Anti-phospho-EIF2S1 (S51) antibody is a recombinant monoclonal antibody that recognizes the human EIF2S1 phosphorylated at Ser51 residue. This phospho-EIF2S1 antibody was drawn and isolated from the cell culture supernatant that cultivates the mammalian cell lines containing vectors of the human phospho-EIF2S1 (S51) monoclonal antibody gene. This anti-phospho-EIF2S1 (S51) antibody underwent affinity-chromatography purification. It can be used for ELISA, WB, IHC, and IF testing with human samples.

The phosphorylation of the EIF2S1 protein is a crucial mechanism for translation control. Phosphorylation of EIF2S1 on residue S51 results in a stable (EIF2–GDP)–EIF2B interaction, which limits the GDP–GTP exchange and prevents active EIF2 liberation, reducing translation initiation. EIF2S1 has been demonstrated to be required for tumorigenesis and progression since tumors have a higher integrated stress response (ISR) than normal tissue in tumorigenesis, during which EIF2S1 maintains efficient translation of numerous genes involved in tumorigenesis.

The production of the phospho-PPP2CA (Y307) recombinant monoclonal antibody involves the utilization of protein technology and DNA recombinant techniques. Initially, animals are immunized with a synthesized peptide derived from human phospho-PPP2CA (Y307), resulting in the generation of B cells. These B cells are then screened to isolate positive ones, followed by single clone identification. The light and heavy chains of the phospho-PPP2CA (Y307) antibody are amplified via PCR and integrated into a plasmid vector to construct a recombinant vector. This recombinant vector is subsequently transfected into host cells to facilitate antibody expression. The phospho-PPP2CA (Y307) recombinant monoclonal antibody is purified from the supernatant of cell culture using affinity chromatography. Stringent validation is conducted to ensure its accuracy and efficacy for ELISA and WB applications. The phospho-PPP2CA (Y307) recombinant monoclonal antibody serves as a valuable tool for detection of human phospho-PPP2CA (Y307) protein in research settings.

The production of the phospho-EGFR (Y1092) recombinant monoclonal antibody involves the application of protein technology and DNA recombinant techniques. The process begins by immunizing animals with a synthesized peptide derived from human phospho-EGFR (Y1092), followed by the isolation of B cells. Positive B cells are then selected and undergo single clone identification. The light and heavy chains of the phospho-EGFR (Y1092) antibody are amplified through PCR and inserted into a plasmid vector to create a recombinant vector. This recombinant vector is transfected into host cells for antibody expression. The phospho-EGFR (Y1092) recombinant monoclonal antibody is purified from the cell culture supernatant using affinity chromatography. It serves as a valuable tool for the detection of human phospho-EGFR (Y1092) protein in ELISA and WB applications.

Phospho-GSK3A/GSK3B (Y216 + Y279) antibody CSB-RA009962A216phHU is a recombinant monoclonal antibody belonging to rabbit IgG. Its production procedures include: the acquisition of the anti-GSK3 Beta-pY216 + GSK3 Alpha-pY279 monoclonal antibody using the synthesized peptide derived from the human phospho-GSK3A/GSK3B (Y216 + Y279) immunizes animals; the determination of DNA sequence of the monoclonal antibody; the clone of the DNA sequence into the plasmid and subsequent transfection into cell lines for expression. This phospho-GSK3A/GSK3B (Y216 + Y279) antibody underwent purification using affinity-chromatography. It has been tested in ELISA and IHC. It is reactive with the human phospho-GSK3A/GSK3B (Y216 + Y279) protein.

All eukaryotes have GSK3, which is a versatile serine/threonine kinase. GSK3 is engaged in a wide range of cellular functions, from glycogen metabolism to cell cycle regulation and proliferation, and is a crucial regulator of numerous signaling pathways, including cellular responses to Wnt, receptor tyrosine kinases, and G protein-coupled receptors. GSK3α and GSK3β are two GSK-3 isoforms. GSK3 kinase activity is activated by phosphorylation on tyrosine residues (GSK3 Y279 and GSK3 Y216).

To create a recombinant monoclonal antibody against SOD2 acetylated at K68, CUSABIO's approach began with the immunization of a rabbit using a synthesized peptide derived from human SOD2 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 utilized as a template for extending SOD2 antibody genes using degenerate primers. These extended SOD2 antibody genes were integrated into a plasmid vector and introduced into host cells for expression. The acetyl-SOD2 (K68) recombinant monoclonal antibody was purified from the cell culture supernatant through affinity chromatography and evaluated for its utility in ELISA and IHC applications. It only reacts with human SOD2 protein acetylated at K68.

SOD2 is an enzyme responsible for scavenging superoxide radicals within the mitochondria, thereby protecting cells from oxidative damage. The acetylation of SOD2 at K68 is known to regulate enzymatic activity, protect against oxidative stress, as well as participate in mitochondrial function and cellular signaling.

The phospho-SMAD2 (S250) recombinant monoclonal antibody is produced using advanced techniques in protein and DNA recombinant technology. Initially, animals are immunized with a synthetic peptide derived from human phospho-SMAD2 (S250), resulting in the generation of B cells. From these B cells, positive clones are carefully selected and identified. The genes encoding the phospho-SMAD2 (S250) antibody are then amplified through PCR and inserted into a plasmid vector, creating a recombinant vector. This recombinant vector is transfected into host cells to enable the expression of the phospho-SMAD2 (S250) antibody. The phospho-SMAD2 (S250) recombinant monoclonal antibody is subsequently purified from the cell culture supernatant using affinity chromatography. This phospho-SMAD2 (S250) recombinant monoclonal antibody offers a reliable means to detect human phospho-SMAD2 (S250) protein with precision and accuracy in ELISA and WB applications.

Generating a recombinant monoclonal antibody targeting HSP90AB1 involved several key steps. Initially, a rabbit was immunized with a synthesized peptide derived from human HSP90AB1 protein. B cells were subsequently isolated from the immunized rabbit, and RNA was extracted from these cells. The extracted RNA was reverse-transcribed into cDNA, which was utilized as a template to extend HSP90AB1 antibody genes using degenerate primers. These extended HSP90AB1 antibody genes were then integrated into a plasmid vector and introduced into host cells for expression. The HSP90AB1 recombinant monoclonal antibody was purified from the cell culture supernatant via affinity chromatography and evaluated for its suitability in ELISA, IHC, and FC assays, demonstrating specificity for human HSP90AB1 protein.

HSP90AB1 is a critical molecular chaperone that plays a central role in protein folding, stabilization, and regulation. Its diverse client protein repertoire includes key players in various cellular processes and signaling pathways. HSP90AB1's functions are essential for maintaining cellular homeostasis, adapting to stress, and supporting the proper functioning of numerous proteins with pivotal roles in health and disease.

In the quest to manufacture the phospho-HSPB1 (S78) recombinant monoclonal antibody, the initial phase involves the retrieval of genes encoding the HSPB1 antibody from rabbits previously exposed to a synthesized peptide originating from the human HSPB1 protein phosphorylated at S78. These antibody genes are then adeptly integrated into specialized expression vectors. Subsequently, the genetically modified vectors are thoughtfully introduced into host suspension cells, where they are diligently cultivated to stimulate the production and secretion of antibodies. Following this growth phase, the phospho-HSPB1 (S78) recombinant monoclonal antibody is subjected to a rigorous purification process employing affinity chromatography techniques, effectively isolating the antibody from the surrounding cell culture supernatant. Lastly, the antibody's efficacy is comprehensively assessed through a diverse range of assays, encompassing ELISA, WB, and IHC tests, thereby confirming its ability to interact effectively with the human HSPB1 protein phosphorylated at S78.

Phosphorylation of HSPB1 at S78 is a critical regulatory mechanism that allows cells to respond to stress, maintain protein quality control, and promote cell survival. Dysregulation of this phosphorylation event can have significant implications in various diseases, including cancer and neurodegenerative disorders.

The synthesized DNA sequence corresponding to the phospho-FOXO3 (S253) monoclonal antibody was cloned into the plasmid and then transfected into the cell line for expression. The product was purified through the affinity-chromatography method and obtained the phospho-FOXO3 (S253) recombinant monoclonal antibody. This FOXO3-pS253 recombinant antibody is a rabbit IgG and has been tested in scientific applications, including ELISA, WB, and IHC. It can be used to detect the human FOXO3 phosphorylated at Ser253 residue.

FOXO3 is a transcription factor that controls a variety of physiological processes such as cell cycle arrest, apoptosis, oxidative stress response, and energy consumption. Various post-translational modifications, such as acetylation, ubiquitination, and phosphorylation, regulate FOXO3. AKT phosphorylates FOXO3 at T32 and S253, forming 14-3-3 binding sites, which modulates FOXO3 transcriptional activity and localization.

CUSABIO got the DNA sequence of the phospho-NFE2L2 (S40) monoclonal antibody that was produced from the splenocytes generated by the phosphopeptide corresponding to human NFE2L2 (phospho S40) immunization. The DNA sequence was cloned into the plasmid and then transfected the into cell lines for in vitro expression. The product is the phospho-NFE2L2 (S40) recombinant monoclonal antibody. It is a rabbit IgG antibody purified using the affinity-chromatography method. This phospho-NFE2L2 (S40)antibody is recommended for WB, IHC, and IF applications and detects the human NFE2L2 phosphorylated at Ser 40 residue.

NFE2L2 is a transcription factor that regulates the physiological response to ROS and oxidative stress. PKC phosphorylates NFE2L2 at Ser40 in response to oxidative stress. Phosphorylated NFE2L2 at Ser40 has been shown to assist its liberation from the cytoplasmic anchor KEAP1 and trigger nuclear translocation. The phosphorylation of NFE2L2 at Ser40 by PKC is a crucial signaling event that leads to a cellular antioxidant response mediated by the antioxidant response element (ARE).