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Becton Dickinson mouse igg2a isotype control
Citrullinated fibrinogen peptides recognized by the sera of C57BL/6 mice immunized with mPAD2 . Sera diluted to 1/80 from mice immunized with mPAD2 (A) or PBS (B) were tested by ELISA for <t>IgG</t> response to peptides under arginine (R) or citrullinated form (C) at 120 days postfirst immunization. OD was read at 405 nm. A positive serum (red squares) was defined by a test OD/background OD ratio higher than 2. Each line reports data from one <t>mouse.</t> Data are combined from a single experiment with 74 mice per experiment.
Mouse Igg2a Isotype Control, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 86/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "PAD2 immunization induces ACPA in wild‐type and HLA‐DR4 humanized mice"

Article Title: PAD2 immunization induces ACPA in wild‐type and HLA‐DR4 humanized mice

Journal: European Journal of Immunology

doi: 10.1002/eji.202249889

Citrullinated fibrinogen peptides recognized by the sera of C57BL/6 mice immunized with mPAD2 . Sera diluted to 1/80 from mice immunized with mPAD2 (A) or PBS (B) were tested by ELISA for IgG response to peptides under arginine (R) or citrullinated form (C) at 120 days postfirst immunization. OD was read at 405 nm. A positive serum (red squares) was defined by a test OD/background OD ratio higher than 2. Each line reports data from one mouse. Data are combined from a single experiment with 74 mice per experiment.
Figure Legend Snippet: Citrullinated fibrinogen peptides recognized by the sera of C57BL/6 mice immunized with mPAD2 . Sera diluted to 1/80 from mice immunized with mPAD2 (A) or PBS (B) were tested by ELISA for IgG response to peptides under arginine (R) or citrullinated form (C) at 120 days postfirst immunization. OD was read at 405 nm. A positive serum (red squares) was defined by a test OD/background OD ratio higher than 2. Each line reports data from one mouse. Data are combined from a single experiment with 74 mice per experiment.

Techniques Used: Mouse Assay, Enzyme-linked Immunosorbent Assay

T‐cell proliferation to mPAD2 is inhibited by anti‐HLA‐DR and/or anti‐I‐A b . Cells from spleen and lymph nodes obtained at 120 days after first immunization were cultured at a density of 5 × 10 6 cells with 2 μg of mPAD2, with anti‐HLA‐DR or anti‐I‐A b antibodies or control IgG. T‐cell responses were evaluated by BrdU incorporation. Data are combined from three experiments with eight mice per experiment. Positive T‐cell responses were defined by test OD/background OD ratio higher than 2 (dotted line).
Figure Legend Snippet: T‐cell proliferation to mPAD2 is inhibited by anti‐HLA‐DR and/or anti‐I‐A b . Cells from spleen and lymph nodes obtained at 120 days after first immunization were cultured at a density of 5 × 10 6 cells with 2 μg of mPAD2, with anti‐HLA‐DR or anti‐I‐A b antibodies or control IgG. T‐cell responses were evaluated by BrdU incorporation. Data are combined from three experiments with eight mice per experiment. Positive T‐cell responses were defined by test OD/background OD ratio higher than 2 (dotted line).

Techniques Used: Cell Culture, BrdU Incorporation Assay, Mouse Assay

IgG response to mPAD2 in C57BL/6 mice immunized with mPAD2 . Sera diluted to 1/40 from mice immunized with mPAD2 were tested by ELISA for IgG response to mPAD2 at 15, 30, 45, 75, 105, and 120 days (d) after first immunization. OD was read at 405 nm. A ratio test OD/background OD (see Material and Methods) equal or higher than 2 defined positive sera (dotted line). Data are combined from two experiments with 38 mice per experiment. Each black dot represents result from a mouse. Means and SD (in red) were calculated for each group of mice. Asterisks represent significant Mann–Whitney p values (* p = 0.01, ** p = 0.001, *** p = 0.0001, **** p
Figure Legend Snippet: IgG response to mPAD2 in C57BL/6 mice immunized with mPAD2 . Sera diluted to 1/40 from mice immunized with mPAD2 were tested by ELISA for IgG response to mPAD2 at 15, 30, 45, 75, 105, and 120 days (d) after first immunization. OD was read at 405 nm. A ratio test OD/background OD (see Material and Methods) equal or higher than 2 defined positive sera (dotted line). Data are combined from two experiments with 38 mice per experiment. Each black dot represents result from a mouse. Means and SD (in red) were calculated for each group of mice. Asterisks represent significant Mann–Whitney p values (* p = 0.01, ** p = 0.001, *** p = 0.0001, **** p

Techniques Used: Mouse Assay, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY

IgG response to mPAD2 in C57BL/6 mice immunized with PBS . Sera diluted to 1/40 from mice immunized with PBS were tested by ELISA for IgG response to mPAD2 at 15, 30, 45, 75, 105, and 120 days (d) after first immunization. OD was read at 405 nm. A ratio test OD/background OD (see Materials and Methods) equal or higher than 2 defined positive sera (dotted line). Each black dot represents result from a mouse. Data are combined from two experiments with 36 mice per experiment. Means and SD (in red) were calculated for each group of mice.
Figure Legend Snippet: IgG response to mPAD2 in C57BL/6 mice immunized with PBS . Sera diluted to 1/40 from mice immunized with PBS were tested by ELISA for IgG response to mPAD2 at 15, 30, 45, 75, 105, and 120 days (d) after first immunization. OD was read at 405 nm. A ratio test OD/background OD (see Materials and Methods) equal or higher than 2 defined positive sera (dotted line). Each black dot represents result from a mouse. Data are combined from two experiments with 36 mice per experiment. Means and SD (in red) were calculated for each group of mice.

Techniques Used: Mouse Assay, Enzyme-linked Immunosorbent Assay

2) Product Images from "C-Reactive Protein Binds to Cholesterol Crystals and Co-Localizes with the Terminal Complement Complex in Human Atherosclerotic Plaques"

Article Title: C-Reactive Protein Binds to Cholesterol Crystals and Co-Localizes with the Terminal Complement Complex in Human Atherosclerotic Plaques

Journal: Frontiers in Immunology

doi: 10.3389/fimmu.2017.01040

Phagocytosis of CCs by granulocytes (A) and monocytes (B) in whole blood is complement dependent and depends on C1q binding. Hirudin whole blood, preincubated 5 min with the C3 inhibitor Compstatin, Cp40, the C5 inhibitor Eculizumab, a C1q inhibitory antibody (C1q Inhib Ab), or a mouse antibody as control (Ms IgG). Whole blood was stimulated with PBS or CC. Phagocytosis was determined as percentage of cells phagocytosing CC determined as a shift in side scatter and by the expression of CR3 measured as MFI. Granulocytes and monocytes were gated based on CD14 expression. Data are given as mean ± SD ( n = 3 healthy donors). * p
Figure Legend Snippet: Phagocytosis of CCs by granulocytes (A) and monocytes (B) in whole blood is complement dependent and depends on C1q binding. Hirudin whole blood, preincubated 5 min with the C3 inhibitor Compstatin, Cp40, the C5 inhibitor Eculizumab, a C1q inhibitory antibody (C1q Inhib Ab), or a mouse antibody as control (Ms IgG). Whole blood was stimulated with PBS or CC. Phagocytosis was determined as percentage of cells phagocytosing CC determined as a shift in side scatter and by the expression of CR3 measured as MFI. Granulocytes and monocytes were gated based on CD14 expression. Data are given as mean ± SD ( n = 3 healthy donors). * p

Techniques Used: Binding Assay, Inhibition, Mass Spectrometry, Expressing

3) Product Images from "Regulation of Human Osteoclast Development by Dendritic Cell- Specific Tr ans membrane Protein (DC-STAMP)"

Article Title: Regulation of Human Osteoclast Development by Dendritic Cell- Specific Tr ans membrane Protein (DC-STAMP)

Journal: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research

doi: 10.1002/jbmr.531

DC-STAMP proteins are phosphorylated on tyrosine residues, interact with SHP-1 and CD16, and may be involved in signal transduction (A) Proteins were isolated from fresh human monocytes, immunoprecipitated (IP) with anti-DC-STAMP antibody 1A2 (lane 2) or with anti-CD16 antibody (lane 3). IP lysates were analyzed by SDS-PAGE followed by immunoblotting (IB) with 1A2. Arrow shows the DC-STAMP band (~53 kDa). (B) Proteins were isolated from fresh human monocytes, IP with anti-SHP1 antibody (lane 2) or with the control antibody mouse IgG (lane 3). IP lysates were analyzed by SDS-PAGE followed by IB with 1A2. Arrow shows the DC-STAMP band (~53 kDa). (C) Proteins were isolated from fresh human monocytes, IP with mouse IgG2a (lane 2), or anti-SHP1 antibody (lane3) or anti-DC-STAMP antibody 1A2 (lane 4). IP lysates were analyzed by SDS-PAGE followed by IB with anti-phosphotyrosine antibody 4G10. The bands of SHP-1 (~70 kDa) and DC-STAMP (~53 kDa) are marked by arrows. (D) Examination of 1A2 effects on DC-STAMP signaling. (I) Human monocytes were cultured in OC-promoting media (RANKL+M-CSF) in the absence (lanes 2 and 4) or presence (lanes 3 and 5) of 1A2 for 8 days. Proteins were isolated and IP with mouse IgG2a (lanes 2 and 3) or with anti-SHP-1 antibody (lanes 4 and 5), and subjected to SDS-PAGE, followed by IB with anti-phosphotyrosine antibody 4G10. Arrow indicates the location of the SHP-1 band. (II) Purified human monocytes were cultured in OC-promoting media (RANKL+M-CSF) in the absence (a to c) or the presence of 1A2 (d to f), or in the presence of mouse IgG2a isotype control (g to i). Cells were harvested and analyzed at 3 different time points (16hrs: a d; 40 hrs: b e; 64 hrs: c f) for phosphorylated PLC-γ2 expression by intracellular staining with the anti- PLC- γ2 antibody (pY759) and flow cytometric analysis.
Figure Legend Snippet: DC-STAMP proteins are phosphorylated on tyrosine residues, interact with SHP-1 and CD16, and may be involved in signal transduction (A) Proteins were isolated from fresh human monocytes, immunoprecipitated (IP) with anti-DC-STAMP antibody 1A2 (lane 2) or with anti-CD16 antibody (lane 3). IP lysates were analyzed by SDS-PAGE followed by immunoblotting (IB) with 1A2. Arrow shows the DC-STAMP band (~53 kDa). (B) Proteins were isolated from fresh human monocytes, IP with anti-SHP1 antibody (lane 2) or with the control antibody mouse IgG (lane 3). IP lysates were analyzed by SDS-PAGE followed by IB with 1A2. Arrow shows the DC-STAMP band (~53 kDa). (C) Proteins were isolated from fresh human monocytes, IP with mouse IgG2a (lane 2), or anti-SHP1 antibody (lane3) or anti-DC-STAMP antibody 1A2 (lane 4). IP lysates were analyzed by SDS-PAGE followed by IB with anti-phosphotyrosine antibody 4G10. The bands of SHP-1 (~70 kDa) and DC-STAMP (~53 kDa) are marked by arrows. (D) Examination of 1A2 effects on DC-STAMP signaling. (I) Human monocytes were cultured in OC-promoting media (RANKL+M-CSF) in the absence (lanes 2 and 4) or presence (lanes 3 and 5) of 1A2 for 8 days. Proteins were isolated and IP with mouse IgG2a (lanes 2 and 3) or with anti-SHP-1 antibody (lanes 4 and 5), and subjected to SDS-PAGE, followed by IB with anti-phosphotyrosine antibody 4G10. Arrow indicates the location of the SHP-1 band. (II) Purified human monocytes were cultured in OC-promoting media (RANKL+M-CSF) in the absence (a to c) or the presence of 1A2 (d to f), or in the presence of mouse IgG2a isotype control (g to i). Cells were harvested and analyzed at 3 different time points (16hrs: a d; 40 hrs: b e; 64 hrs: c f) for phosphorylated PLC-γ2 expression by intracellular staining with the anti- PLC- γ2 antibody (pY759) and flow cytometric analysis.

Techniques Used: Transduction, Isolation, Immunoprecipitation, SDS Page, Cell Culture, Purification, Planar Chromatography, Expressing, Staining, Flow Cytometry

Functional characterization of anti-DC-STAMP mAb 1A2 (A) A positive association was noted between DC-STAMP and CD16 expression. CD14+CD16+ monocytes demonstrated a higher surface expression of DC-STAMP than CD14+CD16-cells. Human PBMC were purified by Ficoll gradient and stained with an antibody cocktail composed of 7-AAD, anti-DC-STAMP and anti-CD16 antibodies. The expression of DC-STAMP on unstained, isotype control, CD14+CD16- and CD14+CD16+ cells are labeled in red, blue, orange and green, respectively. Commercially available anti-DC-STAMP polyclonal antibody KR104 was used for this analysis. (B) Lane 2: total proteins isolated from the RAW cell line; lane 3: proteins isolated from a RAW cell line expressing the PTHR-DC-STAMP fusion protein; lane 4: immunoprecipitated human monocyte proteins by 1A2; lane 5: immunoprecipitated human monocyte proteins by mouse IgG2a. All proteins were denatured, separated by 10% gradient protein gel, and probed with the anti-DC-STAMP mAb 1A2 on western blots. Pink and blue asterisks label the PTHR-DC-STAMP fusion protein and DC-STAMP native protein, respectively. (C) DC-STAMP expression on human PBMC and multinucleated giant cells from giant cell tumor of bone was detected by immunohistochemical (IHC) staining using 1A2, (a) (b). Human PBMC were purified by Ficoll gradient, embedded in paraffin for section, and stained with (a) mouse IgG2a isotype control, or (b) 1A2. (c) (d). Human biopsy samples collected from giant cell tumor were sectioned, and stained with (c) mouse IgG2a isotype control, or (d) 1A2. Both 1A2 and mouse IgG2a isotype control were diluted at 1:1500 for staining. The polarized expression of DC-STAMP in the multinucleated giant cells from a giant cell tumor was labeled by arrows. (D) The anti-DC-STAMP mAb 1A2 was able to block OC formation in vitro. Enriched human monocytes were cultured in the absence (a) or presence (b) of 1A2 for 8 days and TRAP-stained for visualization and enumeration of OC. (c) Enriched human monocytes and PBMC isolated from different subjects were cultured in the absence (open bar), presence of 1A2 (solid bar) or with IgG2a isotype control (slash bar) for 8 days. The concentrations of 1A2 used for monocytes and PBMC were 15 μg/ml and 150 μg/ml, respectively.
Figure Legend Snippet: Functional characterization of anti-DC-STAMP mAb 1A2 (A) A positive association was noted between DC-STAMP and CD16 expression. CD14+CD16+ monocytes demonstrated a higher surface expression of DC-STAMP than CD14+CD16-cells. Human PBMC were purified by Ficoll gradient and stained with an antibody cocktail composed of 7-AAD, anti-DC-STAMP and anti-CD16 antibodies. The expression of DC-STAMP on unstained, isotype control, CD14+CD16- and CD14+CD16+ cells are labeled in red, blue, orange and green, respectively. Commercially available anti-DC-STAMP polyclonal antibody KR104 was used for this analysis. (B) Lane 2: total proteins isolated from the RAW cell line; lane 3: proteins isolated from a RAW cell line expressing the PTHR-DC-STAMP fusion protein; lane 4: immunoprecipitated human monocyte proteins by 1A2; lane 5: immunoprecipitated human monocyte proteins by mouse IgG2a. All proteins were denatured, separated by 10% gradient protein gel, and probed with the anti-DC-STAMP mAb 1A2 on western blots. Pink and blue asterisks label the PTHR-DC-STAMP fusion protein and DC-STAMP native protein, respectively. (C) DC-STAMP expression on human PBMC and multinucleated giant cells from giant cell tumor of bone was detected by immunohistochemical (IHC) staining using 1A2, (a) (b). Human PBMC were purified by Ficoll gradient, embedded in paraffin for section, and stained with (a) mouse IgG2a isotype control, or (b) 1A2. (c) (d). Human biopsy samples collected from giant cell tumor were sectioned, and stained with (c) mouse IgG2a isotype control, or (d) 1A2. Both 1A2 and mouse IgG2a isotype control were diluted at 1:1500 for staining. The polarized expression of DC-STAMP in the multinucleated giant cells from a giant cell tumor was labeled by arrows. (D) The anti-DC-STAMP mAb 1A2 was able to block OC formation in vitro. Enriched human monocytes were cultured in the absence (a) or presence (b) of 1A2 for 8 days and TRAP-stained for visualization and enumeration of OC. (c) Enriched human monocytes and PBMC isolated from different subjects were cultured in the absence (open bar), presence of 1A2 (solid bar) or with IgG2a isotype control (slash bar) for 8 days. The concentrations of 1A2 used for monocytes and PBMC were 15 μg/ml and 150 μg/ml, respectively.

Techniques Used: Functional Assay, Expressing, Purification, Staining, Labeling, Isolation, Immunoprecipitation, Western Blot, Immunohistochemistry, Blocking Assay, In Vitro, Cell Culture

4) Product Images from "NK cells engineered to express a GD2-specific antigen receptor display built-in ADCC-like activity against tumour cells of neuroectodermal origin"

Article Title: NK cells engineered to express a GD2-specific antigen receptor display built-in ADCC-like activity against tumour cells of neuroectodermal origin

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/j.1582-4934.2011.01343.x

Transduction of NK-92 cells with retroviral vectors encoding chimeric scFv(ch14.18)-ζ antigen receptors. (A) Schematic representation of pL-scFv(ch14.18)-ζ-SN constructs. The Moloney murine leukaemia virus 5′ long terminal repeat (LTR) controls the expression of chimeric scFv(ch14.18)-ζ antigen receptors which consist of an N-terminal immunoglobulin heavy-chain leader peptide (signal peptide), a GD 2 -specific single-chain antibody scFv(ch14.18) with heavy (V H ) and light chain (V L ) variable domains in V H -linker-V L (HL) or V L -linker-V H (LH) orientation, a Myc-tag, the hinge region of CD8α and the CD3-ζ chain. The neomycin-resistance gene for G418 selection of transduced cells is driven by the SV40 early promoter. (B) Surface expression of chimeric scFv(ch14.18)-ζ antigen receptors. After G418 selection of transduced cells (G418), NK-92-scFv(ch14.18)HL-ζ and NK-92-scFv(ch14.18)LH-ζ cells expressing homogenous levels of the CARs on their surface were enriched by immunomagnetic separation with mAb 9E10 and goat antimouse IgG-coated magnetic beads (MACS). Single cell clones were derived by limiting dilution (LD). Representative clones are shown. After each selection step, surface expression of scFv(ch14.18)-ζ receptors was determined by flow cytometry using mAb 9E10 and FITC-labelled goat antimouse secondary antibody. NK-92 cells transduced with empty pLXSN served as a control.
Figure Legend Snippet: Transduction of NK-92 cells with retroviral vectors encoding chimeric scFv(ch14.18)-ζ antigen receptors. (A) Schematic representation of pL-scFv(ch14.18)-ζ-SN constructs. The Moloney murine leukaemia virus 5′ long terminal repeat (LTR) controls the expression of chimeric scFv(ch14.18)-ζ antigen receptors which consist of an N-terminal immunoglobulin heavy-chain leader peptide (signal peptide), a GD 2 -specific single-chain antibody scFv(ch14.18) with heavy (V H ) and light chain (V L ) variable domains in V H -linker-V L (HL) or V L -linker-V H (LH) orientation, a Myc-tag, the hinge region of CD8α and the CD3-ζ chain. The neomycin-resistance gene for G418 selection of transduced cells is driven by the SV40 early promoter. (B) Surface expression of chimeric scFv(ch14.18)-ζ antigen receptors. After G418 selection of transduced cells (G418), NK-92-scFv(ch14.18)HL-ζ and NK-92-scFv(ch14.18)LH-ζ cells expressing homogenous levels of the CARs on their surface were enriched by immunomagnetic separation with mAb 9E10 and goat antimouse IgG-coated magnetic beads (MACS). Single cell clones were derived by limiting dilution (LD). Representative clones are shown. After each selection step, surface expression of scFv(ch14.18)-ζ receptors was determined by flow cytometry using mAb 9E10 and FITC-labelled goat antimouse secondary antibody. NK-92 cells transduced with empty pLXSN served as a control.

Techniques Used: Transduction, Construct, Expressing, Selection, Immunomagnetic Separation, Magnetic Beads, Magnetic Cell Separation, Clone Assay, Derivative Assay, Flow Cytometry, Cytometry

5) Product Images from "The First Propeller Domain of LRP6 Regulates Sensitivity to DKK1"

Article Title: The First Propeller Domain of LRP6 Regulates Sensitivity to DKK1

Journal: Molecular Biology of the Cell

doi: 10.1091/mbc.E08-12-1252

mAb135 antagonizes DKK1. HEK293 A6 cells were incubated with increasing amounts of mAb135 IgG (A), mAb135 Fab (B), or isotype control antibody before treament with Wnt3A (200 ng/ml) in the presence or absence of DKK1 (400 ng/ml). HEK293 A6 cells were
Figure Legend Snippet: mAb135 antagonizes DKK1. HEK293 A6 cells were incubated with increasing amounts of mAb135 IgG (A), mAb135 Fab (B), or isotype control antibody before treament with Wnt3A (200 ng/ml) in the presence or absence of DKK1 (400 ng/ml). HEK293 A6 cells were

Techniques Used: Incubation

mAb135 enhances Wnt signaling. (A) HEK 293 A6 stable 16TCF reporter cells were treated with media control or Wnt3A (200 ng/ml) in the presence of increasing concentrations of mAb135 IgG, mAb135 Fab, or isotype control IgG. (B) HEK 293 A6 cells were treated
Figure Legend Snippet: mAb135 enhances Wnt signaling. (A) HEK 293 A6 stable 16TCF reporter cells were treated with media control or Wnt3A (200 ng/ml) in the presence of increasing concentrations of mAb135 IgG, mAb135 Fab, or isotype control IgG. (B) HEK 293 A6 cells were treated

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