The production of the GYPA recombinant monoclonal antibody begins with the acquisition of GYPA antibody genes. These GYPA antibody genes are then introduced into appropriate host cells, which are cultured for synthesizing GYPA antibodies through a cell-based expression and translation system. This method offers several advantages, including significantly enhancing the purity and stability of the resulting GYPA recombinant monoclonal antibodies, as well as improving their affinity and specificity. Following synthesis, the GYPA recombinant monoclonal antibody undergoes a purification process using affinity chromatography. Subsequently, it undergoes testing through ELISA and FC assays. This antibody exclusively targets the human GYPA protein.

GYPA (glycophorin A) is a key component of the erythrocyte membrane with roles in maintaining membrane structure, blood group determination, mechanical resilience, and potentially cell adhesion and signaling. Its presence on the surface of red blood cells is essential for their proper function in oxygen transport and maintaining blood compatibility.

The process of generating the phospho-RAF1 (S43) recombinant monoclonal antibody commences with the isolation of genes responsible for coding the RAF1 antibody from rabbits previously immunized with a synthesized peptide derived from the human RAF1 protein phosphorylated at S43. These antibody genes are subsequently introduced into expression vectors, and the genetically modified vectors are carefully transfected into host suspension cells. After successful transfection, positive cells are cultured to promote the robust expression and secretion of antibodies. Following this cultivation phase, the phospho-RAF1 (S43) recombinant monoclonal antibody undergoes a meticulous purification process utilizing affinity chromatography, effectively separating the antibody from the surrounding cell culture supernatant. Ultimately, the functionality of the antibody is comprehensively evaluated through ELISA and IF, unequivocally confirming its capacity to interact with the human RAF1 protein phosphorylated at S43.

Phosphorylation of RAF1 at S43 is a crucial regulatory event in the MAPK signaling pathway, impacting cell growth, survival, and differentiation. Dysregulation of this phosphorylation event can have significant implications in cancer and other diseases driven by aberrant signaling.

The process of creating the WDR5 recombinant monoclonal antibody begins by obtaining the WDR5 antibody genes. These genes are then introduced into suitable host cells, which are cultured for synthesizing WDR5 antibodies using a cell-based expression and translation system. This method offers several advantages, including significantly improving the purity and stability of the resulting WDR5 recombinant monoclonal antibodies, as well as enhancing their affinity and specificity. Following synthesis, the WDR5 recombinant monoclonal antibody undergoes purification through affinity chromatography. Subsequently, it undergoes thorough testing via various assays, including ELISA, IHC, and FC. This antibody specifically recognizes the human WDR5 protein.

WDR5 is a critical component of protein complexes involved in epigenetic regulation, chromatin remodeling, and gene expression control. Its primary function is to promote histone methylation at specific gene promoters, thereby regulating gene activation and repression. Proper WDR5-mediated regulation is crucial for normal development, cellular differentiation, and maintaining the balance of gene expression in health and disease.

CUSABIO designed the vector clones for the expression of a recombinant JUN antibody in mammalian cells. The vector clones were obtained by inserting the JUN antibody heavy and light chains into the plasma vectors. The recombinant JUN antibody was purified from the culture medium through affinity-chromatography. It can be used to detect JUN protein from Human in the ELISA, WB, IHC, IF.

The phospho-JUN (S63) antibody can be used to detect the endogenous levels of the JUN phosphorylated at Ser63 residue. The phosphorylation of Ser63 in the NH2-terminal transactivation domain of JUN is required for its transcriptional activity. The phosphorylation of JUN has also been linked to the mediation of apoptosis when survival signals are interrupted. JUN is involved in various cellular processes, including proliferation, apoptosis, survival, tumorigenesis, and tissue morphogenesis.

CUSABIO cloned PRKDC antibody-coding genes into plasma vectors and then transfected these vector clones into mammalian cells using a lipid-based transfection reagent. Following transient expression, the recombinant antibodies against PRKDC were harvested and characterized. The recombinant PRKDC antibody was purified by affinity-chromatography from the culture medium. It can be used to detect PRKDC protein from Human in the ELISA, IF.

Protein kinase, DNA-activated, catalytic polypeptide (PRKDC) encodes a 465 kDa catalytic subunit of DNA-dependent protein kinase that plays a pivotal role in the maintenance of genomic stability and is a critical component of DNA double-strand break repair and recombination. DNA repair genes may serve as potential biomarkers of malignancies or therapeutic targets. Additional analysis showed that a PRKDC mutation was significantly associated with a high mutation load in cervical cancer, colon adenocarcinoma, head and neck squamous cell carcinoma, lung adenocarcinoma, gastric adenocarcinoma and endometrial cancer. Patients with gastric cancer or colon cancer harboring PRKDC mutations were also highly associated with MSI-high status. Loss of PRKDC expression is associated with impaired DNA repair. A loss-of-function PRKDC mutation or DNA-PK inhibitor can enhance the efficacy of immune therapy.

The CLEC4C recombinant monoclonal antibody was produced through a series of steps. Initially, the CLEC4C antibody genes were incorporated into plasmid vectors. These engineered plasmid vectors were subsequently introduced into appropriate host cells, utilizing exogenous protein expression technology to enable antibody production. Following this, the CLEC4C recombinant monoclonal antibody underwent purification using affinity chromatography and underwent thorough validation for its suitability in ELISA assays. During functional ELISA testing, it was established that this CLEC4C recombinant monoclonal antibody demonstrated a strong binding affinity for the human CLEC4C protein (CSB-MP855470HUh7) at a concentration of 2 μg/mL, with an EC₅₀ falling within the range of 7.658 to 12.99 ng/mL.

CLEC4C is primarily expressed in the liver and lymph nodes and plays a significant role in the immune system. The main function of CLEC4C protein is to serve as a pattern recognition receptor in the immune system, helping to recognize and respond to pathogens by binding to their carbohydrate structures. CLEC4C also plays a role in antigen presentation, immune regulation, and cell adhesion.

The phospho-MAPK3 (T202) + MAPK1 (T185) recombinant monoclonal antibody production generally commences with the insertion of the phospho-MAPK3 (T202) + MAPK1 (T185) antibody-encoding gene into expression vectors. These vectors are subsequently delivered into host cells through polyethyleneimine-mediated transfection. The host cells, housing these vectors, are cultured to generate and release the antibodies. Following purification via affinity chromatography, the antibodies are subjected to assessments through ELISA, WB, IHC, and IF tests, confirming their ability to recognize the human phospho-MAPK3 (T202) + MAPK1 (T185) protein.