CUSABIO got the DNA sequence of the histone H2B type 1-K monoclonal antibody that was produced from the splenocytes derived from animals with the human histone H2B type 1-K synthesized peptide immunization. The DNA sequence was cloned into the plasmid and then transfected into cell lines for in vitro expression. The product is the histone H2B type 1-K recombinant monoclonal antibody. It is a rabbit IgG antibody purified using the affinity-chromatography method. This histone H2B type 1-K antibody is recommended for ELISA, WB, and IHC applications and detects the histone H2B type 1-K protein from human sources.

A study by Shih-Yi Lin et al. has reported that Alpha 1-Antitrypsin and H2B1K are diagnostic and prognostic biomarkers for urothelial carcinoma after proteome profiling of urinary exosomes. H2B1K has been demonstrated to have prognostic significance, as 3-fold increases in its levels properly predicted recurrence.

The DNA coding for the human monoclonal antibody against synthetic phosphopeptide of RB1 (S807) was integrated into the plasmid and then transfected into the cell line for in vitro expression. After purification from the tissue culture supernatant (TCS) through affinity-chromatography, the product recombinant monoclonal phospho-RB1 (S807) antibody was isolated. This phospho-RB1 Ser807 antibody detects endogenous RB1 protein only when phosphorylated at Serine 807. It is a rabbit IgG and is reactive with human samples. And it is suitable for ELISA and IF analyses.

RB1 gene is the first isolated tumor suppressor gene in human. It is a negative regulator of the cell cycle and regulates the expression of genes required for cell proliferation and differentiation by binding with transcription factor E2F1, thus maintaining the balance of cell growth and development. Therefore, the function of the RB1 gene is related to the cell cycle, cell senescence, cell apoptosis, cell differentiation, and growth inhibition. In general, Rb1 phosphorylation is required to release transcriptional target inhibition and promote cell cycle progression.

The phospho-MYB (S11) recombinant monoclonal antibody is a highly specific antibody against the phosphorylated human MYB at Ser 11. This phospho-MYB (S11) antibody was expressed by transfecting the human phospho-MYB (S11) 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-MYB (S11) antibody can be used in ELISA and IF applications.

Phosphorylation of c-Myb has been linked to the modulation of c-Myb/DNA binding. Ramsay et al. found that constitutive phosphorylation by CK2 at serines 11 and 12 is required for full-length c-Myb to have high-affinity specific DNA binding activity in vitro. CK2 phosphorylation of c-Myb at serines 11 and 12 lowers the effectiveness of c-Myb DNA binding to low-affinity sites, according to Luscher et al.

The production of the mono-methyl-histone H3.1 (K36) recombinant monoclonal antibody comprises the cloning of genes responsible for encoding the HIST1H3A antibody and their subsequent expression within mammalian cell expression systems. This process involves the cloning of both heavy and light chain genes of the HIST1H3A antibody into expression vectors, which are later introduced into host cells through transfection. Subsequently, the host cells take on the role of producing and secreting the antibodies. Following production, the antibody undergoes purification using affinity chromatography techniques. The final antibody product is rigorously tested for functionality across a range of applications, including ELISA, WB, ICC, and IF, specifically designed for the accurate detection of the human HIST1H3A protein mono-methylated at K36.

Mono-methylation of HIST1H3A at lysine 36 (K36) primarily functions in transcriptional repression and chromatin compaction, with roles in alternative splicing, DNA repair, cellular identity, epigenetic memory, and implications in disease. It is a crucial epigenetic modification that helps regulate gene expression and chromatin structure.

The production of the tri-methyl-histone H4 (K20) recombinant monoclonal antibody starts with the isolation of genes responsible for encoding the HIST1H4A antibody from rabbits previously immunized with a synthesized peptide derived from the human HIST1H4A protein tri-methylated at K20. These antibody genes are then meticulously cloned 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. After this cultivation phase, the tri-methyl-histone H4 (K20) recombinant monoclonal antibody is subjected to a rigorous purification process utilizing 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, WB, and ICC tests, conclusively confirming its ability to interact effectively with the human HIST1H4A protein tri-methylated at K20.

Tri-methylation of HIST1H4A at K20 is an epigenetic modification associated with gene repression and the formation of repressive chromatin structures, such as heterochromatin and silenced gene loci. It plays a vital role in regulating gene expression, maintaining chromatin integrity, and contributing to genome stability.

In the quest to produce the acetyl-histone H3.1 (K4) 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 acetylated at K4. These 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 HIST1H3A 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, ICC, and IF tests, unequivocally confirming its ability to interact effectively with the human HIST1H3A protein acetylated at K4.

Acetylation of HIST1H3A at K4 is a key epigenetic modification that promotes an open chromatin structure and activates gene expression. It plays a central role in transcriptional regulation, cellular differentiation, and the maintenance of gene expression patterns across generations of cells. Dysregulation of this modification can have significant implications for health and disease.

The DNA sequence of the phospho-EIF4E (S209) monoclonal antibody was obtained by CUSABIO from splenocytes isolated from animals with human EIF4E phosphopeptide (S209) immunization. The DNA sequence was cloned into the plasmid and then transfected into cell lines for in vitro expression. The product is the phospho-EIF4E (S209) recombinant monoclonal antibody. It's an affinity-chromatography purified rabbit IgG antibody. This phospho-EIF4E (S209) antibody detects the phospho-EIF4E (S209) protein from human sources in ELISA, WB, and IHC applications.

EIF4E plays an essential role in the efficient translation of the vast majority of capped cellular mRNAs. It functions as a nucleation location for the construction of the 48S preinitiation complex by binding to the 5'-methylated guanosine cap of mRNA. EIF4E is overexpressed in numerous epithelial tumors and regulates the translation of multiple malignancy-associated mRNAs. Phosphorylation of EIF4E at serine 209 has been linked to tumor growth and decreased survival in malignant melanoma, according to Julia H Carter et al.

CUSABIO put the phospho-GATA3 (S308) monoclonal antibody DNA sequence into the plasmid, which was subsequently transfected into the cell line for expression. Immunizing mice with the synthetic phospho-peptide corresponding to residues surrounding Ser 308 of human GATA3 produced the phospho-GATA3 (S308) monoclonal antibody. The recombinant phospho-GATA3 (S308) monoclonal antibody was obtained after the product was purified using affinity chromatography. It's a rabbit IgG antibody. This phospho-GATA3 (S308) antibody has undergone ELISA, WB, and IHC quality testings. It is reactive with human samples. This anti-pSer308-GATA3 antibody may be used to address the functional role of GATA3 phosphorylation.

GATA3 is mostly expressed in T lymphocytes and is essential for both early thymic T-cell development and functional differentiation of naive CD4 T cells into Th2 cells. GATA3, a T-cell transcription factor, has been found to influence Th2 T-cell development in a number of investigations. It also plays a role in mammary gland development and the preservation of luminal epithelial cells' differentiated state. Posttranslational modifications, the proteasome pathway, and phosphorylation all can regulate GATA3 activity. In ER-positive breast cancer cells, phosphorylation of GATA3 at Ser308 has previously been utilized as a marker of proteasomal turnover.

CUSABIO engineered a vector by inserting a sequence encoding the phospho-MYC (T58+S62) monoclonal antibody and then transfected this vector into the cell line for in vitro expression. The monoclonal antibody was generated from immunized animals with the synthesized peptide derived from phosphorylated human MYC at Thr 58 and Ser 62 residues. The collected tissue culture supernatant (TCS) underwent affinity-chromatography purification to get the recombinant phospho-MYC (T58+S62) monoclonal antibody. This anti-phospho-MYC (T58+S62) antibody is a rabbit IgG. It is suitable for the detection of the human phospho-MYC (T58+S62) in ELISA and WB.

The c-Myc oncoprotein is a pleiotropic transcription factor that regulates a variety of cellular processes, including cell proliferation, cell growth, and cell differentiation, as well as genome stability and cell death pathways. Most human cancers constitutively highly express c-Myc, and high c-Myc expression in animal models can induce carcinogenesis. Conserved Thr 58 and Ser 62 phosphorylation sites that help regulate c-Myc protein stability affect c-Myc expression, and altered ratios of Thr 58 and Ser 62 phosphorylation have been reported in human cancer.

The recombinant RPS6KB1 antibody expression is induced in mammalian cells transfected with a recombinant plasma vector. The recombinant plasma vector was constructed by inserting the gene coding for the antibody against RPS6KB1 into the plasma. The recombinant RPS6KB1 antibody was purified from the cell culture medium using affinity-chromatography. It can react with samples containing RPS6KB1 protein from Human and has been validated for use in the ELISA, WB, IF, IP.

The T421/S424 phospho-RPS6KB1 antibody can detect the RPS6KB1 protein phosphorylated at T421/S424 sites. RPS6KB1, also known as S6K1 or p70S6K, is a serine/threonine kinase of ribosomal protein and is essential for protein translation and elongation. It is involved in the PI3K/mTOR signaling pathway. Growth factors and hormones can activate RPS6KB1 by phosphorylating its numerous serine and threonine sites in a sequential manner. Active RPS6KB1 phosphorylates ribosomal protein S6, leading to selective translation of the 5'-terminal oligopyrimidine tract mRNAs that code for ribosomal proteins and elongation factors.