of lanes 5 and 6, respectively. (D) α3 integrin was immunoprecipitated from Brij 96 lysates of 3.3 × 10 5 transduced A431 cells. Levels of CD81 and α3 within the immunoprecipitates were revealed by immunoblotting with M38 anti-CD81 mAb (top) or with anti-α3 pAb (bottom).

    Journal: The Journal of Cell Biology

    Article Title: EWI-2 regulates ?3?1 integrin-dependent cell functions on laminin-5

    doi: 10.1083/jcb.200309113

    Figure Lengend Snippet: Biochemical analysis of the EW2xCD2c chimera. (A) Wild-type and mutant EWI proteins were immunoprecipitated using anti-FLAG antibody, and then samples were analyzed by blotting using anti-α3, anti-CD81 (M38), and anti-FLAG pAbs. CD81 coprecipitating with EWI-2 is indicated with a small black arrow (middle). On the bottom, dark arrows indicate mature EWI proteins, and white arrows indicate immature forms. (B) From Brij 96 lysates of 10 6 cell surface–biotinylated, transduced A431 cells, EWI proteins were immunoprecipitated using anti-FLAG antibody, and then analyzed by HRP-ExtrAvidin ® blotting. The locations of α3 integrin, intact EW2xCD2c, intact EWI-2, CD9, and CD81 are indicated. Two exposures of the same blot are presented to allow comparison of the relative amounts of α3, CD9, and CD81 that coprecipitate with each protein. Note that intact EW2xCD2 (∼78 kD) and intact EWI-2 (∼70 kD) are each accompanied by two smaller cleavage products. (C) 3.6 × 10 6 A431 cells expressing EW2xCD2c or EWI-2were lysed in Brij 96, and the indicated proteins were immunoprecipitated. Samples were then immunoblotted for FLAG (M2 anti-FLAG mAb) or CD81 as above. In all cases, small differences in total protein in the lysates were measured by amido black assay and corrected before immunoprecipitation. Lanes 1* and 2* represent shorter exposures of lanes 5 and 6, respectively. (D) α3 integrin was immunoprecipitated from Brij 96 lysates of 3.3 × 10 5 transduced A431 cells. Levels of CD81 and α3 within the immunoprecipitates were revealed by immunoblotting with M38 anti-CD81 mAb (top) or with anti-α3 pAb (bottom).

    Article Snippet: The M2 anti-FLAG epitope mAb, either biotinylated or conjugated to agarose, and a rabbit anti-FLAG pAb were purchased from Sigma-Aldrich.

    Techniques: Mutagenesis, Immunoprecipitation, Expressing