The production of the mutated-HIST1H3A (K27) recombinant monoclonal antibody generally begins with the incorporation of the HIST1H3A antibody-encoding gene into expression vectors. These vectors are then introduced into host cells using polyethyleneimine-mediated transfection. The host cells, housing the expression vectors, are cultured to manufacture and release the antibodies. Subsequent purification via affinity chromatography is followed by assessments through ELISA and IHC assays, verifying their ability to specifically bind to the human HIST1H3A protein mutated at K27.

HIST1H3A mutated at K27 is known as H3K27M mutation and disrupts normal epigenetic regulation, leading to altered gene expression patterns that contribute to the development of aggressive pediatric brain tumors, most notably diffuse intrinsic pontine gliomas (DIPG) and midline gliomas.

The formyl-HIST1H3A (K122) recombinant monoclonal antibody generation typically starts with the insertion of the HIST1H3A antibody-encoding gene into expression vectors. These vectors are subsequently delivered into host cells through polyethyleneimine-mediated transfection methods. The host cells containing these vectors are cultured to produce and release the antibodies. After purification using affinity chromatography, the antibodies undergo testing through ELISA and IHC assays to confirm their recognition of the human HIST1H3A protein formylated at K122.

The AGO2 recombinant monoclonal antibody expression generally involves inserting the target gene that encodes the AGO2 antibody into expression vectors and then transferring these vectors into host cells via polyethylenimine-mediated transfection. Cells harboring the expression vectors are cultured to produce and secrete the antibodies. Following affinity chromatography purification, these antibodies' activities are assessed by ELISA, IF, and FC tests. They can recognize human AGO2 protein.

AGO2 is a central player in the RNAi pathway, where it associates with small RNA molecules to guide the silencing of specific target mRNAs. This post-transcriptional gene regulation has critical roles in gene expression, development, antiviral defense, and genome stability.

The ALB recombinant monoclonal antibody production begins with the extraction of ALB antibody genes. These genes are isolated from B cells derived from immunoreactive rabbits and then undergo amplification and are cloned into phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the generation of functional antibodies. The resulting ALB recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It can be used to recognize the human ALB protein in ELISA and FC applications.

Serum albumin (ALB) is the most abundant protein in human blood plasma and plays a central role in maintaining the physiological stability and homeostasis of the bloodstream. Its ability to transport, buffer, and protect various molecules and its influence on blood volume regulation makes it a critical component of human health. Dysregulation of albumin levels or function can have significant clinical implications.

The CHAT recombinant monoclonal antibody is synthetically produced in vitro using a systematic approach. Initially, CHAT antibody genes are extracted from B cells isolated from immunoreactive rabbits. These genes undergo amplification and are cloned into suitable phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the production of functional antibodies in significant quantities. The resulting CHAT recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It is suitable for the precise detection of human and mouse CHAT protein in various applications, including ELISA, WB, IHC, IF, and FC.

CHAT protein is responsible for catalyzing the synthesis of acetylcholine, a neurotransmitter that plays essential roles in neurotransmission, neuromuscular function, autonomic regulation, and cognitive processes. Its activity is crucial for the proper functioning of the nervous system and is of clinical significance in the context of neurological disorders and therapeutic interventions.

The SLC1A2 recombinant monoclonal antibody is synthesized in vitro through a systematic process. Initially, SLC1A2 antibody genes are isolated from B cells derived from immunoreactive rabbits. These genes undergo amplification and are cloned into phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the generation of functional antibodies in significant quantities. The resulting SLC1A2 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It can recognize human SLC1A2 protein in three applications, including ELISA, WB, and FC.

SLC1A2, or EAAT2/GLT-1, is a crucial protein responsible for clearing excess glutamate from the synaptic cleft, preventing excitotoxicity, and maintaining proper neurotransmission and brain function. Its role in glutamate transport is fundamental to neuronal health, synaptic plasticity, and the prevention of neurological disorders associated with glutamate dysregulation.

The phospho-ERBB2 (Y1139) recombinant monoclonal antibody is synthetically generated in vitro, starting with the extraction of ERBB2 antibody genes from B cells isolated from immunoreactive rabbits. These genes are then amplified and cloned into suitable phage vectors, which are subsequently introduced into mammalian cell lines to enable the production of functional antibodies in substantial quantities. Following this, the phospho-ERBB2 (Y1139) recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. It can used for the accurate detection of human ERBB2 protein phosphorylated at Y1139 in ELISA, IHC, and IF applications.

Phosphorylation of ERBB2 at Y1139 is a crucial post-translational modification that activates signaling pathways involved in cell growth, proliferation, and differentiation. Dysregulation of ERBB2 phosphorylation is implicated in cancer and is the target of therapeutic interventions in various malignancies, particularly breast cancer.

The NUMA1 recombinant monoclonal antibody is generated through in vitro processes using synthetic genes. This methodology involves the retrieval of NUMA1 antibody genes from B cells sourced from immunoreactive rabbits, followed by their amplification and cloning into appropriate phage vectors. These vectors are then introduced into mammalian cell lines, enabling the production of functional antibodies in substantial quantities. Subsequently, the NUMA1 recombinant monoclonal antibody is purified from the culture supernatant of the transfected cell lines through affinity chromatography. Its functionality has been tested in ELISA and FC applications to react with human NUMA1 protein.

NUMA1 is a multifunctional protein primarily known for its critical role in organizing and stabilizing the mitotic spindle during cell division. Proper spindle assembly and chromosome segregation are essential for the accurate transmission of genetic material to daughter cells, and NUMA1 plays a central role in these processes.