Utilizing in vitro expression systems, the SDCBP recombinant monoclonal antibody is generated by cloning the DNA sequences of SDCBP antibodies from immunoreactive rabbits. The immunogen utilized in this process is a synthesized peptide originating from the human SDCBP protein. Subsequently, the genes encoding the SDCBP antibodies are incorporated into plasmid vectors, and these recombinant plasmid vectors are introduced into host cells to facilitate the expression of the antibody. Once expressed, the SDCBP recombinant monoclonal antibody undergoes purification through affinity chromatography. It is then subjected to extensive testing in ELISA, WB, IF, and FC applications, conclusively demonstrating reactivity with the human SDCBP protein.

SDCBP is a versatile protein involved in cell adhesion, signaling, intracellular trafficking, and cytoskeleton regulation. SDCBP's interactions with syndecan receptors and other binding partners allow it to participate in a wide range of cellular processes, with implications for normal physiological functions and pathological conditions, including cancer and immune responses.

CD146 antibody CSB-RA013563A0HU is a recombinant monoclonal antibody produced from the expression of the plasmids that were integrated by the CD146 monoclonal antibody DNA sequence in cell lines. The CD146 monoclonal antibody was generated from splenocytes isolated from the animals that were immunized with the human CD146synthesized peptide. The CD146 recombinant antibody is a rabbit IgG antibody. It underwent purification using the affinity-chromatography method. It can detect the CD146 protein from human samples. And it is suitable for multiple scientific applications, including ELISA, WB, IHC, IF, and FC analyses.

CD146, also called MCAM, is a cell surface receptor for a variety of ligands, including certain growth factors and extracellular matrixes, as well as an adhesion molecule. CD146 is involved in a variety of physiological and pathological cell functions through bidirectional interactions with its ligands. CD146 overexpression has been detected in the majority of malignancies and has been linked to cancer development and progression.

The production of the mono-methyl-Histone H3.1 (R17) recombinant monoclonal antibody is a stepwise procedure that begins with the cloning of genes encoding the HIST1H3A antibody, which includes both the heavy and light chains. These cloned genes are then inserted into expression vectors designed for optimal performance. Following this, the modified expression vectors are introduced into host cells through transfection, where the host cells undertake the task of producing and secreting the antibody. The purified antibody is obtained through affinity chromatography to ensure its purity and functionality. To guarantee its effectiveness, the antibody undergoes a series of rigorous tests across diverse applications, such as ELISA, WB, ICC, and IF, tailored for the precise detection of the human HIST1H3A protein mono-methylated at R17.

Mono-methylation of Histone H3.1 at arginine 17 (R17) is involved in transcriptional regulation, chromatin structure, DNA repair, cellular identity, and epigenetic signaling, and has implications in various diseases.

The development of the acetyl-Histone H3.1 (K14) recombinant monoclonal antibody begins with the cloning of genes responsible for encoding the HIST1H3A antibody, encompassing both heavy and light chains. These cloned genes are then inserted into an expression vector, which is subsequently introduced into host cells through transfection. The host cells are cultured to produce and secrete the antibody. Following this, the antibody undergoes purification using affinity chromatography to ensure its purity and effectiveness. Rigorous testing then confirms its functionality in various applications, including ELISA, WB, ICC, and IF, allowing for precise detection of the human and rat
HIST1H3A proteins acetylated at K14.

Acetylation of histone H3.1 at lysine 14 (K14) primarily functions in transcriptional activation, chromatin accessibility, cellular identity, epigenetic memory, and coordinated gene regulation, and has implications in various diseases.

Producing the acetyl-histone H4 (K16) recombinant monoclonal antibody is a methodical process that commences with the cloning of genes encoding the HIST1H4A antibody, covering both heavy and light chains. These cloned genes are integrated into expression vectors, which are introduced into host cells through transfection. Subsequently, the host cells are entrusted with antibody production and secretion in a suitable medium. The purified antibody, obtained through affinity chromatography, undergoes comprehensive testing to assess its functionality across diverse applications such as ELISA, WB, ICC, IF, and FC, all tailored for detecting the human and mouse HIST1H4A proteins acetylated at K16.

Histone H4 is a core histone involved in chromatin structure and gene regulation. Acetylation of histone H4 at lysine 16 (H4K16) primarily functions in chromatin decondensation, transcriptional activation, DNA repair, epigenetic signaling, cellular memory, and coordinated gene regulation.

To create the phospho-histone H3.1 (S1) recombinant monoclonal antibody, genes encoding the HIST1H3A antibody are first cloned, encompassing both heavy and light chains. These cloned genes are then inserted into expression vectors, which are introduced into host cells via transfection. The host cells are responsible for the production and secretion of the antibody. Affinity chromatography is employed to ensure the antibody's purity, after which it undergoes rigorous functionality testing in various applications, including ELISA, WB, ICC, and IF, enabling accurate detection of the human HIST1H3A protein phosphorylated at S1.

Phosphorylation at H3.1 S1 can promote chromatin condensation thus leading to gene repression. During mitosis, histone H3.1 S1 phosphorylation plays a role in chromosome condensation and segregation. It helps ensure accurate cell division by regulating chromosomal architecture. Phosphorylated H3.1 S1 is also associated with DNA damage response and repair processes. H3.1 S1 phosphorylation is also linked to cell cycle regulation, epigenetic signaling, and coordinated gene regulation.

The production of the acetyl-Histone H4 (K5) recombinant monoclonal antibody commences with the cloning of genes encoding the HIST1H4A antibody, which includes both heavy and light chains. These cloned genes are integrated into expression vectors, which are subsequently transfected into host cells. The host cells are cultured for antibody production and secretion. The purified antibody is achieved through affinity chromatography, guaranteeing its purity and efficacy. It is further subjected to comprehensive testing across various applications, including ELISA, WB, ICC, and IF, enabling precise detection of the human HIST1H4A protein acetylated at K5.

Acetylation at H4K5 promotes chromatin decondensation and is primarily associated with transcriptional activation. H4K5 acetylation is involved in DNA repair processes. H4K5 acetylation often occurs in conjunction with other histone modifications, forming a complex regulatory code that fine-tunes gene expression.

The synthesized DNA sequence corresponding to the phospho-Histone H2AX (S139) monoclonal antibody was cloned into the plasmid and then transfected into the cell line for expression. The monoclonal antibody against phospho-Histone H2AX (S139) was generated from the animals immunized by phospho-peptide containing human Histone H2AX S139 site. The product was purified through the affinity-chromatography method and obtained the phospho-Histone H2AX (S139) recombinant monoclonal antibody. This phospho-Histone H2AX (S139) recombinant antibody is a rabbit IgG and has been tested in scientific applications, including ELISA, WB, and IHC. It only recognizes phosphorylated serine 139 of human H2AX.

The S139 phosphorylated H2AX, also termed γH2AX, is a sensitive marker for DNA double-strand breaks (DSBs) and is responsible for the recruitment of cell cycle checkpoint and DNA repair factors to the damaged site.

Anti-phospho-Histone H1.4 (T17) antibody is a recombinant monoclonal antibody that recognizes the human Histone H1.4 phosphorylated at Thr17 residue. This phospho-Histone H1.4 (T17) antibody was drawn and isolated from the tissue culture supernatant (TCS) that cultivates the cell lines containing vectors of the human phospho-Histone H1.4 (T17) monoclonal antibody gene. It underwent affinity-chromatography purification. It is a rabbit IgG. And it can be used for ELISA, IHC, and IF testing with human samples.

The higher-order chromatin structure is maintained and established partially by the linker histone H1. H1.4, one of the 11 human H1 isoforms, is one of the most widely expressed somatic H1 variations, with significant levels of expression in many cells. Phosphorylation of H1 has been recognized as its most prominent modification. The antibodies against phospho-Histone H1.4 (T17) are helpful in the detection and localization of histone H1.4 phosphorylated at Thr17.

Creating the acetyl-Histone H2A type 1-B/E (K9) recombinant monoclonal antibody involves cloning the genes encoding the HIST1H2AB antibody, including both heavy and light chains. These cloned genes are inserted into expression vectors, which are then introduced into host cells through transfection. The host cells take on the responsibility of producing and secreting the antibody. The antibody is subsequently purified through affinity chromatography to ensure its purity and effectiveness. Rigorous functionality testing in applications like ELISA, ICC, and IF confirms its suitability for the precise detection of the human HIST1H2AB protein acetylated at K9.

H2A type 1-B/E K9 acetylation is primarily associated with transcriptional activation. It helps recruit transcriptional activators, coactivators, and chromatin remodeling complexes to gene promoters. This enhances the initiation and progression of transcription, leading to increased gene expression. Acetylation of H2A type 1-B/E at K9 is involved in DNA repair, epigenetic signaling, and coordinated gene regulation.