invivo mab rat igg2a isotype control antibody clone 2a3  (Bio X Cell)

Journal: Nature Communications

Article Title: CD200R1-CD200 checkpoint inhibits phagocytosis differently from SIRPα-CD47 to suppress tumor growth

doi: 10.1038/s41467-025-60456-3

Figure Lengend Snippet: a Mass spectrometry analysis of CD11b immunoprecipitates from BMDMs. Left: experimental workflow for isolating the CD11b-interacting proteins. Right: relative abundance of CD11b-interacting proteins, with a focus on cell surface receptors with inhibitory potential, indicated by a color gradient. ITIM, immunoreceptor tyrosine-based inhibitory motif; ITSM, immunoreceptor tyrosine-based switch motif; NPXY, asparagine, proline, any residue, tyrosine. IP, immunoprecipitation. b Immunoblot analysis of CD11b and CD200R1 interaction in immunoprecipitates from WT, Itgb2 −/− and Cd200r1 −/− BMDMs. Relative abundance is shown at the bottom of each panel. c Flow cytometry analysis of CD200 expression on parental (top) and Tac expression on Tac + (bottom) mouse tumor cell lines. Red curves represent staining with CD200 or Tac mAbs. Filled curves, control (Ctrl) mAbs. d Microscopy-based phagocytosis assay of non-opsonized (−) or IgG-opsonized (+) Tac + WEHI-231, Tac + A20, Tac + J558 and Tac + TUBO cells by WT BMDMs, in presence of CD200 mAb OX-90 (rat IgG2a) or Ctrl mAb 2A3 (rat IgG2a). Tumor cells were opsonized with Tac mAb 7G7 (mouse IgG2a), ( n = 3). e Time-course pHrodo-based phagocytosis assay using IgG-opsonized Tac + WEHI-231 cells and WT BMDMs. WEHI-231 cells were labeled with pHrodo red dye, and BMDMs were labeled with CSFE. Phagocytosis over time (0-4 h) was analyzed using an IncuCyte Live Cell Analyzer. Left: representative images at 2 h (scale bar, 100 μm; arrows, BMDMs with engulfed tumor cells). Right: quantification of cumulative phagocytosis (top) and time-specific increase in phagocytosis (Δ phagocytosis; bottom) over 0-4 h, ( n = 3). f Confocal microscope-based conjugate formation and actin polarization assay of IgG-opsonized WEHI-231 cells labeled with CSFE (green) and co-incubated with WT BMDMs labeled with Cell Trace Violet (CTV; blue), in presence of CD200 mAb or Ctrl mAb. Actin (red) was detected by β-actin mAb. Left: representative images (scale bar, 10 μm; arrows, BMDMs with fully polarized actin). Scale, 10 μm. Right: quantification of conjugate formation (top) and of conjugates with fully polarized actin (bottom), ( n = 3). g As per Fig. 1d, except that phagocytosis of complement (C3bi)-opsonized WEHI-231 cells by WT BMDMs in the presence of blocking CD200 mAb OX-90, blocking CD11b mAb 5C6 (rat IgG2b), Ctrl mAb 2A3 or Ctrl mAb LTF-2 (rat IgG2b), ( n = 3). h As per Fig. 1d, expect that phagocytosis of IgG-opsonized WEHI-231 cells by WT BMDMs in the presence of CD200R1 mAb OX-131 (mouse IgG1, Fc-silent) or Ctrl mAb (mouse IgG1, Fc-silent), ( n = 3). Data are from three ( a – h ) independent experiments. Each symbol represents one mouse. Data are presented as mean ± s.e.m. Statistical analysis: two-tailed t -test ( d – f , h ) with multiple comparisons ( e ); One-way ANOVA test with multiple comparisons ( g ); ns, not significant. See also Supplementary Fig. and Supplementary Table .

Article Snippet: For phagocytosis assays and in vivo assays, the following mAbs were used: CD200 mAb OX-90 (BioXCell, Lebanon, NH); CD200R1 mAb OX-131 (Absolute Antibody, Boston, MA), SIRPα mAb no. 27 ; rat IgG2b isotype Ctrl mAb LTF-2 (BioXCell); rat IgG2a isotype Ctrl mAb 2A3 (BioXCell); Ctrl mAb MOPC-21 (in-house generated); and blocking CD11b mAb 5C6 (BioXCell).

Techniques: Mass Spectrometry, Residue, Immunoprecipitation, Western Blot, Flow Cytometry, Expressing, Staining, Control, Microscopy, Phagocytosis Assay, Labeling, Incubation, Blocking Assay, Two Tailed Test

Journal: Nature Communications

Article Title: CD200R1-CD200 checkpoint inhibits phagocytosis differently from SIRPα-CD47 to suppress tumor growth

doi: 10.1038/s41467-025-60456-3

Figure Lengend Snippet: a Flow cytometry analysis of CD200R1 expression (left) on WT (top) or Cd200r1 −/− (bottom) BMDMs, and CD200 expression (right) on Cd200 +/+ (top) or Cd200 −/− (bottom) WEHI-231 cells, as measured by flow cytometry. Red curves, CD200R1 or CD200 mAbs. Filled curves, Ctrl mAb. b As per Fig. , except that phagocytosis of IgG-opsonized WEHI-231 cells in the presence of WT or Cd200r1 −/− BMDMs was studied, ( n = 3). c As per Fig. 2b, except that phagocytosis of IgG-opsonized Cd200 +/+ and Cd200 −/− WEHI-231 cells, in the presence of WT or Cd200r1 −/− BMDMs, ( n = 3). Data are from three independent experiments ( a – c ). Each symbol represents one mouse. Data are mean ± s.e.m. Statistical analysis: two-way ANOVA test, with multiple comparisons ( b , c ), ns not significant. See also Supplementary Fig. .

Article Snippet: For phagocytosis assays and in vivo assays, the following mAbs were used: CD200 mAb OX-90 (BioXCell, Lebanon, NH); CD200R1 mAb OX-131 (Absolute Antibody, Boston, MA), SIRPα mAb no. 27 ; rat IgG2b isotype Ctrl mAb LTF-2 (BioXCell); rat IgG2a isotype Ctrl mAb 2A3 (BioXCell); Ctrl mAb MOPC-21 (in-house generated); and blocking CD11b mAb 5C6 (BioXCell).

Techniques: Flow Cytometry, Expressing

Journal: Nature Communications

Article Title: CD200R1-CD200 checkpoint inhibits phagocytosis differently from SIRPα-CD47 to suppress tumor growth

doi: 10.1038/s41467-025-60456-3

Figure Lengend Snippet: a Flow cytometry analysis of CD200 (top) or tumor antigens (CD20, CD38, CD123, DLL3 and SLAMF7; bottom) on various human tumor cell lines. Red curves, CD200 mAb or tumor antigen-specific mAbs. Filled curves, Ctrl mAbs. b As per Fig. , except using IL-4-primed human blood monocyte-derived macrophages and human tumor cells in the presence of samalizumab (human IgG1, Fc-silent) or Ctrl mAb MOPC21 (human IgG1, Fc-silent). IgG opsonization was performed using CD20 mAb rituximab (SLVL, 721.221), CD38 mAb daratumumab (NCI-H929), CD123 mAb talacotuzumab (KG-1a), DLL3 mAb rovalpituzumab (NCI-H209), or SLAMF7 mAb elotuzumab (SK-MEL-28) ( n = 3 or 4). c As per Fig. 5b, except using the indicated cell lines and samalizumab (human IgG1, Fc-silent), CD47 mAb B6H12 (human IgG1, Fc-silent), or Ctrl mAb MOPC21 (human IgG1, Fc-silent). Tumor cells were opsonized as detailed for Fig. 5b, ( n = 3). d –f Subcutaneous injection of SLVL cells in NSG mice, followed by intraperitoneal injection of rituximab (mouse IgG2a version) combined with samalizumab or Ctrl mAb every 2 days, ( n = 8). d Schematic representation of the experimental workflow. e Tumor volume over time. f Tumor weight. g –i Subcutaneous injection of 721.221 cells in NSG mice, followed by intraperitoneal injection of rituximab (mouse IgG2a version) combined with samalizumab or Ctrl mAbs every 2 days, ( n = 10). g Schematic representation of the experimental workflow. h Tumor volume over time. i Tumor weight. Data are from three to four ( a, b ), three ( c ), or two ( d-i ) independent experiments. Each symbol represents one human sample or one mouse. Data are presented as mean ± s.e.m. Statistical analysis: two-tailed t-test ( f , i ), with multiple comparisons ( b, c , e , h ). ns, not significant. See also Supplementary Fig. .

Article Snippet: For phagocytosis assays and in vivo assays, the following mAbs were used: CD200 mAb OX-90 (BioXCell, Lebanon, NH); CD200R1 mAb OX-131 (Absolute Antibody, Boston, MA), SIRPα mAb no. 27 ; rat IgG2b isotype Ctrl mAb LTF-2 (BioXCell); rat IgG2a isotype Ctrl mAb 2A3 (BioXCell); Ctrl mAb MOPC-21 (in-house generated); and blocking CD11b mAb 5C6 (BioXCell).

Techniques: Flow Cytometry, Derivative Assay, Injection, Two Tailed Test

Journal: Nature Communications

Article Title: CD200R1-CD200 checkpoint inhibits phagocytosis differently from SIRPα-CD47 to suppress tumor growth

doi: 10.1038/s41467-025-60456-3

Figure Lengend Snippet: a Partial sequences of the cytoplasmic domain of CD200R1 from different species. The conserved tyrosines (Y 286 , Y 289 , and Y 297 ; based on mouse amino acid numbering) are in red, whereas the conserved NPxY motif is boxed. Identical residues are depicted by asterisks (*), while conserved and semi-conserved amino acids are highlighted by colons (:) and periods (.), respectively. b Phagocytosis of IgG-opsonized WEHI-231 cells by WT BMDMs expressing GFP alone, or Cd200r1 −/− BMDMs expressing GFP alone or CD200R1 variants, in the presence of CD200 mAb or Ctrl mAb, ( n = 3). c Mass spectrometry analyzes of cytoplasmic proteins with inhibitory potential interacting with synthetic biotinylated CD200R1 peptides, with or without phosphorylation at Y 286 or Y 297 in pull-down assays. Peptides are depicted at the top. Interactors identified by phosphorylated peptides are shown below. Negative regulators of immune cell activation, either adaptors, kinases, phosphatases or Ras-GAP, are indicated. d Immunoblot analysis of Dok-1 and Dok-2 expression (left) and phagocytosis of IgG-opsonized WEHI-231 cells (right) by BMDMs from WT or Dok1 −/− Dok2 −/− mice. β-actin as loading Ctrl (left). Normalized protein abundance (in %) relative to actin is shown below the top panel, ( n = 4). e Same as Fig. 6d except that WT BMDMs transduced with Ctrl or Csk-specific siRNAs [ Csk knockdown ( Csk KD )] were used. Two different Csk-specific siRNAs were studied. Csk expression (left) and phagocytosis (right) were studied, ( n = 4). f Summary of fold-changes in phagocytosis for the various genetically deficient BMDMs in response to CD200 mAb, compared to WT BMDMs, ( n = 3 or 4). g WT or Dok1 −/− Dok2 −/− BMDMs were stimulated or not for 1 min with biotinylated CD200R1 mAb OX-110 and streptavidin. Cell lysates were immunoprecipitated with α-Dok-1, α-Dok-2, α-Csk, or normal rabbit serum (NRS), and probed by immunoblotting with antibodies targeting phosphotyrosine (pTyr), Dok-1, Dok-2 or Csk. h WT or Dok1 −/− Dok2 −/− BMDMs were stimulated or not for 30 s with biotinylated CD200R1 mAb OX-110 and streptavidin. Cell lysates were probed with α-pLyn (Tyr 507) or α-Lyn Abs (top). A quantification of multiple independent experiments is shown at the bottom, ( n = 3). Data are from three ( b , e , g , h ) or four d independent experiments, two (pY 297 peptide) and three (pY 286 peptide) ( c ) independent experiments. Each symbol represents one mouse ( b , d , e ). Data are mean ± s.e.m. Statistical analysis: two-way ANOVA test, with multiple comparisons ( b , d , e , h ); One-way ANOVA test, with multiple comparisons ( f ). ns not significant. See also Supplementary Figs. , and Supplementary Table .

Article Snippet: For phagocytosis assays and in vivo assays, the following mAbs were used: CD200 mAb OX-90 (BioXCell, Lebanon, NH); CD200R1 mAb OX-131 (Absolute Antibody, Boston, MA), SIRPα mAb no. 27 ; rat IgG2b isotype Ctrl mAb LTF-2 (BioXCell); rat IgG2a isotype Ctrl mAb 2A3 (BioXCell); Ctrl mAb MOPC-21 (in-house generated); and blocking CD11b mAb 5C6 (BioXCell).

Techniques: Expressing, Mass Spectrometry, Phospho-proteomics, Activation Assay, Western Blot, Quantitative Proteomics, Transduction, Knockdown, Immunoprecipitation

Journal: Nature Communications

Article Title: CD200R1-CD200 checkpoint inhibits phagocytosis differently from SIRPα-CD47 to suppress tumor growth

doi: 10.1038/s41467-025-60456-3

Figure Lengend Snippet: a Flow cytometry analysis of CD200 (red curves; top) and CD47 (lavender curves; bottom) expression on J558, A20 and WEHI-231 cells (left). Filled curves, Ctrl mAbs. The right panel shows relative expression levels of CD200 and CD47. b As per Fig. , except that mAbs were used in combination: CD200 mAb OX-90 (rat IgG2a), SIRPα mAb 27 (mouse IgG2a, Fc-silent), Ctrl mAb 2A3 (rat IgG2a), and Ctrl mAb MOPC21 (mouse IgG2a, Fc-silent), ( n = 3). c – f Luciferase + Tac + GFP + WEHI-231 cells were injected intravenously into Rag1 −/− mice, followed by intraperitoneal injection of Tac mAb combined with the indicated mAbs every 2 days starting from day 4, ( n = 5). c Schematic representation of the experimental workflow. Tumor progression was measured over time using luminescence. Representative photographs of mice ( d ) and quantification ( e ). f Kaplan – Meier curves of survival. g Phagocytosis of normal activated human T cells or B cells by autologous human macrophages, in the presence of samalizumab (human IgG1, Fc-silent), CD47 mAb B6H12 (human IgG1, Fc-silent) or Ctrl mAb (human IgG1, Fc-silent). T cells were not opsonized (implying phagocytosis was mediated by SLAMF7), whereas B cells were opsonized with rituximab (human IgG1, Fc-active) ( n = 3). Data are from three ( a , b , g ) or two ( c – f ) independent experiments. Each symbol represents one mouse or donor. Data are mean ± s.e.m. Statistical analysis: two-way ANOVA test, with multiple comparisons ( b , e ); log-rank (Mantel-Cox) test ( f ); one-way ANOVA test, with multiple comparisons ( g ). ns, not significant.

Article Snippet: For phagocytosis assays and in vivo assays, the following mAbs were used: CD200 mAb OX-90 (BioXCell, Lebanon, NH); CD200R1 mAb OX-131 (Absolute Antibody, Boston, MA), SIRPα mAb no. 27 ; rat IgG2b isotype Ctrl mAb LTF-2 (BioXCell); rat IgG2a isotype Ctrl mAb 2A3 (BioXCell); Ctrl mAb MOPC-21 (in-house generated); and blocking CD11b mAb 5C6 (BioXCell).

Techniques: Flow Cytometry, Expressing, Luciferase, Injection

Journal: Cancer Immunology, Immunotherapy : CII

Article Title: NECTIN4 regulates the cell surface expression of CD155 in non-small cell lung cancer cells and induces tumor resistance to PD-1 inhibitors

doi: 10.1007/s00262-025-04079-z

Figure Lengend Snippet: Evaluation of NECTIN4 and CD155 interactions and colocalization. A , Co-immunoprecipitation (Co-IP) experiments were performed using HEK293T cells transfected with CD155 and Flag-NECTIN4 expression vectors. Cell lysates were immunoprecipitated using Flag antibody or CD155 antibody, and immunoblotting was performed. Mouse IgG was used as a control for immunoprecipitation. B , A proximity ligation assay (PLA) targeting CD155 and NECTIN4 was performed in empty vector control and NECTIN4 overexpressing H322 and EBC1 cell lines. The close colocalization of CD155 and NECTIN4 was detected by red fluorescent signals. Nuclei were stained with DAPI. Scale bars, 20 μm. The number of PLA signals indicating colocalization of CD155 and NECTIN4 was determined from z-projection images generated by z-stacking of optical sections for individual cells. C , Schematic diagram of domain-deleted Flag-NECTIN4. D , HEK293T cells were co-transfected with the CD155 expression vector and full-length Flag-NECTIN4 or domain-deleted Flag-NECTIN4 expression vectors, followed by co-immunoprecipitation. As references, input samples were analyzed by immunoblotting, and samples immunoprecipitated with CD155 antibody were detected with Flag antibody by immunoblotting. Statistical analysis was conducted using Student’s t test. * p < 0.05, **p < 0.01. OE, overexpression

Article Snippet: One week after transplantation, tumor-bearing mice were treated intraperitoneally with monoclonal antibodies (mAbs) as follows: 200 μg of anti-PD-1 mAb (RMP1-14, BioXcell, #BE0146), 150 μg of anti-TIGIT mAb (1G9, BioXcell, #BE0274), 200 μg of control IgG2a mAb (2A3, BioXcell, #BE0089), and 150 μg of control IgG1 mAb (MOPC-21, BioXcell, #BE0083).

Techniques: Immunoprecipitation, Co-Immunoprecipitation Assay, Transfection, Expressing, Western Blot, Control, Proximity Ligation Assay, Plasmid Preparation, Staining, Generated, Over Expression

Journal: Cancer Immunology, Immunotherapy : CII

Article Title: NECTIN4 regulates the cell surface expression of CD155 in non-small cell lung cancer cells and induces tumor resistance to PD-1 inhibitors

doi: 10.1007/s00262-025-04079-z

Figure Lengend Snippet: Overexpression of NECTIN4 confers resistance to PD-1 inhibitors. A , Schematic representation of the experiment: the subcutaneous transplantation of 4T1 EV control or NECTIN4-overexpressing cells, followed by treatment with anti-PD-1 antibody. The treatment was initiated on day 7 after tumor transplantation and administered every three days for a total of three times. Anti-PD-1 mAb, or IgG2a isotype were administered at a dose of 200 µg. B , Graph showing tumor volumes after transplantation. Tumor volumes were calculated using the formula: length × width × width/2. C , Individual tumor volume progression in each group. D , Analysis of tumor-infiltrating lymphocytes (TILs) by flow cytometry. Experiments were conducted with five mice per group and the data are presented as the mean ± SD. All in vivo experiments were performed in duplicates, with similar results. Statistical analysis was conducted using one-way ANOVA followed by Tukey’s test (B) or Student’s t-test (D). * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. EV, empty vector; OE, overexpression

Article Snippet: One week after transplantation, tumor-bearing mice were treated intraperitoneally with monoclonal antibodies (mAbs) as follows: 200 μg of anti-PD-1 mAb (RMP1-14, BioXcell, #BE0146), 150 μg of anti-TIGIT mAb (1G9, BioXcell, #BE0274), 200 μg of control IgG2a mAb (2A3, BioXcell, #BE0089), and 150 μg of control IgG1 mAb (MOPC-21, BioXcell, #BE0083).

Techniques: Over Expression, Transplantation Assay, Control, Flow Cytometry, In Vivo, Plasmid Preparation

Journal: Cancer Immunology, Immunotherapy : CII

Article Title: NECTIN4 regulates the cell surface expression of CD155 in non-small cell lung cancer cells and induces tumor resistance to PD-1 inhibitors

doi: 10.1007/s00262-025-04079-z

Figure Lengend Snippet: Overcoming anti-PD-1 antibody resistance in NECTIN4-overexpressing 4T1 cells by combination therapy with anti-TIGIT antibody. A , Schematic representation of the experiment: the subcutaneous transplantation of 4T1 EV control or NECTIN4-overexpressing cells, followed by treatment with anti-PD-1 antibody alone or in combination with anti-TIGIT antibody. The treatment was initiated on day 7 after tumor transplantation and administered every three days for a total of three times. Anti-PD-1 mAb, or IgG2a isotype were administered at a dose of 200 µg, and anti-TIGIT mAb or IgG1 isotype were administered at a dose of 150 µg. B , Graph showing tumor volume progression after transplantation. C , Comparison of tumor weights in each group, measured post-excision. D , Photographs of tumors excised two days after the completion of treatment. E , Analysis of tumor-infiltrating lymphocytes (TILs) by flow cytometry. Experiments were conducted with five mice per group and the data are presented as the mean ± SD. All in vivo experiments were performed in duplicates, with similar results. Statistical analysis was conducted using one-way ANOVA followed by Tukey’s test (B, C) or Student’s t-test (E). * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. EV, empty vector; OE, overexpression

Article Snippet: One week after transplantation, tumor-bearing mice were treated intraperitoneally with monoclonal antibodies (mAbs) as follows: 200 μg of anti-PD-1 mAb (RMP1-14, BioXcell, #BE0146), 150 μg of anti-TIGIT mAb (1G9, BioXcell, #BE0274), 200 μg of control IgG2a mAb (2A3, BioXcell, #BE0089), and 150 μg of control IgG1 mAb (MOPC-21, BioXcell, #BE0083).

Techniques: Transplantation Assay, Control, Comparison, Flow Cytometry, In Vivo, Plasmid Preparation, Over Expression

Journal: The Journal of Clinical Investigation

Article Title: Cxcr3 promotes protection from colorectal cancer liver metastasis by driving NK cell infiltration and plasticity

doi: 10.1172/JCI184036

Figure Lengend Snippet: ( A ) Experimental scheme of macrophage-NK cell coculture in vitro. ( B ) Lef,: representative contour plot of CD49a and CD49b expression by NK cells upon 72 hours coculture with macrophages purified from HL and LM with or without TGF-β-RI inhibitor (SB431542, 2.5 nM). Right, fold change (F.C.) of frequency ± SEM of CD49a + cells among NK cells cultured with macrophages from HL, MFL, or LM relative to NK cells cultured alone (IL-15 * P = 0.03, IL-15+TGF-β-RI inhibitor * P = 0.044, 2-tailed Student’s t test in HL Mac versus LM Mac in IL-15 and LM Mac in IL-15 versus IL-15+ TGF-β-RI inhibitor). 3 experiments were performed in duplicate. ( C ) Left, percent of migration of splenic NK cells in response to supernatants collected from MC38- or SL4-derived LM macrophages and no chemokine control (NC) (n > 3, * P = 0.01, **** P < 0.0001, 1-way ANOVA). Right, percent of migration in response to MC38-derived MFL, LM macrophage supernatants and NC ( n > 3, **** P < 0.0001, 1-way ANOVA). ( D ) Fold change of CD49a (left) and frequency of CD49a + CD69 + cells (right) in NK cells cultured alone or with LM-derived macrophages from MC38 and SL4 LM ( n = 5, * P < 0.02, **** P < 0.0001, 1-way ANOVA). ( E and F ) Top, experimental workflow of in vivo treatment with anti-CSF1R and with MC-21. ( E ) Bottom, representative contour plots show ILC1, CD49a + and CD49a – NK cells in LM of control mAb (Rat IgG2a)-treated and anti-CSF1R-treated tumor-bearing mice. Numbers in plots indicate frequency among NK1.1 + NKp46 + cells. Histogram plots show mean frequency ± SEM ( n = 9 total mice in 2 independent experiments, CD49a + NK ** P = 0.003, CD49a – NK * P = 0.02, 2-tailed Student’s t test). ( F ) Bottom, representative contour plots show ILC1, CD49a + , and CD49a – NK cells in LM of control mAb (Rat IgG2a)-treated and MC-21–treated tumor-bearing mice. Numbers in plots indicate frequency among NK1.1 + NKp46 + cells. Histogram plots show mean frequency ± SEM ( n = 4, 2 independent experiments were performed).

Article Snippet: To deplete F4/80 hi MAM tumor-bearing mice were treated i.p. with anti-CSF1R (CD115, clone AFS98, BioXcell) or control Rat IgG2a (clone 2A3, BioXcell) mAbs as following: 60 mg/kg at day +7 intrasplenic injection, 30 mg/kg at days +10 and +13, and 20 mg/kg at day +16.

Techniques: In Vitro, Expressing, Purification, Cell Culture, Migration, Derivative Assay, Control, In Vivo

Journal: Cell reports

Article Title: Clostridioides difficile toxin B subverts germinal center and antibody recall responses by stimulating a drug-treatable CXCR4-dependent mechanism

doi: 10.1016/j.celrep.2024.114245

Figure Lengend Snippet:

Article Snippet: InVivoPlus TM isotype control mAb, clone 2A3 , BioXCell , Cat# BP0089 RRID: AB_1107769.

Techniques: Control, Virus, Recombinant, Expressing, Suspension, Protease Inhibitor, SYBR Green Assay, Cell Isolation, Binding Assay, Bradford Protein Assay, Cell Counting, Enzyme-linked Immunosorbent Assay, Gene Expression, Software, Simple Western, Protein Extraction