The recombinant PRKAA2 antibody is a monoclonal antibody generated by cloning PRKAA2 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 PRKAA2 antibody was purified using affinity-chromatography. It has verified to detect PRKAA2 protein from Human in the ELISA, WB, IF.

The Thr172 Phospho-PRKAA2 antibody can detect the PRKAA2 protein phosphorylated at the Thr172 residue. PRKAA2 is the AMPK alpha 2 subunit and its phosphorylation of threonine at site 172 by upstream AMPKK plays a determinant role in fully activating AMPK. AMPK participates in the regulation of energy-producing metabolic and biosynthetic pathways during physiologic and pathologic cellular stress. AMPK activation enhances fatty acid oxidation, glucose transport, glycolysis while inhibiting triglyceride and protein synthesis.

The coding sequence for the phospho-ESR1 (S118) monoclonal antibody (isolated by immunizing animals with the synthetic phosphopeptide derived from human ESR1 around the phosphorylation site of Ser 118) was cloned into the plasmids and then transfected into cell lines for in vitro expression. The product underwent affinity-chromatography-mediated purification to get the phospho-ESR1 (S118) recombinant monoclonal antibody. This p-S118-ESR1 antibody is a rabbit IgG. It is suitable for the detection of human ESR1 phosphorylated at Ser 118 residue in ELISA and IHC applications.

ESR1 is a ligand-dependent transcription factor that affects the expression of target genes. Two transcription activation functions, AF-1 and AF-2, act in a promoter- and cell-specific manner to activate gene expression. While estrogen (E2) binding regulates the activity of AF-2, phosphorylation at several sites regulates the activity of AF-1. S118, one of these phosphorylation sites, is of special relevance because its mutation inhibits ESR1 function considerably. S118 has been demonstrated to be phosphorylated by the ERK1/2 mitogen-activated protein kinases (MAPK) and the cyclin-dependent protein kinase Cdk7 in previous research.

The phospho-STAT3 (S727) recombinant monoclonal antibody is a highly specific antibody against the pS727-STAT3 from human sources. This phospho-STAT3 (S727) antibody was expressed by transfecting the human phospho-STAT3 (S727) 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. Its isotype matches with the rabbit IgG. This phospho-STAT3 (S727) antibody can be used in ELISA, WB, IHC, and IP applications.

STAT3 has a role in a variety of biological processes, including cancer and immunology. When JAKs associated with cytokine-stimulated receptors phosphorylate STAT3 monomers at tyrosine 705 (pY705), cytoplasmic STAT3 monomers dimerize and translocate to the nucleus, where the homodimers promote target gene transcription. Members of the MAPK and c-Jun N-terminal kinase families can also phosphorylate STAT3 at serine 727 (pS727). The role of pS727 has been shown to improve STAT3's transcriptional activity, and later pS727 was shown to reduce the duration of STAT3's transcriptional activity for the socs3 gene by promoting pY705 dephosphorylation.

The BECN1 recombinant monoclonal antibody is created through the utilization of in vitro expression systems. These systems are established by cloning the DNA sequences of BECN1 antibodies obtained from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human BECN1 protein. Subsequently, the genes encoding the BECN1 antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are then transfected into host cells to enable the expression of the antibody. Following expression, the BECN1 recombinant monoclonal antibody undergoes affinity-chromatography purification. Rigorous testing in ELISA and FC applications confirms its reactivity with the human BECN1 protein.

BECN1 is a key component of the autophagic machinery and is essential for the initiation and regulation of autophagy, a process that plays a central role in cellular quality control, homeostasis, and responses to stress. Dysregulation of BECN1 and autophagy has been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

The creation of the phospho-STAT1 (S727) recombinant monoclonal antibody involves the utilization of protein technology and DNA recombinant techniques. The procedure begins with the immunization of animals using a synthesized peptide derived from human phospho-STAT1 (S727). Next, B cells are isolated from the immunized mice. Positive B cells are then selected and subjected to single clone identification. The light and heavy chains of the phospho-STAT1 (S727) antibody are amplified using PCR and inserted into a plasmid vector to create a recombinant vector, which is subsequently transfected into host cells to facilitate antibody expression. Finally, the phospho-STAT1 (S727) recombinant monoclonal antibody is purified from the cell culture supernatant using affinity chromatography. It has been validated for use in ELISA, WB, IHC, and IF to detect human STAT1 phosphorylated at S727 residue.

CUSABIO's strategy for developing a recombinant monoclonal antibody targeting EGF began with the immunization of a rabbit using a synthesized peptide derived from human EGF protein. Subsequent steps involved isolating B cells from the immunized rabbit and extracting RNA from these cells. The extracted RNA was reverse-transcribed into cDNA, which was employed as a template for extending EGF antibody genes using degenerate primers. These engineered EGF antibody genes were then incorporated into a plasmid vector and introduced into host cells for expression. The resulting EGF recombinant monoclonal antibody was isolated from the cell culture supernatant via affinity chromatography and assessed for its suitability in ELISA, IHC, and FC applications, demonstrating specific recognition of human EGF protein.

EGF is a versatile and essential growth factor that regulates various cellular processes, including cell proliferation, differentiation, and tissue repair. Its signaling through the EGFR is tightly controlled to ensure proper tissue development and maintenance.

In efforts to develop a recombinant monoclonal antibody specific to SATB2, the initial step involved the immunization of a rabbit with a synthesized peptide derived from human SATB2 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 SATB2 antibody genes using degenerate primers. These engineered SATB2 antibody genes were then integrated into a plasmid vector and introduced into host cells for expression. Subsequently, the SATB2 recombinant monoclonal antibody was isolated from the cell culture supernatant via affinity chromatography and assessed for its suitability in ELISA and IHC applications. It only shows reactivity with human SATB2 protein.

SATB2 is a multifunctional protein that plays crucial roles in development, cell differentiation, and gene regulation. Its functions are particularly important in craniofacial development, bone formation, neuronal development, and the maintenance of chromatin structure. Dysregulation of SATB2 can have significant implications for health and development.

To create the phospho-TP53 (S392) 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 TP53 protein phosphorylated at S392. 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-TP53 (S392) recombinant monoclonal antibody undergoes a rigorous purification process using affinity chromatography techniques, effectively separating the antibody from the surrounding cell culture supernatant. Finally, the functionality of the antibody is comprehensively assessed through a battery of tests, including ELISA and WB, conclusively confirming its capability to interact effectively with the human TP53 protein phosphorylated at S392.

The phospho-NBN (S343) recombinant monoclonal antibody is a highly specific antibody against the phosphorylated human NBN at Ser 343. This phospho-NBN (S343) antibody was expressed by transfecting the S343 phospho-NBN 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. Its isotype matches with the rabbit IgG. This anti-NBN-pS343 antibody can be used in ELISA and WB applications.

NBN is a part of the MRE11/RAD50/NBN complex, which is involved in the detection and repair of DNA double-strand breaks in the early stages. The Nijmegen breakage syndrome is caused by mutations in the NBN gene (NBS). ATM phosphorylation of NbN is required for some human cell responses to DNA damage. The central region of NBN has several SQ motifs that are phosphorylated by ATM. In particular, phosphorylation of serine residues S278 and S343 are required for intra-S phase checkpoint activation.

In the development of the phospho-MYC (S62) recombinant monoclonal antibody, the initial phase comprises the retrieval of genes responsible for coding the MYC antibody. These genes are acquired from rabbits that have been previously exposed to a synthesized peptide derived from the human MYC protein phosphorylated at S62. Subsequently, these antibody genes are seamlessly integrated into specialized expression vectors. Following this genetic modification, the vectors are introduced into host suspension cells, which are carefully cultured to stimulate the expression and secretion of antibodies. Following this cultivation phase, the phospho-MYC (S62) recombinant monoclonal antibody is subjected to a thorough purification process utilizing affinity chromatography techniques, effectively separating the antibody from the surrounding cell culture supernatant. Ultimately, the functionality of the antibody is comprehensively evaluated through a diverse array of assays, including ELISA, WB, and IF tests, unequivocally confirming its capacity to interact with the human MYC protein phosphorylated at S62.

Phosphorylation of MYC at S62 is a crucial regulatory mechanism that modulates MYC's transcriptional activity and function. Dysregulation of this phosphorylation event can have significant implications for cancer development and progression, making MYC an important target for cancer research and therapy.