Monoclonal Antibodies
Product List
NANOG Monoclonal Antibody
The monoclonal NANOG antibody is produced from the hybridoma generated by fusing mouse myeloma cells with splenocytes from mice immunized with recombinant human NANOG protein. It is purified from mouse ascites using protein G, achieving a purity exceeding 95%. This unconjugated NANOG monoclonal antibody aligns with the mouse IgG1 isotype. It is suitable for various applications including ELISA, Western Blot, Immunocytochemistry, Immunofluorescence, and Flow Cytometry. The antibody can detect the NANOG protein in human, mouse, and rat samples.
NANOG, a transcription factor, plays a crucial role in the self-renewal of embryonic stem cells (ES), acting as a vital factor in maintaining pluripotency. Research has demonstrated the strict involvement of NANOG in the process of carcinogenesis, suggesting its potential as a prognostic marker for malignant tumors.
CDH1 Monoclonal Antibody
The CDH1 monoclonal antibody is a highly specific and sensitive reagent for detecting human CDH1 expression in biological samples. Its production is based on hybridoma technology. The recombinant human CDH1 protein (amino acids 155-707) is used to immunize mice to isolate spleen cells, which are then fused with myeloma cells to generate hybridomas. Hybridomas producing the CDH1 antibody are selected, cultured, and harvested for the desired antibodies. After protein G purification, this CDH1 monoclonal antibody achieves a purity exceeding 95%. Its specificity has been validated through four applications: ELISA, Western blotting, immunofluorescence, and flow cytometry.
CDH1 plays a crucial role in cell adhesion and tissue architecture within epithelial tissues. The CDH1 protein regulates various cellular processes including cell differentiation, proliferation, and apoptosis. It also plays a vital role in maintaining the polarity and integrity of epithelial tissues.
PD-L1 Monoclonal Antibody
The PD-L1 monoclonal antibody is produced by fusing spleen cells from mice immunized with recombinant human PD-L1 protein (amino acids 19-238) with myeloma cells. This antibody exhibits high specificity for human PD-L1 protein and finds applications in various research areas including ELISA, Western blotting, Immunohistochemistry, Immunofluorescence, and Flow cytometry. The antibody undergoes Protein G purification, achieving a purity level of 95%.
PD-L1 plays a pivotal role in regulating the immune system by interacting with its receptor PD-1, which is present on activated T cells. The binding of PD-L1 to PD-1 leads to the inhibition of T-cell activity, preventing excessive immune responses that could result in tissue damage and autoimmune disorders. Notably, PD-L1 is also utilized by cancer cells as a mechanism to evade the immune system, enabling them to escape destruction by immune cells.
CD146 Monoclonal Antibody
This monoclonal anti-CD146 antibody (mouse IgG2a isotype) is produced from a hybridoma generated by fusing mouse myeloma cells with splenocytes from an immunized mouse. The splenocytes were isolated from a mouse immunized with recombinant human CD146 protein (amino acids 50-646). This unconjugated CD146 antibody is purified using protein G, resulting in a purity exceeding 95%. It exhibits specificity for CD146 from human samples. The antibody is suitable for applications including ELISA, Western blotting, Immunofluorescence, and Flow Cytometry.
CD146 serves as a Ca2+-independent cell adhesion molecule, mediating heterophilic cell-cell interactions. It plays a significant role in various biological processes, including inflammation, differentiation, adhesion, tumorigenicity, metastasis, invasion, and angiogenesis.
OCT4 Monoclonal Antibody
The OCT4 Monoclonal Antibody is generated by immunizing mice with Recombinant Human POU Domain, Class 5, Transcription Factor 1 Protein (1-360AA). This IgG2b subtype antibody exhibits reactivity with Human, Mouse, and Rat OCT4, a crucial POU transcription factor.
OCT4, prominently expressed in embryonic stem cells, regulates the expression of genes that drive cell proliferation. In conjunction with Sox2, OCT4 plays a vital role in maintaining the pluripotency and renewal of stem cells. Fluctuations in OCT4 levels trigger the differentiation of these germ cells by activating specific genes.
Aberrant OCT4 expression has been implicated in the embryogenesis and proliferation of cancer cells. The OCT4 Antibody binds to OCT4 in cancerous cells, making it valuable for detecting OCT4 and investigating anti-OCT4 therapeutic strategies.
CD14 Monoclonal Antibody
This product is a mouse monoclonal antibody targeting human CD14 (amino acids 20-345), encompassing the mature extracellular domain in its membrane-bound GPI-anchored form. The IgG1 isotype antibody is purified by protein A chromatography, achieving >95% purity. It exhibits cross-reactivity with CD14 from human, mouse, and rabbit. This antibody is suitable for ELISA, Western blotting, flow cytometry, immunofluorescence, and immunohistochemistry. It is a valuable tool for immunological research, particularly in characterizing disease-associated immune pathways and pro-inflammatory responses to pathogens. Human CD14, a monocyte differentiation antigen, plays a critical role in activating the innate immune response. Expressed on the surface of monocytes and most tissue macrophages, CD14 regulates immune responses to bacterial lipopolysaccharide (LPS), and also mediates cellular and immune responses to diacylated and triacylated lipopeptides, and electronegative low-density lipoprotein (LDL-).
lacZ Monoclonal Antibody
This lacZ monoclonal antibody is produced through a meticulous process. Mice are immunized with recombinant Escherichia coli Beta-galactosidase protein (amino acids 2-1024). Subsequently, splenocytes from immunized mice are isolated and fused with myeloma cells to generate hybridomas. The selected hybridomas, capable of secreting lacZ antibody, are then cultured to harvest large quantities of the monoclonal antibody. This lacZ monoclonal antibody undergoes purification using protein G, achieving a purity exceeding 95%. It finds utility in a range of applications including ELISA, Western blotting, immunofluorescence, immunoprecipitation, and flow cytometry for the detection of Escherichia coli lacZ protein.
LacZ protein, a β-galactosidase enzyme, catalyzes the hydrolysis of the glycosidic bond between a galactose and a glucose or galactose molecule. Its primary function lies in breaking down lactose into glucose and galactose, which the cell can then utilize for energy production. Furthermore, lacZ protein serves as a valuable reporter gene in molecular biology experiments, enabling the detection of the expression of genes of interest.
Introduction
Monoclonal antibodies (mAbs) are laboratory-produced molecules engineered to serve as substitute antibodies that can restore, enhance, or mimic the immune system’s attack on cells . They are produced by identical immune cells that are all clones of a unique parent cell . Monoclonal antibodies can be classified based on their source and structure:
Monoclonal antibodies exhibit several key biological properties:
Monoclonal antibodies play crucial roles in the immune system:
- Pathogen Recognition: Bind to specific antigens on pathogens, marking them for destruction .
- Immune Response: Enhance the immune system’s ability to fight infections and diseases .
- Therapeutic Functions: Used in treating various diseases, including cancer, autoimmune disorders, and infectious diseases .
Monoclonal antibodies interact with other molecules and cells through various mechanisms:
The expression and activity of monoclonal antibodies are tightly regulated:
Monoclonal antibodies have a wide range of applications in biomedical research and medicine:
