The vectors expressing anti-GSK3B antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-GSK3B (Ser9), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening GSK3B 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 GSK3B antibody. Recombinant GSK3B antibody in the culture medium was purified using affinity-chromatography. It can react with GSK3B protein from Human and is used in the ELISA, WB, IHC, IF.

The protein encoded by GSK3B is a serine-threonine kinase belonging to the glycogen synthase kinase subfamily. It is a negative regulator of glucose homeostasis and is involved in energy metabolism, inflammation, ER-stress, mitochondrial dysfunction and apoptosis pathways. According to some studies, GSK3B may have the following characteristics.
Inhibition of DYRK1A and GSK3B induces human β-cell proliferation. GSK3B polymorphisms alter transcription and splicing and interact with Tau haplotypes to alter disease risk in Parkinson's disease. A phased approach was used to investigate the role of GSK3B in dementia susceptibility in several different cohorts of patients with Alzheimer's disease and frontotemporal dementia. miR-769 may act as a tumor promoter by targeting GSK3B during human melanoma development. GSK3B induces autophagy by phosphorylating ULK1. ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-dependent phosphorylation of CRMP2.

The vectors expressing anti-MAPK3/MAPK1 antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-MAPK3 (T202/Y204) + MAPK1 (T185/Y187), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening MAPK3/MAPK1 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 MAPK3/MAPK1 antibody. Recombinant MAPK3/MAPK1 antibody in the culture medium was purified using affinity-chromatography. It can react with MAPK3/MAPK1 protein from Human and is used in the ELISA, WB.

The phosphorylated mitogen-activated protein kinase3/1 (MAPK3/1) protein is expressed in some primordial follicles and all growing follicles. Culture of 3 days post-parturition (dpp) ovaries with the MAPK3/1 signaling inhibitor U0126 significantly reduced the number of activated follicles and was accompanied by dramatically reduced granulosa cell proliferation and increased oocyte apoptosis. MAPK3 and its isoforms have been commonly ascribed analogous downstream functions due to their striking similarities. However, it is becoming increasingly clear that these isoforms- particularly MAPK3 and MAPK1 have explicitly different functions. While MAPK1 has a more pronounced role in cell proliferation and developmental processes. MAPK3 does not seem to be required during development and its deficiency may be compensated for by MAPK1. So far, a deficiency of MAPK3 in the CNS has been associated with facilitated learning and long-term memory. MAPK3 (Erk1) is important for the induction of T-cell anergy. Our goal was to determine the influence of MAPK3 on the capacity of DC to arm T-cell responses in autoimmunity.

The process of obtaining the recombinant monoclonal antibody against ATP7B begins with the insertion of ATP7B antibody genes into plasmid vectors. These modified plasmid vectors are then introduced into suitable host cells for expression using exogenous protein expression techniques. Afterward, the ATP7B recombinant monoclonal antibody is subjected to purification through affinity chromatography. It has undergone thorough validation for specific applications, including ELISA, IF, and FC. Importantly, this antibody specifically targets the human ATP7B protein.

ATP7B is a critical protein involved in copper homeostasis, ensuring the proper uptake, transport, distribution, and excretion of copper within the body. Dysfunctional ATP7B can lead to copper-related disorders, such as Wilson's disease, characterized by copper accumulation and associated health problems.

CUSABIO cloned PTEN 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 PTEN were harvested and characterized. The recombinant PTEN antibody was purified by affinity-chromatography from the culture medium. It can be used to detect PTEN protein from Human in the ELISA, WB.

PTEN is a protein-coding gene that encodes Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN. Disorders associated with PTEN include Cowden syndrome 1 and macrocephaly/autism syndrome. Its related pathways include metabolism and T cell receptor and co-stimulatory signaling. According to some studies, PTEN may have the following characteristics.
PTEN may inhibit tumor cell growth by antagonizing protein tyrosine kinases, and may regulate tumor cell invasion and metastasis through interactions at focal adhesions. PTEN is frequently disrupted in a variety of sporadic tumors and is targeted by germline mutations in patients with cancer susceptibility syndromes. The mechanisms regulating PTEN expression and function, including transcriptional regulation, post-transcriptional regulation of noncoding RNAs, post-translational modifications, and protein-protein interactions, are altered in cancer.

The generation of the DSG2 recombinant monoclonal antibody involved the incorporation of DSG2 antibody genes into plasmid vectors. These engineered plasmid vectors were subsequently introduced into suitable host cells using exogenous protein expression techniques to facilitate antibody production. After that, the DSG2 recombinant monoclonal antibody underwent a purification process via affinity chromatography. Rigorous validation for ELISA suitability of this antibody was performed. In a functional ELISA assay, it was established that the DSG2 recombinant monoclonal antibody exhibited robust binding affinity to the human DSG2 protein (CSB-MP622752HU) at a concentration of 2 μg/mL, with an EC₅₀ falling within the range of 20.26 to 38.00 ng/mL.

The main function of the DSG2 protein is to mediate cell-cell adhesion by forming desmosomes, thereby contributing to tissue integrity and stability in various tissues, including the skin and the heart. Dysregulation of DSG2 can have significant implications for tissue function and may be associated with certain diseases such as pemphigus vulgaris and arrhythmogenic cardiomyopathy.

In the production of the phospho-RB1 (S780) recombinant monoclonal antibody, the process commences with the extraction of RB1 antibody genes from immunized rabbits, originally exposed to a synthetic peptide derived from the human RB1 protein phosphorylated at S780. These isolated genes are then ingeniously inserted into expression vectors. Following this step, the modified vectors are skillfully introduced into host suspension cells, where they are diligently cultivated to stimulate the production and secretion of the antibodies. Subsequently, the phospho-RB1 (S780) recombinant monoclonal antibody is subjected to a rigorous purification technique involving affinity chromatography, enabling the separation of the antibody from the surrounding cell culture supernatant. Ultimately, the antibody's functionality is comprehensively assessed across a spectrum of assays, encompassing ELISA, IHC, IF, and IP tests, thereby confirming its capability to interact with human RB1 protein phosphorylated at S780.

Phosphorylation of retinoblastoma 1 (RB1) at S780 is often associated with the transition from the G1 phase to the S phase of the cell cycle, where cells prepare for DNA replication. When phosphorylated at S780, RB1 becomes inactivated, leading to the release of E2F transcription factors and allowing them to promote the transcription of genes required for cell cycle progression and cell proliferation. Dysregulation of RB1 phosphorylation at S780 can contribute to uncontrolled cell proliferation and is frequently observed in various cancers.

The production of the IL2RA recombinant monoclonal antibody involved the incorporation of IL2RA antibody genes into plasmid vectors. These engineered plasmid vectors were then introduced into suitable host cells using exogenous protein expression technology to facilitate antibody expression. Subsequently, the IL2RA recombinant monoclonal antibody underwent a purification process utilizing affinity chromatography. It was rigorously validated for its compatibility with ELISA. In a functional ELISA test, it was demonstrated that this IL2RA recombinant monoclonal antibody exhibited strong binding affinity to the human IL2RA protein (CSB-MP011649HU3) at a concentration of 2 μg/mL, with an EC₅₀ falling within the range of 2.463 to 3.353 ng/mL.

IL2RA, also known as CD25, functions as a component of the IL-2 receptor complex on the surface of certain immune cells, particularly T cells. IL-2RA is a critical protein involved in regulating IL-2 signaling, T-cell activation, and immune responses.

In the production of the phospho-MTOR (S2448) recombinant monoclonal antibody, the initial step involves isolating the genes responsible for encoding the MTOR antibody from rabbits that have been immunized with a synthesized peptide derived from the human MTOR protein phosphorylated at S2448. Following this, these antibody genes are cloned into specialized expression vectors, after which the genetically modified vectors are introduced into mammalian suspension cells. These mammalian cells are then cultured, allowing them to express and secrete the antibodies. Subsequently, a meticulous purification process utilizing affinity chromatography is employed to isolate the phospho-MTOR (S2448) recombinant monoclonal antibody from the cell culture supernatant. Finally, the antibody's functionality is rigorously assessed through a battery of tests, including ELISA, WB, IHC, and IF, effectively confirming its ability to react with human MTOR protein phosphorylated at S2448.

Phosphorylation of MTOR at S2448 is a critical regulatory event in cell signaling. MTOR is a serine/threonine kinase that plays a central role in controlling cell growth, proliferation, and survival. When phosphorylated at S2448, MTOR becomes activated and is involved in promoting protein synthesis, cell growth, and cell survival.