CUSABIO cloned the DNA sequence encoding the phospho-EIF2AK2 (T446) monoclonal antibody into the plasmid and then transfected into the cell line for expression. The product is the recombinant phospho-EIF2AK2 (T446) monoclonal antibody. It belongs to the rabbit IgG and is purified through the affinity-chromatography method. This EIF2AK2-pT446 antibody has been quality tested in ELISA, WB, IHC, and IF. It can recognize the human EIF2AK2 phosphorylated at Thr446 residue.

EIF2AK2, also known as PKR, plays an important role in the antiviral defense and cellular homeostasis by modulating mRNA translation. It detects dsRNA molecules produced during DNA and RNA virus replication and mounts a powerful antiviral response by inhibiting viral mRNA translation, causing infected cells to die. PKR is activated by the homodimerization and subsequent autophosphorylation on Thr446 and Thr451 after binding dsRNA.

The synthesized DNA sequence corresponding to the phospho-IRF3 (S386) 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 p-S386-IRF3 recombinant monoclonal antibody. This anti-IRF3-pS386 recombinant antibody is a rabbit IgG and has been tested in ELISA and WB. It only targets the human IRF3 phosphorylated at Ser 386 residue.

IRF3 plays an important role in the innate immune defense against viral infection. Phosphorylation of IRF3's 7 C-terminal Ser/Thr residues, including Ser385, Ser386, Ser 396, Ser 398, Ser 402, Ser 405, and Thr 404, occurs when the host cell is infected. This phosphorylation causes IRF3 to form a complex with the coactivators CREB-binding protein (CBP)/p300, activating target genes in the nucleus. Autoinhibition is reduced when these 7 Ser/Thr residues are phosphorylated. Phosphorylation of Ser 386 was demonstrated to be essential for IRF3 activation since mutation of this residue abrogated all IRF3 activation.

Phospho-HSF1 (S326) antibody CSB-RA010791A326phHU is a recombinant monoclonal antibody belonging to rabbit IgG. Its production procedures include: the acquisition of the phospho-HSF1 (S326) monoclonal antibody using the phosphopeptide corresponding to human EIF2S1 (phospho S326) immunizes animals; the determination of DNA sequence of the phospho-HSF1 (S326) monoclonal antibody; the clone of the DNA sequence into the plsamid and subsequent transfection into cell lines for expression. This phospho-HSF1 (S326) antibody underwent purification using affinity chromatography. It has been tested in multiple applications, including ELISA, WB, and IHC. It specifically targets the human HSF1 phosphorylated at Ser 326 residue.

HSF1 orchestrates a complex transcriptional mechanism that aids adaptability and survival in stressful situations. It keeps track of the structural integrity of the proteome. Stresses such as thermal shock, hypoxia, heavy metals, reactive oxygen species, and pH shifts stimulate the activation of HSF1. HSF1 is involved in the initiation of tumors as well as the promotion and maintenance of cancer cell proliferation. Phosphorylation of S326 by AKT1, mTOR, p38, and MEK1 is a key regulator of HSF1 transcriptional activity.

The DNA sequence coding for the CD21 monoclonal antibody developed from animals immunized with a human CD21 synthetic peptide was cloned into an expression vector and then transfected into a cell line for in vitro expression. The recombinant CD21 monoclonal antibody was obtained through affinity chromatography purification of the product from the tissue culture supernatant (TCS). The human CD21 is especially targeted by this CD21 antibody. It's a rabbit IgG antibody. This CD21 antibody has been evaluated using ELISA, WB, IHC, IF, and FC methods.

CD21, also termed CR2, binds to a number of endogenous ligands, including the complement component C3 fragments iC3b, C3dg, and C3d, the low-affinity IgE receptor CD23, and interferon-alpha. By binding to C3d, which is covalently linked to targets, CR2 connects the innate complement-mediated immune response to pathogens and foreign antigens with the adaptive immune response, leading to a cell signaling event that lowers the threshold for B cell activation. A range of autoimmune and inflammatory disorders are linked to mutations or deletions of the CR2 gene in humans and the CR2 gene in mice.

To manufacture the phospho-RPS6KA1 (S380) recombinant monoclonal antibody, the journey begins with the retrieval of genes responsible for encoding this antibody from rabbits that have previously undergone immunization with a synthesized peptide originating from the human RPS6KA1 protein phosphorylated at S380. Subsequently, these antibody genes are seamlessly 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 growth phase, the phospho-RPS6KA1 (S380) recombinant monoclonal antibody undergoes a meticulous purification process using affinity chromatography techniques, effectively isolating the antibody from the surrounding cell culture supernatant. Lastly, the functionality of the antibody is rigorously assessed through a battery of tests, including ELISA, WB, and IP, conclusively affirming its ability to effectively react with the human RPS6KA1 protein phosphorylated at S380.

Phosphorylation of RPS6KA1 at S380 is a crucial regulatory mechanism that allows cells to respond to extracellular signals and stressors, modulating gene expression and influencing various cellular processes, including cell growth and stress responses. Dysregulation of this phosphorylation event can have significant implications in diseases and conditions related to cell proliferation and gene expression.

Phospho-ERN1 (S724) recombinant monoclonal antibody was prepared by cloning the coding sequence for the phospho-ERN1 (S724) monoclonal antibody (produced by immunizing animals with the synthetic phosphopeptide of ERN1) into the plasmids and transfecting the clones into cell lines. It is a rabbit IgG purified through the affinity-chromatography method. This phospho-ERN1 (S724) antibody detects endogenous levels of human ERN1 only when phosphorylated at Ser724. It can be applied in ELISA, WB, and IF analyses.

Phosphorylation at Ser724 residue of the ERN1 protein can regulate its transcriptional and enzymatic activities. Phospho-ERN1 (S724) antibodies are used to analyze ERN1 Ser724 phosphorylation, which is a highly conserved site within the kinase activation domain.

In the quest to produce the histone H3.1 recombinant monoclonal antibody, the initial phase involves the extraction of genes encoding the HIST1H3A antibody from rabbits that have been previously exposed to a synthesized peptide derived from the human HIST1H3A protein. These HIST1H3A antibody genes are then seamlessly integrated into specialized expression vectors. Following this genetic modification, the modified vectors are introduced into host suspension cells, which are carefully cultured to stimulate the expression and secretion of antibodies. Subsequently, the Histone H3.1 recombinant monoclonal antibody is subjected to a meticulous purification process utilizing affinity chromatography techniques, effectively isolating the antibody from the surrounding cell culture supernatant. Finally, the functionality of the antibody is comprehensively assessed through a diverse range of assays, including ELISA, WB, IHC, IF, and FC tests, unequivocally confirming its ability to interact effectively with the human histone H3.1.

Histone H3.1, a variant of the histone H3 protein family, along with other histone variants and post-translational modifications, plays a fundamental role in shaping the epigenetic landscape of the genome, influencing gene expression, and maintaining genomic integrity. Its dynamic interactions with DNA and various proteins are critical for the proper functioning of the cell.

Anti-phospho-RPS6KA1 (T359+S363) antibody is a recombinant monoclonal antibody that recognizes the human RPS6KA1 phosphorylated at Thr359 and Ser363 residues. This phospho-RPS6KA1 (T359+S363) antibody was drawn and isolated from the tissue culture supernatant (TCS) that cultivates the cell lines containing vectors of the human phospho-RPS6KA1 (T359+S363) monoclonal antibody gene. It underwent affinity-chromatography purification. It is a rabbit IgG. And it can be used for ELISA, WB, IF, and IP testing with human samples.

RPS6KA1 (RSK1) is a growth-factor regulated serine⁄threonine kinase that is involved in the MAPK and PI3K signaling pathways. The C-terminal kinase domain of RPS6KA1 is involved in autophosphorylation, whereas the N-terminal kinase domain is responsible for the phosphorylation of all exogenous substrates. It controls cellular proliferation and differentiation by phosphorylating transcription factors, signaling kinases, and proapoptotic proteins.

The phospho-TP53 (T55) monoclonal antibody's DNA sequence was inserted into the plasmid, which was subsequently transfected into the cell line for expression. The phospho-TP53 (T55) recombinant monoclonal antibody was produced after purification using affinity chromatography. This rabbit IgG phospho-TP53 (T55) recombinant antibody has been evaluated in scientific applications such as ELISA, WB, and IF. The T55 phospho-specific antibody exclusively reacts with phosphorylated human TP53 at Thr 55.

The tumor suppressor P53 is a transcriptional factor involved in the modulation of cell growth, cell cycle, apoptosis, and senescence. TP53 is tightly regulated by posttranslational modifications. Phosphorylation of TP53 plays an important role in the cellular response to various stresses. Phosphorylation of multiple sites in the inherently disordered N-terminal transactivation domain activates TP53 after DNA damage. During various stages of the cellular DNA damage response, the phosphorylation status of Thr55 regulates both the activation and termination of p53-mediated transcriptional programs.

Anti-phospho-GYS1 (S641) antibody is a recombinant monoclonal antibody that recognizes the human GYS1 phosphorylated at Ser 641 residue. This phospho-GYS1 (S641) antibody was drawn and isolated from the tissue culture supernatant (TCS) that cultivates the cell lines containing vectors of the human phospho-GYS1 (S641) monoclonal antibody gene. It underwent affinity-chromatography purification. It is a rabbit IgG. This phospho-specific recombinant antibody can be used for ELISA, WB, and IF testing with human samples.

GYS1 catalyzes the conversion of glucose to glycogen and is activated by allostery and dephosphorylation, respectively. GYS1 activity is inhibited by phosphorylation via glycogen synthase kinase 3, AMPK, PKA, and casein kinase 2. The dephosphorylation of specific Ser/Thr residues enhances GYS1 activity.