To produce a recombinant monoclonal antibody against DEK, CUSABIO initiated the process by immunizing a rabbit with a synthesized peptide corresponding to human DEK. Following immunization, B cells were isolated from the rabbit, and RNA was extracted from these cells. The extracted RNA was reverse-transcribed into cDNA, which was utilized as a template for extending DEK antibody genes using degenerate primers. These extended DEK antibody genes were then integrated into a plasmid vector and introduced into host cells for expression. The DEK recombinant monoclonal antibody was purified from the cell culture supernatant through affinity chromatography and evaluated for its utility in ELISA, IHC, IF, and FC applications, with specificity demonstrated for human DEK protein.

DEK is a nuclear protein that has been implicated in both normal cellular functions and disease-related processes. It is known to play various roles in the cell nucleus and is associated with several cellular processes, including chromatin organization, DNA binding, transcription regulation, cell cycle regulation, and immune response.

To generate a recombinant monoclonal antibody specific to ARG1, the initial step involved immunizing a rabbit with a synthesized peptide derived from human ARG1 protein. B cells were subsequently isolated from the immunized rabbit, and RNA was extracted from these cells. The extracted RNA was reverse-transcribed into cDNA, which was utilized as a template to extend ARG1 antibody genes using degenerate primers. These engineered ARG1 antibody genes were incorporated into a plasmid vector and transfected into host cells for expression. The resulting ARG1 recombinant monoclonal antibody was isolated from the cell culture supernatant through affinity chromatography and evaluated for its utility in ELISA and IHC applications. It is only reactive with human ARG1 protein.

The main function of the ARG1 protein is to catalyze the conversion of arginine, an amino acid, into ornithine and urea in the urea cycle. This enzymatic reaction takes place in the liver and is a critical step in the process of removing toxic ammonia from the body. Mutations or deficiencies in the ARG1 gene can lead to a rare genetic disorder known as arginase deficiency or argininemia.

The coding sequence for the phospho-PRKCZ (T560) monoclonal antibody (isolated by immunizing animals with the human pT560-PRKCZ) was cloned into the plasmids and then transfected into cell lines for in vitro expression. The product underwent affinity-chromatography-mediated purification to get the phospho-PRKCZ (T560) recombinant monoclonal antibody. This anti-pT560-PRKCZ antibody is a rabbit IgG. It is suitable for the detection of human PRKCZ phosphorylated at Thr 560 residue. And it can be used in ELISA and WB applications.

PRKCZ is an atypical protein kinase C isoform that regulates a variety of signaling events, including cell proliferation, cell survival, and cell motility, all of which are critical for cancer formation and progression. PRKCZ is involved in a number of signaling pathways, including the activation of the ERK/MAPK cascade, the p70 ribosomal S6 kinase signaling cascade, the transcription factor NF-B, and cell polarity regulation. Kelly K. Y. Seto et al. discovered that PRKCZ is a promising regulatory component of the IGF1R and ITGB3 pathways, implying that it could be important in ovarian tumorigenesis.

A recombinant monoclonal antibody targeting HNF4A was generated through a series of steps. Initially, a rabbit was immunized with a synthesized peptide derived from human HNF4A protein. B cells were then isolated from the immunized rabbit, and RNA was extracted from these cells. The RNA was reverse-transcribed into cDNA, which was utilized as a template to extend HNF4A antibody genes using degenerate primers. These engineered HNF4A antibody genes were incorporated into a plasmid vector and introduced into host cells for expression. The resultant HNF4A recombinant monoclonal antibody was subsequently purified from the cell culture supernatant via affinity chromatography and evaluated for its performance in ELISA, WB, IHC, IF, and FC applications, demonstrating specific recognition of human and rat HNF4A protein.

The HNF4A protein is a critical transcription factor that regulates gene expression in various tissues, with a primary focus on the liver. Its functions are essential for maintaining metabolic homeostasis, organ development, and the proper functioning of multiple physiological processes, including glucose and lipid metabolism, detoxification, and pancreatic function.

CUSABIO developed the phospho-SMAD2 (S255) recombinant monoclonal antibody using protein technology and DNA recombinant techniques. The first step is to obtain the phospho-SMAD2 (S255) antibody gene. Immunizing an animal with a synthesized peptide derived from human phospho-SMAD2 (S255) and isolating B cells. These B cells are then screened to isolate positive ones, followed by single clone identification. Next, the light and heavy chains of the phospho-SMAD2 (S255) antibody are amplified via PCR and integrated into a plasmid vector to construct a recombinant vector. This recombinant vector is subsequently transfected into host cells to facilitate antibody expression. The phospho-SMAD2 (S255) recombinant monoclonal antibody is purified from the supernatant of cell culture using affinity chromatography. Finally, stringent validation is conducted to ensure its accuracy and efficacy for the detection of human SMAD2 protein phosphorylated at S255 residue in ELISA and IF applications.

The process of creating a recombinant monoclonal antibody against TPSB2 began with the immunization of a rabbit using a synthesized peptide derived from human TPSB2 protein. B cells were isolated from the immunized rabbit, and RNA was extracted from these B cells. The RNA was reverse-transcribed into cDNA, which served as a template for extending TPSB2 antibody genes using degenerate primers. The extended TPSB2 antibody genes were then incorporated into a plasmid vector and introduced into host cells for expression. Subsequent purification of the TPSB2 recombinant monoclonal antibody from the cell culture supernatant was achieved through affinity chromatography. The TPSB2 antibody was subsequently assessed for its utility in ELISA, WB, and FC applications, with specificity demonstrated toward human and mouse TPSB2 protein.

TPSB2 is primarily found in mast cells, which are immune cells involved in allergic and inflammatory reactions. The main role of the TPSB2 protein is to function as a protease involved in the degradation of proteins, particularly in the context of immune and inflammatory responses.

CUSABIO designed the vector clones for the expression of a recombinant CDC37 antibody in mammalian cells. The vector clones were obtained by inserting the CDC37 antibody heavy and light chains into the plasma vectors. The recombinant CDC37 antibody was purified from the culture medium through affinity-chromatography. It can be used to detect CDC37 protein from Human in the ELISA, WB.

The phospho-CDC37 (S13) antibody is specific for phosphorylated CDC37. CDC37 function is modulated through phosphorylation at S13 by protein kinase CK2. Phosphorylation of CDC37 at S13 is essential for its kinase binding activity and its ability to stimulate the nucleotide-regulated conformational switching of Hsp90. CDC37 suppressed the ATP hydrolysis step and allows the prolonged combination of Hsp90 dimers with client proteins and more effective chaperone activity.

To generate a recombinant monoclonal antibody against L1CAM, CUSABIO initiated the process by immunizing a rabbit with a synthesized peptide derived from human L1CAM. B cells were subsequently isolated from the immunized rabbit, and RNA was extracted from these cells. The extracted RNA was reverse-transcribed into cDNA, which was then used as a template to extend L1CAM antibody genes using degenerate primers. These synthesized L1CAM antibody genes were incorporated into a plasmid vector and transfected into host cells for expression. The resulting L1CAM recombinant monoclonal antibody was isolated from the cell culture supernatant via affinity chromatography and assessed for its suitability in ELISA, IHC, and FC assays, demonstrating specificity for human L1CAM protein.

The L1CAM protein is primarily associated with neural development and plays a crucial role in axon guidance, cell adhesion, and synapse formation in the nervous system. It also has implications for neural regeneration, tumor invasion, and potentially other cellular processes outside the nervous system.

The process of producing the EGFR recombinant monoclonal antibody begins by acquiring the EGFR antibody genes. These genes are then introduced into appropriate host cells, which are cultured for synthesizing EGFR antibodies. This method offers several advantages, including a substantial enhancement in the purity and stability of the resulting EGFR recombinant monoclonal antibodies, as well as an increase in their affinity and specificity. Following synthesis, the EGFR recombinant monoclonal antibody undergoes purification through affinity chromatography. Subsequently, it undergoes comprehensive testing via various assays, including ELISA, IHC, and FC. This antibody exclusively recognizes the human EGFR protein.

EGFR is a vital cell surface receptor involved in regulating various aspects of cell growth, differentiation, and survival. Its dysregulation can contribute to cancer development, making it an important target for cancer therapy. Additionally, EGFR signaling plays a role in tissue repair, development, and immune modulation.

The vectors expressing anti-PXN antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-PXN (Y118), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening PXN antibody gene, and amplifying heavy and light chain sequence by PCR and cloning them into plasma vectors. After that, the vector clones were transfected into the mammalian cells for production. The product is the recombinant PXN antibody. Recombinant PXN antibody in the culture medium was purified using affinity-chromatography. It can react with PXN protein from Human and is used in the ELISA, WB.

PXN encodes a cytoskeletal protein involved in the actin-membrane attachment at sites of cell adhesion to the extracellular matrix. According to some studies, PXN may have the following characteristics.
The MBNL3 splicing factor increases the expression of PXN through alternative splicing of lncRNA-PXN-AS1 and promotes hepatocellular carcinoma. Nobiletin inhibits angiogenesis by modulating Src/FAK/STAT3-mediated signaling in ER+ breast cancer cells via PXN. ETV4 overexpression promotes the progression of non-small cell lung cancer by upregulating the transcription of PXN and MMP1. Pan-cancer analysis reveals immunological roles and prognostic potential of PXN in human cancers.