The product CSB-RA019025A542phHU is a recombinant GDNF monoclonal antibody. It was generated by transfecting the human phospho-PTPN11 (Y542) monoclonal antibody gene-vector clones into the cell line for in vitro production and subsequent purification from the tissue culture supernatant (TCS) through affinity-chromatography. This phospho-PTPN11 (Y542) antibody is reactive with human PTPN11 phosphorylated at Y542. And it has been tested for use in multiple applications, including ELISA, WB, and IP.

PTPN11, also known as Shp2, is a widely expressed protein tyrosine phosphatase, and its kinase-induced hyperactivity has been linked to a variety of cancers. RTKs like EPHA2 phosphorylate Y542 and Y580 on PTPN11, which prolongs ERK activation by keeping PTPN11 in an open conformation. According to studies, phosphorylated Y542 interacts intramolecularly with the N-SH2 domain of Shp2 to relieve PTPase basal inhibition, whereas phosphonate at Y580 enhances PTPase activity through interacting with the C-SH2 domain.

In the quest to develop the phospho-MAPT (S396) recombinant monoclonal antibody, the initial phase involves the extraction of genes encoding this antibody from rabbits that have been previously exposed to a synthesized peptide derived from the human MAPT protein phosphorylated at S396. These antibody genes are then seamlessly integrated into specialized expression vectors. Following this genetic modification, the vectors are carefully introduced into host suspension cells, which are diligently cultured to stimulate the expression and secretion of antibodies. Subsequently, the phospho-MAPT (S396) recombinant monoclonal antibody is subjected to a meticulous purification process utilizing affinity chromatography, effectively isolating the antibody from the surrounding cell culture supernatant. Finally, the antibody's functionality is comprehensively evaluated through ELISA and WB tests, unequivocally confirming its capacity to interact effectively with the human MAPT protein phosphorylated at S396.

The process of generating a recombinant monoclonal antibody against MKI67 began with the immunization of a rabbit using a synthesized peptide from human MKI67 protein. B cells were subsequently isolated from the immunized rabbit, and RNA was extracted from these B cells. The extracted RNA was reverse-transcribed into cDNA, which was utilized as a template for amplifying MKI67 antibody genes using degenerate primers. These amplified MKI67 antibody genes were then integrated into a plasmid vector and introduced into host cells for expression. The MKI67 recombinant monoclonal antibody was then purified from the cell culture supernatant through affinity chromatography and subjected to ELISA, IHC, and FC applications, displaying specific reactivity with human MKI67 protein.

The main function of the MKI67 protein, also known as Ki-67, is as a cellular marker for cell proliferation. MKI67 is not directly involved in regulating the cell cycle or cell proliferation itself but serves as a valuable marker for assessing the proliferative activity of cells. Its primary function is to indicate whether a cell is in an active, proliferative state.

The DNA sequence coding for the pS82-HSPB1 monoclonal antibody produced from the animals with the phosphopeptide corresponding to the resides surrounding the Ser 82 of human HSPB1 immunization was cloned into the expression vector, which was further transfected into a cell line for in vitro expression. The product is the recombinant phospho-HSPB1-S82 monoclonal antibody. It specifically targets the human HSPB1 phosphorylated at Ser 82 residue. It belongs to the rabbit IgG. The affinity-chromatography purification method was used to purify this phosphorylated HSPB1 antibody. ELISA, WB, and IHC have been tested for this HSPB1 antibody.

HSPB1, an abundant molecular chaperone, is found in striated muscle and is phosphorylated in response to several stimuli, including mechanical stress. In response to stretch, HSPB1 is phosphorylated in cells and tissues, causing translocation to the Z-discs and to locations of elevated traction force within the cytoskeleton, implying that phosphorylation may initiate or regulate its interactions with mechanosensitive clients like FLNC at these sites. MAPKAPK2/3 phosphorylates HSPB1 at serine sites 15, 78, and 82 in the N-terminal region of the protein, outside of the alpha-crystallin domain.

In efforts to create a recombinant monoclonal antibody specific to NEUROD1, the initial step involved immunizing a rabbit with a synthesized peptide derived from human NEUROD1 protein. 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 served as a template for extending NEUROD1 antibody genes using degenerate primers. These extended NEUROD1 antibody genes were incorporated into a plasmid vector and introduced into host cells for expression. Subsequently, the NEUROD1 recombinant monoclonal antibody was purified from the cell culture supernatant through affinity chromatography and evaluated for its utility in ELISA, IF, and FC applications, showing specific reactivity with human NEUROD1 protein.

NEUROD1 is a critical transcription factor that orchestrates the differentiation and maturation of neurons during development, contributes to the formation of neural circuits, and plays a role in the maintenance of neuronal identity. Its functions are essential for the proper functioning of the nervous system, and its dysregulation can have significant implications for neurological health and disease.

CUSABIO got the DNA sequence of the pY15-CDK2 monoclonal antibody that was produced from the splenocytes generated by the human CDK2 synthesized phosphopeptide immunization. The DNA sequence was cloned into the plasmid and then transfected into cell lines for in vitro expression. The product is the phospho-CDK2 (Y15) recombinant monoclonal antibody. It is a rabbit IgG antibody purified using the affinity-chromatography method. This anti-pY15-CDK2 antibody is recommended for ELISA WB, IHC, and IP applications and detects the human CDK2 phosphorylated at Tyr 15 residue.

CDK2, a small serine/threonine kinase, regulates the initiation and progression of the S phase of the cell cycle, and the regulation of CDK2 involves cyclin binding and phosphorylation. Several mechanisms, including phosphorylation and dephosphorylation processes, regulate CDK2 activity. Cables increases Wee1-mediated CDK2 tyrosine 15 phosphorylation, thus decreasing CDK2 kinase activity and inhibiting cell growth. CDK2 is inactivated by phosphorylation of T14 and Y15, and activation of CDK2 needs dephosphorylation of both T14 and Y15 by Cdc25, as well as phosphorylation of T160 by CDK activating kinase (CAK).

The process of generating a recombinant monoclonal antibody against CASP9 began with the immunization of a rabbit using a synthesized peptide from human CASP9 protein. B cells were subsequently isolated from the immunized rabbit, and RNA was extracted from these B cells. The extracted RNA was reverse-transcribed into cDNA, which was employed as a template to extend CASP9 antibody genes using degenerate primers. These extended CASP9 antibody genes were incorporated into a plasmid vector and transfected into host cells for expression. The CASP9 recombinant monoclonal antibody was then purified from the cell culture supernatant through affinity chromatography and subjected to ELISA, IF, and FC applications. It shows specific reactivity with human CASP9 protein.

CASP9 is a key regulator of apoptosis, serving as the initiator caspase in the intrinsic pathway. Its activation marks the commitment of a cell to undergo programmed cell death, a fundamental process in development, tissue homeostasis, and the elimination of damaged or potentially harmful cells.

In the development of the phospho-STAT3 (Tyr705) recombinant monoclonal antibody, the process kicks off with the retrieval of genes responsible for encoding this antibody from rabbits that have undergone immunization with a synthesized peptide derived from the human STAT3 protein phosphorylated at Tyr705. These antibody genes are subsequently cloned into specialized expression vectors. Following this genetic modification, the vectors are introduced into host suspension cells, which are carefully cultivated to stimulate the production and secretion of antibodies. Subsequently, the phospho-STAT3 (Tyr705) recombinant monoclonal antibody is subjected to a meticulous purification process utilizing affinity chromatography techniques, effectively isolating the antibody from the surrounding cell culture supernatant. Lastly, the functionality of the antibody is comprehensively evaluated through a diverse array of assays, including ELISA, WB, and IHC tests, unequivocally confirming its capacity to interact with the human STAT3 protein phosphorylated at Tyr705.

Phosphorylation of STAT3 at Tyr705 is a crucial regulatory event that controls its transcriptional activity and influences various cellular processes, including immune responses and cell fate decisions. Dysregulation of this phosphorylation event can have significant implications in cancer, inflammation, and other diseases.

To manufacture the phospho-CDK1/CDK2/CDK3 (T14) recombinant monoclonal antibody, the journey begins with the retrieval of genes responsible for encoding the CDK1/CDK2/CDK antibody from rabbits that have previously been exposed to a synthesized peptide derived from the human CDK1/CDK2/CDK protein phosphorylated at T14. Subsequently, these antibody genes are skillfully cloned into specialized expression vectors. Following this genetic modification, the modified vectors are carefully introduced into host suspension cells, which are then diligently cultured to promote the expression and secretion of antibodies. After this cultivation phase, the phospho-CDK1/CDK2/CDK3 (T14) recombinant monoclonal antibody is meticulously purified from the cell culture supernatant through the application of affinity chromatography. Finally, the antibody's functionality is rigorously assessed through ELISA and WB, conclusively affirming its ability to effectively react with the human CDK1/CDK2/CDK protein phosphorylated at T14.

In order to develop a recombinant monoclonal antibody against ACTA1, CUSABIO initiated the process by immunizing a rabbit with a synthesized peptide derived from human ACTA1. Subsequently, B cells were isolated from the immunized rabbit, and RNA was extracted from these B cells. The extracted RNA was reverse-transcribed into cDNA, serving as a template for extending ACTA1 antibody genes using degenerate primers. These extended ACTA1 antibody genes were integrated into a plasmid vector and introduced into host cells for expression. The ACTA1 recombinant monoclonal antibody was then purified from the cell culture supernatant via affinity chromatography and assessed for its suitability in ELISA, IHC, and FC applications. It shows specific recognition of the human ACTA1 protein.

ACTA1 is a major component of the thin filaments in skeletal muscle fibers, where it interacts with myosin to generate the contractile force required for muscle contraction. Mutations in the ACTA1 gene can lead to various muscle disorders such as congenital myopathies.