The mono-methyl-histone H3.1 (R128) recombinant monoclonal antibody production process initiates with the cloning of genes responsible for encoding the HIST1H3A antibody, covering both heavy and light chains. These cloned genes are integrated into expression vectors, which are introduced into host cells via transfection. The host cells assume the task of producing and secreting the antibody. After purification through affinity chromatography to guarantee its purity, the antibody undergoes comprehensive functionality testing in ELISA and WB applications, ensuring accurate detection of the human and mouse HIST1H3A proteins mono-methylated at R128.

Histone H3.1 mono-methylation at arginine 128 (R128) may promote transcriptional activation or repression depending on the context and the specific proteins involved. H3.1 R128 mono-methylation can serve as an epigenetic signal, indicating specific chromatin states and influencing cellular processes such as differentiation, development, and cellular identity.

The development of the hydroxyl-histone H2A type 1-B/E (Y39) recombinant monoclonal antibody starts with the cloning of genes encoding the HIST1H2AB antibody, comprising both heavy and light chains. These cloned genes are inserted into expression vectors, which are then transfected into host cells. The host cells are responsible for the production and secretion of the antibody. Following purification through affinity chromatography to ensure its purity, the antibody undergoes rigorous functionality testing across ELISA and WB applications, enabling precise detection of the human histone H2A type 1-B/E protein hydroxylated at Y39.

The generation of the mono-methyl-Histone H4 (K16) recombinant monoclonal antibody entails a multi-step process that initiates with the cloning of the genes responsible for encoding the HIST1H4A antibody. These genes, encompassing both the heavy and light chains, are integrated into expression vectors designed for optimal performance. The next phase involves the introduction of the expression vectors into host cells through transfection, where the host cells are subsequently tasked with the production and secretion of the antibody. To ensure its purity and efficacy, the antibody then undergoes a meticulous purification procedure utilizing affinity chromatography. Once purified, the antibody is put through ELISA and IF tests, ultimately enabling precise and reliable detection of the human and rat HIST1H4A proteins mono-methylated at K16.

Mono-methylation of HIST1H4A at K16 primarily functions in chromatin compaction, transcriptional repression, DNA repair, cellular identity, long-range chromatin interactions, and epigenetic memory, and has implications in various diseases. It is a crucial epigenetic modification that helps regulate gene expression and chromatin structure.

The mono-methyl-histone H3.1 (R2) recombinant monoclonal antibody production involves cloning genes encoding for the HIST1H3A antibody and expressing them in mammalian cell expression systems. The genes encoding the heavy and light chains of the HIST1H3A antibody are cloned into expression vectors, which are then introduced into host cells via transfection. The host cells then produce and secrete the antibodies, which can be purified through affinity chromatography. The resulting antibody has been tested for functionality in ELISA, WB, ICC, and IF applications for the detection of human HIST1H3A protein mono-methylated at R2.

Mono-methylation of HIST1H3A at arginine 2 (R2) is an epigenetic modification that can influence gene expression and chromatin structure, particularly promoting gene activation and accessibility. Its dynamic regulation is crucial for maintaining cellular identity and responding to environmental cues, with potential implications in various diseases.

In the development of the mono-methyl-histone H3.1 (K18) recombinant monoclonal antibody, the initial phase comprises the retrieval of genes responsible for coding the HIST1H3A antibody. These genes are acquired from rabbits that have been previously exposed to a synthesized peptide derived from the human HIST1H3A protein mono-methylated at K18. 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 mono-methyl-histone H3.1 (K18) 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, ICC, and IF tests, unequivocally confirming its capacity to interact with the human HIST1H3A protein mono-methylated at K18.

The recombinant monoclonal antibody against histone H2A type 1-B/E was prepared by transfecting the vector containing the DNA for the histone H2A type 1-B/Emonoclonal antibody into the cell lines for in vitro production. The product was purified using affinity chromatography to obtain the histone H2A type 1-B/E recombinant antibody. This antibody is a rabbit IgG and recognizes human histone H2A type 1-B/E. It has been tested and approved for use in ELISA, WB, and IF.

Histone proteins are required for the shift between active and inactive chromatin states, both structurally and functionally. Histones have evolved to play a variety of roles in gene regulation and epigenetic silencing, despite their high conservation due to restrictions to maintain the overall shape of the nucleosomal octameric core. DMA replication, transcription, repair, and recombination are influenced by histone variations, post-translational modifications, and interactions with chromatin remodeling complexes.

CUSABIO cloned the DNA sequence encoding the CD31 monoclonal antibody into the plasmid and then transfected into the cell line for expression. The product was purified through the affinity-chromatography method and then got the recombinant CD31 monoclonal antibody. It belongs to the rabbit IgG. This CD31 antibody is recommended to detect human CD31 protein in ELISA, WB, IHC, and FC applications.

CD31, also known as PECAM1, plays a crucial role in endothelial cell tight junctions, leukocyte trafficking, and immunological response through its homophilic and heterophilic binding patterns. It also has a role in vasculogenesis and angiogenesis, as well as being a key mediator of transendothelial migration (TEM).

In the development of the acetyl-histone H3.1 (K56) recombinant monoclonal antibody, the initial phase comprises the retrieval of genes responsible for coding the HIST1H3A antibody. These genes are acquired from rabbits that have been previously exposed to a synthesized peptide derived from the human HIST1H3A protein acetylated at K56. 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 acetyl-histone H3.1 (K56) 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, ICC, and IF tests, unequivocally confirming its capacity to interact with the human HIST1H3A protein acetylated at K56.

Acetylation of HIST1H3A at K56 is a critical histone modification that generally promotes an open chromatin structure and facilitates gene activation. It plays a significant role in regulating gene expression, DNA repair, and epigenetic inheritance, contributing to various cellular processes and maintaining genome integrity. Dysregulation of K56 acetylation can have important implications for diseases and developmental processes.

The acetyl-Histone H2B type 1-B/HIST1H2BB (K20) recombinant monoclonal antibody is a highly specific antibody against the acetylated HIST1H2BB at K20 from human and mouse sources. This acetyl-HIST1H2BB (K20) antibody was expressed by transfecting the human acetyl-HIST1H2BB (K20)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 acetyl-HIST1H2BB (K20) antibody can be used in ELISA, WB, ICC, IF, and FC applications.

HIST1H2BB is a subtype of histone core component H2B. Antibodies against the HIST1H2BB are useful for the localization and detection of the HIST1H2BB of acetylation at Lys20 residue.

To manufacture the di-methyl-histone H3.1 (K9) recombinant monoclonal antibody, the journey begins with the retrieval of genes responsible for encoding the HIST1H3A antibody from rabbits that have previously undergone immunization with a synthesized peptide originating from the human HIST1H3A protein di-methylated at K9. 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 di-methyl-histone H3.1 (K9) 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 IF, conclusively affirming its ability to effectively react with the human HIST1H3A protein di-methylated at K9.

Di-methylated K9 HIST1H3A is also found at centromeres, which are essential for proper chromosome segregation during cell division. When HIST1H3A is di-methylated at K9, it contributes to the repression of gene transcription. This modification creates a repressive chromatin environment by preventing the binding of transcription factors and other regulatory proteins to the DNA.