The process of generating the RAN recombinant monoclonal antibody commences with the acquisition of the RAN antibody genes. These RAN antibody genes are then introduced into suitable host cells, which are cultured for the synthesis of RAN antibodies. This approach offers numerous benefits, including a significant enhancement in the purity and stability of the resulting RAN recombinant monoclonal antibodies, as well as an increase in their affinity and specificity. After synthesis, the RAN recombinant monoclonal antibody undergoes purification via affinity chromatography. Subsequently, it undergoes extensive testing through various assays, including ELISA, IHC, IF, and FC. This antibody specifically targets the human RAN protein.

The GTP-binding nuclear protein Ran is a critical regulator of nucleocytoplasmic transport, facilitating the import and export of molecules between the nucleus and cytoplasm. Its role in maintaining proper cellular compartmentalization, coordinating mitotic processes, and regulating the integrity of nuclear pore complexes makes Ran essential for fundamental cellular functions and cell cycle progression.

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

Anti-phospho-specific T401 BRAF antibody can recognize the BRAF protein phosphorylated at T401 residue. BRAF is a core component of the RAS-RAF-MEK-ERK signaling cascade that is involved in the control of various cell activities including cell proliferation, survival, differentiation, and migration. Phosphorylation of BRAF at T401 by activated ERK contributes to the RAF dimerization. Studies have shown that the calcineurin target reside on BRAF is T401, a site of negative feedback phosphorylation by ERK1/2. Phosphorylated BRAF at T401 and S419 residues are somatically mutated in tumors.

The vectors expressing anti-PRKCA antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-PRKCA (T638), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening PRKCA 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 PRKCA antibody. Recombinant PRKCA antibody in the culture medium was purified using affinity-chromatography. It can react with PRKCA protein from Human and is used in the ELISA, WB, IF.

The PRKCA gene is large, containing 17 exons spanning 0.5Mb of genomic DNA. It encodes the PKC alpha protein and is a cytoplasmic serine/threonine kinase member of the AGC (PKA, PKG, PKC) family. According to some studies, PRKCA may have the following characteristics.
PRKCA acts as a repeatedly mutated tumor gene in human cancers and uncovers potential therapeutic holes in this uncommon brain tumor. Multipoint SNP analysis indicated an association with PRKCA and its telomeric flanking regions in both populations, and combined SNP haplotype and genotype analysis revealed an allelic variant of PRKCA. PRKCA fusions are highly diagnostic for PGNT, and rare fusion partners can be identified by RNA-sequencing detection. Genomic analysis of pigment epithelial melanoma reveals recurrent alterations in PRKAR1A and PRKCA genes.

The process for creating the TP53 recombinant monoclonal antibody begins by obtaining the TP53 antibody genes, which are then introduced into suitable host cells. These cells serve as the foundation for synthesizing TP53 antibodies using a cell-based expression and translation system. This method offers multiple advantages, notably enhancing the purity and stability of the resultant TP53 recombinant monoclonal antibodies, as well as elevating their affinity and specificity. Post-synthesis, the TP53 recombinant monoclonal antibody goes through a purification stage involving affinity chromatography. Subsequently, it undergoes comprehensive testing, including ELISA, WB, IF, and FC assays. This antibody exclusively targets the human TP53 protein.

TP53 is a critical protein involved in maintaining genomic integrity and preventing the formation of cancer. Its functions include cell cycle regulation, DNA repair, apoptosis induction, and various other roles in response to cellular stress. Mutations in the TP53 gene are commonly associated with a higher risk of cancer development due to the loss of its tumor suppressor functions.

The recombinant PAK3/PAK1/PAK2 antibody is a monoclonal antibody generated by cloning PAK3/PAK1/PAK2 antibody genes into plasma vectors and transfecting vector clones into stable cell lines for production. For recombinant antibody generation, mammalian cell lines like CHO cells and HEK293 are commonly used. The recombinant PAK3/PAK1/PAK2 antibody was purified using affinity-chromatography. It has verified to detect PAK3/PAK1/PAK2 protein from Human in the ELISA, WB, IHC.

PAKs are subdivided into two groups: type I PAKs (PAK1, PAK2, and PAK3) and type II PAKs (PAK4, PAK5, and PAK6). PAKs contain a highly conserved C-terminal kinase domain but a variable N-terminal regulatory domain responsible for their implication in a variety of intracellular signaling pathways. Both groups bind Cdc42 and Rac1 GTPases through their p21 GTPase-binding domain (PBD) but only the PAKs of group I are activated by this interaction. p21-Activated kinases play important roles in cell physiology and are key regulators of several signaling pathways including actin cytoskeleton dynamics and cell cycle progression. Particularly, the p21-activated kinases PAK1 and PAK2 play essential roles in cell division and brain development and are well-known oncogenes. Moreover, in addition to their roles in cytoskeleton and proliferation regulation, PAKs play an important role in neuronal development. Some recent data shows that PAK3, whose expression is restricted to the CNS, is specifically implicated in the pathophysiology of mental retardation and in some cancers.

The rabbit IgG recombinant phospho-STAT5A (Y694) monoclonal antibody specifically targets the phosphorylated STAT5A at Tyr 694. The DNA encoding the phospho-STAT5A (Y694) monoclonal antibody was inserted into the plasmid and subsequently transfected into the cell line for expression. The product was purified through the affinity-chromatography method to get the pY694-STAT5A recombinant antibody. This phospho-STAT5A (Y694) antibody shows reactivity with human samples. It has been validated for ELISA, WB, and IHC applications.

STAT5, frequently activated in hematological malignancies, is a critical signaling node downstream of the BCR-ABL oncogene. STAT5 is typically activated when phosphorylated at Tyr 694 residue in the C-terminus by receptor-associated Jaks. In certain malignancies of both hematopoietic and non-hematopoietic origin, phosphorylation of STAT5 at Tyr 694 is required for cell survival, proliferation, angiogenesis, and metastasis.

The production of the phospho-NFKBIA (S32) recombinant monoclonal antibody starts with the isolation of genes responsible for encoding this antibody from rabbits previously immunized with a synthesized peptide derived from the human NFKBIA protein phosphorylated at S32. These antibody genes are then meticulously cloned into specialized expression vectors. Following this genetic modification, the modified vectors are introduced into host suspension cells, which are carefully cultured to stimulate the expression and secretion of antibodies. After this cultivation phase, the phospho-NFKBIA (S32) recombinant monoclonal antibody is subjected to a rigorous purification process utilizing affinity chromatography techniques, effectively separating the antibody from the surrounding cell culture supernatant. Finally, the functionality of the antibody is comprehensively assessed through a diverse range of assays, including ELISA, WB, and IF tests, conclusively confirming its ability to interact effectively with the human NFKBIA protein phosphorylated at S32.

Phosphorylation of NFKBIA at S32 is a critical regulatory event in the NF-κB signaling pathway, controlling the activation of NF-κB and influencing various cellular processes, including immune responses, inflammation, and cell survival. Dysregulation of this phosphorylation event can have significant implications in inflammatory diseases, cancer, and other pathological conditions.

Phospho-MAPT (T231) antibody CSB-RA013481A231phHU is a recombinant monoclonal antibody produced from the expression of the plasmids that were constructed by the pT231-MAPT monoclonal antibody (generated from animals with the synthesized peptide derived from human phospho-MAPT (T231) immunization) DNA sequence in cell lines. The phospho-MAPT (T231) antibody was purified through affinity- chromatography method. It is a rabbit IgG antibody. It is recommended for the detection of human MAPT phosphorylated at T231 in ELISA and WB analyses.

Tau's ability to bind and assemble microtubules (MTs) is regulated by phosphorylation and other posttranslational modifications. Tau phosphorylation reduces its affinity for MTs and eliminates its capacity to drive MT polymerization in general, but the specific consequences vary depending on the number and position of phosphorylation sites. Phosphorylated T231 selectively forms a salt bridge with R230 that can compete with the buildup of intermolecular salt bridges to tubulin.

The PIK3R1 recombinant monoclonal antibody is generated using in vitro expression systems developed by cloning the DNA sequences of PIK3R1 antibodies from immunoreactive rabbits. The immunogen used in this process is a synthesized peptide derived from the human PIK3R1 protein. Subsequently, the genes encoding the PIK3R1 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells to facilitate the expression of the antibody. Following expression, the PIK3R1 recombinant monoclonal antibody undergoes affinity-chromatography purification. It is rigorously tested for functionality in ELISA and IHC applications, demonstrating reactivity with the human PIK3R1 protein during these laboratory evaluations.

PIK3R1 is a critical regulatory protein that plays a central role in controlling the PI3K signaling pathway. This pathway influences a wide range of cellular functions, including cell growth, proliferation, survival, metabolism, and immune responses. Dysregulation of PIK3R1 or the PI3K pathway can have significant implications in various diseases, including cancer and metabolic disorders.

To create the phospho-RPS6KA5 (S376) recombinant monoclonal antibody, the process initiates with the isolation of genes responsible for coding this antibody from rabbits that have been previously exposed to a synthesized peptide originating from the human RPS6KA5 protein phosphorylated at S376. These antibody genes are then meticulously integrated into specialized expression vectors. Following this genetic modification, the vectors are thoughtfully introduced into host suspension cells, which are diligently cultivated to encourage the production and secretion of antibodies. After this cultivation phase, the phospho-RPS6KA5 (S376) recombinant monoclonal antibody undergoes a thorough purification process using affinity chromatography techniques, effectively separating the antibody from the surrounding cell culture supernatant. Finally, the functionality of the antibody is rigorously assessed through ELISA and IHC, conclusively confirming its capability to interact effectively with the human RPS6KA5 protein phosphorylated at S376.

Phosphorylation of RPS6KA5 at S376 is a crucial regulatory mechanism that allows cells to respond to extracellular signals and stressors, modulating gene expression and influencing various cellular processes. Dysregulation of this phosphorylation event can have significant implications in diseases and conditions related to cell growth, stress responses, and gene expression.