Monoclonal Antibodies

This HSPA8 monoclonal antibody was developed using hybridoma technology. The antibody-producing hybridomas were generated by fusing myeloma cells with spleen cells from immunized mice. The mice were immunized with recombinant human HSPA8 protein (amino acids 2-646). This HSPA8 monoclonal antibody is designed to detect endogenous levels of human HSPA8 protein. It has been purified using protein G and rigorously validated for its performance in ELISA, Western blotting, immunohistochemistry, immunofluorescence, and flow cytometry applications. Its purity exceeds 95%.

The HSPA8 protein primarily functions as a chaperone within the cell, assisting in protein folding, transport, and degradation. It accomplishes this by binding to nascent polypeptide chains or misfolded proteins, guiding them through various cellular processes. HSPA8 plays a critical role in maintaining cellular homeostasis by preventing the accumulation of misfolded or aggregated proteins, which can lead to cellular dysfunction and disease. It is also involved in the regulation of apoptosis, antigen processing, and cell signaling.

The YWHAZ monoclonal antibody specifically recognizes the YWHAZ protein and has demonstrated high specificity in human, mouse, and rat samples. It is suitable for use in a variety of applications, including ELISA, WB, IHC, IF, and FC. This YWHAZ monoclonal antibody was generated from YWHAZ antibody-secreting hybridomas, which were produced by fusing myeloma cells with spleen cells from an immunized mouse. The recombinant human 14-3-3 protein zeta/delta protein (133-212aa) was used as the immunogen. This YWHAZ monoclonal antibody undergoes protein A-mediated purification, achieving a purity level of up to 95%.

YWHAZ, also known as 14-3-3 protein zeta/delta, plays a crucial role in regulating a broad range of cellular processes, including signal transduction, cell cycle regulation, apoptosis, and gene expression through interactions with various protein partners. YWHAZ is involved in regulating multiple signaling pathways such as the PI3K/Akt, MAPK, and NF-κB pathways, and plays a significant role in mediating cell survival and growth.

The CD63 monoclonal antibody is a highly specific reagent employed to detect the CD63 protein in a variety of human and rabbit samples. It was generated through a process involving the immunization of mice with recombinant human CD63 protein (amino acids 103-203), followed by the fusion of immunized mouse spleen cells with myeloma cells to produce hybridomas. These hybridomas were subsequently selected and cultured in the mouse abdominal cavity, resulting in the production of ascites containing CD63 monoclonal antibodies. The resulting CD63 monoclonal antibody was rigorously screened for specificity using a range of assays, including ELISA, Western blotting, immunohistochemistry, immunofluorescence, and flow cytometry. Its purity is over 95%, achieved through protein G purification.

CD63 protein plays a pivotal role in vesicular trafficking, antigen presentation, and cell signaling. Within cells, CD63 protein interacts with other tetraspanins, integrins, and adhesion molecules to regulate the formation and stability of multimeric protein complexes. It is also involved in the internalization and sorting of plasma membrane proteins to lysosomes for degradation, as well as the fusion of lysosomes with autophagosomes during autophagy.

This monoclonal CD9 antibody is produced from the hybridoma resulting from the fusion of mouse myeloma cells and splenocytes from mice immunized with recombinant human CD9 antigen protein (amino acids 112-195). The antibody is purified from mouse ascites using protein G and achieves a purity exceeding 95%. This unconjugated CD9 monoclonal antibody aligns with the mouse IgG1 isotype. It is suitable for various applications including ELISA, Western blotting, immunohistochemistry, immunofluorescence, and flow cytometry. Notably, it can only detect the human CD9 protein.

CD9, a tetraspanin, is expressed across all major subsets of leukocytes and is also highly expressed by endothelial cells. Through interactions with other tetraspanins, as well as with diverse transmembrane and intracellular proteins, CD9 plays a crucial role in modulating a range of cellular activities. These include intracellular signaling transduction, proliferation, activation, survival, migration, invasion, adhesion, and diapedesis.

The BCL2 monoclonal antibody is produced using hybridoma technology. Mice were immunized with a recombinant human BCL2 protein (amino acids 2-211), and their spleen B cells were fused with myeloma cells to create hybridomas. Antibody-producing hybridomas were selected and cultured, and BCL2 monoclonal antibodies were harvested from mouse ascites. This monoclonal antibody demonstrates high specificity for human and mouse BCL2 protein, as evidenced by its performance in ELISA, Western blotting, and flow cytometry applications. The antibody is purified to a high degree (>95%) using protein G affinity chromatography.

BCL2 protein plays a crucial role in regulating the mitochondrial pathway of apoptosis. As an anti-apoptotic protein, it prevents apoptosis by binding and sequestering pro-apoptotic proteins, such as BAX and BAK, thereby inhibiting mitochondrial outer membrane permeabilization (MOMP) and the release of cytochrome c. Cytochrome c release initiates the caspase cascade, ultimately leading to cell death. BCL2 is also involved in regulating other cellular processes, including autophagy and oxidative stress.