Rabbit Polyclonal MCSFReceptor(CSF1R) Antibody

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     All lanes : Anti-MCSF Receptor (CSF1R) Antibody (C-term) at 1:1000 dilution Lane 1: THP-1 whole cell lysate Lane 2: rat spleen lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG,  (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 108 kDa Blocking/Dilution buffer: 5% NFDM/TBST.    

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     Overlay histogram showing HepG2 cells stained with P34603(green line).  The cells were fixed with 2% paraformaldehyde (10 min) and then permeabilized with 90% methanol for 10 min.  The cells were then icubated in 2% bovine serum albumin to block non-specific protein-protein interactions followed by the antibody (P34603,  1:25 dilution) for 60 min at 37ºC.  The secondary antibody used was Goat-Anti-Rabbit IgG, DyLight® 488 Conjugated Highly Cross-Adsorbed(1583138) at 1/200 dilution for 40 min at 37ºC.  Isotype control antibody (blue line) was rabbit IgG1 (1μg/1x10^6 cells) used under the same conditions.  Acquisition of >10, 000 events was performed.    

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     Overlay histogram showing HepG2 cells stained with P34603(green line).  The cells were fixed with 2% paraformaldehyde (10 min) and then permeabilized with 90% methanol for 10 min.  The cells were then icubated in 2% bovine serum albumin to block non-specific protein-protein interactions followed by the antibody (P34603,  1:25 dilution) for 60 min at 37ºC.  The secondary antibody used was Goat-Anti-Rabbit IgG, DyLight® 488 Conjugated Highly Cross-Adsorbed(1583138) at 1/200 dilution for 40 min at 37ºC.  Isotype control antibody (blue line) was rabbit IgG1 (1μg/1x10^6 cells) used under the same conditions.  Acquisition of >10, 000 events was performed.    

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     Immunohistochemical analysis of P34603 on paraffin-embedded Human tonsil tissue.  Tissue was fixed with formaldehyde at room temperature.  Heat induced epitope retrieval was performed by EDTA buffer (pH9. 0).  Samples were incubated with primary antibody(1:100) for 1 hour at room temperature.  Undiluted CRF Anti-Polyvalent HRP Polymer antibody was used as the secondary antibody.    

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     Immunohistochemical analysis of P34603 on paraffin-embedded Human placenta tissue.  Tissue was fixed with formaldehyde at room temperature.  Heat induced epitope retrieval was performed by EDTA buffer (pH9. 0).  Samples were incubated with primary antibody(1:100) for 1 hour at room temperature.  Undiluted CRF Anti-Polyvalent HRP Polymer antibody was used as the secondary antibody.    

The macrophage colony-stimulating factor receptor (CSF1R), also known as CD115 or c-FMS, is a tyrosine kinase receptor encoded by the *CSF1R* gene. It binds ligands such as CSF-1 (colony-stimulating factor 1) and interleukin-34 (IL-34), regulating the survival, proliferation, and differentiation of macrophages, monocytes, and other myeloid-lineage cells. CSF1R signaling plays critical roles in tissue homeostasis, immune regulation, and disease processes, including cancer, inflammatory disorders, and neurodegenerative conditions.

CSF1R-targeting antibodies are designed to modulate this pathway, primarily as antagonists to block receptor activation. By inhibiting CSF1R, these antibodies suppress the recruitment and function of tumor-associated macrophages (TAMs) in cancers, thereby disrupting pro-tumorigenic microenvironments and enhancing anti-tumor immune responses. Some antibodies, like emactuzumab and cabiralizumab, have reached clinical trials for conditions such as tenosynovial giant cell tumor and pancreatic cancer, often combined with checkpoint inhibitors.

Additionally, CSF1R antibodies are explored in inflammatory diseases (e.g., rheumatoid arthritis) to dampen pathogenic macrophage activity and in neurodegenerative disorders (e.g., Alzheimer’s disease) to modulate microglia responses. Challenges include balancing therapeutic efficacy with potential immunosuppressive side effects. Most CSF1R antibodies are monoclonal, engineered for specificity to extracellular domains, and may act by preventing ligand binding or receptor dimerization. Their development highlights the therapeutic potential of targeting myeloid cells in diverse pathologies.