The vectors expressing anti-ATM antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-ATM (S1981), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening ATM 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 ATM antibody. Recombinant ATM antibody in the culture medium was purified using affinity-chromatography. It can react with ATM protein from Human and is used in the ELISA, IF.

ATM is a protein-coding gene that encodes the serine-protein kinase ATM. Diseases associated with ATM include ataxia and mantle cell lymphoma. Its related pathways include miRNA regulation of DNA damage response and DNA damage response. According to some research, ATM may have the following features.
ATM is an important sensor of reactive oxygen species in human cells. A portion of nuclear ATM co-localizes with γ-H2AX at DSBs in response to DNA damage. ATM is also active in other cellular signaling pathways involved in maintaining cellular homeostasis. Various injury-induced responses may be activated by enhancing the protein kinase activity of ATM. ATM is activated by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex. ATM and ATR often work together to signal DNA damage and regulate downstream processes.

The vectors expressing anti-SNCA antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-SNCA (S129), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening SNCA 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 SNCA antibody. Recombinant SNCA antibody in the culture medium was purified using affinity-chromatography. It can react with SNCA protein from Human and is used in the ELISA, IHC, IF.

SNCA is a protein-coding gene encoding Alpha-synuclein. Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. SNCA may function to integrate presynaptic signaling and membrane trafficking. According to some studies, SNCA may have the following characteristics.
SNCA variants are associated with an increased risk of multiple system atrophy. The SNCA and MAPT regions are the major genes whose common variants are influencing the risk of Parkinson's disease. Compared with LRRK2 and VPS35, SNCA mutation carriers had a younger age of onset. Autophagy regulation allows aged cells to escape SNCA-induced toxicity. SNCA-induced toxicity in aged cells is associated with selective degradation of mitochondria.

The OSM recombinant monoclonal antibody was created by inserting the OSM antibody genes into plasmid vectors. These engineered plasmid vectors were subsequently introduced into suitable host cells using exogenous protein expression techniques to enable antibody production. Following the production phase, the OSM recombinant monoclonal antibody underwent a purification process via affinity chromatography. This antibody is recommended for use in ELISA. In the functional ELISA, this OSM recombinant monoclonal antibody effectively bound to the human OSM protein (CSB-MP017260HU1) at a concentration of 2 μg/mL, with an EC₅₀ falling within the range of 3.048 to 3.860 ng/mL.

Oncostatin-M (OSM) is a multifunctional cytokine that plays a central role in various physiological and pathological processes. Its functions include regulating the inflammatory response, modulating immune cells, influencing hematopoiesis, promoting tissue repair, and affecting tumor growth, among other roles.

Phospho-LAT (Y191) antibody CSB-RA012767A191phHU is a recombinant monoclonal antibody expressed by the plasmids containing the coding sequence of the LAT monoclonal antibody in the host cell lines. The synthesized peptide derived from phospho-LAT at Y191 residue was used to immunize the animals to get and isolate the LAT monoclonal antibody. This recombinant antibody against the phosphorylated LAT at Y191 is a rabbit IgG and can react with human samples. It underwent affinity-chromatography purification. And it can be used in ELISA, WB, IHC, IF, and IP applications.

LAT is a palmitoylated and membrane-associated adaptor protein phosphorylated at multiple tyrosine residues (e.g. Tyr132, Tyr171, Tyr191, and Tyr226) by ZAP-70 upon TCR stimulation. Phospho-LAT is activated and serves as an essential scaffold for the assembly of TCR-coupled signaling complexes that mediate productive T cell activation.

In the production of the phospho-TP53 (S33) recombinant monoclonal antibody, the initial phase entails the extraction of genes responsible for coding the TP53 antibody from rabbits previously subjected to immunization with a synthesized peptide originating from the human TP53 protein phosphorylated at S33. Subsequently, these antibody genes are introduced into specialized expression vectors. Following this step, the genetically modified vectors are meticulously transfected into host suspension cells. Once this transfection is successfully achieved, positive cells are cultivated to facilitate the robust expression and subsequent secretion of the antibodies. Following this cell culture phase, the phospho-TP53 (S33) recombinant monoclonal antibody undergoes a rigorous purification process employing affinity chromatography techniques, which effectively isolates the antibody from the surrounding cell culture supernatant. Ultimately, the antibody's efficacy is comprehensively assessed through a battery of examinations, spanning ELISA, IHC, and IF tests, conclusively affirming its ability to interact effectively with human TP53 protein phosphorylated at S33.

Phosphorylation of p53 at S33 is a critical mechanism for coordinating DNA repair, cell cycle regulation, and cell fate decisions in response to stress and damage. Dysregulation of this phosphorylation event can lead to uncontrolled cell proliferation and is often observed in cancer cells.

To generate the MYL9 recombinant monoclonal antibody, the MYL9 antibody genes were initially integrated into plasmid vectors. These engineered plasmid vectors were subsequently introduced into suitable host cells utilizing exogenous protein expression techniques to facilitate antibody production. Subsequent to this production phase, the MYL9 recombinant monoclonal antibody underwent purification via affinity chromatography. This antibody is suitable for ELISA. In the functional ELISA, it was established that the MYL9 recombinant monoclonal antibody demonstrated robust binding to the human MYL9 protein (CSB-YP015318HU) at a concentration of 2 μg/mL, displaying an EC₅₀ within the range of 4.628 to 6.430 ng/mL.

MYL9 is a versatile protein that functions as a regulatory subunit of myosin II in both muscle and non-muscle cells. Its main roles include regulating muscle contraction, controlling cell motility, and participating in various cellular processes associated with changes in cell shape and movement. The phosphorylation of MYL9 and its interactions with other proteins are central to its functions in these processes.

The STAT3 recombinant monoclonal antibody was produced by first incorporating STAT3 antibody genes into plasmid vectors. These constructed plasmid vectors were then introduced into appropriate host cells to enable antibody expression using exogenous protein expression technology. Following this, the STAT3 recombinant monoclonal antibody underwent purification via affinity chromatography and was subsequently verified for its suitability in ELISA assays. In a functional ELISA test, it was determined that this STAT3 recombinant monoclonal antibody could efficiently bind to the human STAT3 protein (CSB-BP022812HU(A4)j7) at a concentration of 2 μg/mL, displaying an EC₅₀ within the range of 41.31 to 75.59 ng/mL.

STAT3 is a multifunctional protein that plays a central role in cellular signaling, immune responses, inflammation, and various physiological and pathological processes. Its regulation of gene expression makes it a key player in coordinating cellular responses to extracellular signals and maintaining tissue homeostasis. Dysregulation of STAT3 signaling can have profound implications for health and disease.

The recombinant monoclonal antibody targeting ERBB2 is produced through a series of steps. Initially, ERBB2 antibody genes are integrated into plasmid vectors. These modified plasmid vectors are then introduced into suitable host cells for expression using exogenous protein expression techniques. Subsequently, the ERBB2 recombinant monoclonal antibody is purified using affinity chromatography. Comprehensive validation of this antibody has been conducted for specific applications, including ELISA and IHC. It's important to emphasize that this antibody exclusively recognizes the human ERBB2 protein.

The main function of ERBB2 (HER2) is to regulate cell signaling pathways that control cell growth, proliferation, differentiation, and survival. Dysregulation of ERBB2 signaling is associated with cancer development and progression.