Other Proteins

PROS1, also known as protein S, is a vitamin K-dependent protein that plays a crucial role in the regulation of blood coagulation. It functions as a cofactor for protein C, another key player in the coagulation cascade. PROS1 acts as an anticoagulant by inhibiting the activity of certain clotting factors and promoting the breakdown of blood clots. It helps maintain the balance between clotting and anticoagulation, preventing the formation of excessive blood clots that can lead to thrombosis.

Please note this product may be subject to fees, we invite you to contact your local office. Recombinant human TL1A (TNF-like ligand 1A (also known as Vascular endothelial growth inhibitor, VEGI or TNFSF15), encompassing amino acids 72 to 251(end). This construct contains an N-terminal His-tag (6xHis) followed by an Avi-Tag™. This protein was affinity purified. The protein runs as two bands in SDS-PAGE due to variable glycosylation, as confirmed by PNGase treatment.

Please note this product may be subject to fees, we invite you to contact your local office. Recombinant human TL1A (TNF-like ligand 1A (also known as Vascular endothelial growth inhibitor, VEGI or TNFSF15), encompassing amino acids 72 to 251(end). This construct contains an N-terminal His-tag (6xHis) followed by an Avi-Tag™. This protein was affinity purified. The protein runs as two bands in SDS-PAGE due to variable glycosylation, as confirmed by PNGase treatment.

Products in EpiCypher’s IDEA Toolbox (Innovation and Discovery of Epigenetic Applications) offer access to reagents without known or fully defined uses, enabling researchers to explore cutting-edge applications. Due to their novelty and unexplored potential, EpiCypher will engage in limited technical support. CUTANA™ Uncharged 6xHis-pAG-Tn5 is a fusion of proteins A and G to E.coli transposase (Tn5), the key enzyme for CUT&Tag [1]. The fusion protein contains a polyhistidine tag (6xHis) to enable applications that require affinity purification steps (for an untagged version of uncharged pAG-Tn5, see EpiCypher 15-1025). Uncharged Tn5 must be loaded with user-designed mosaic adapter DNA prior to use in CUT&Tag (see reference [1] and Application Notes). His-pAG-Tn5 enables purification of differentially barcoded antibody-Tn5 complexes such as those described in MulTI-Tag (Multiple Target Identification by Tagmentation) and multi-CUT&Tag workflows to simultaneously interrogate multiple ch

Histone phosphorylation is a post-translational modification (PTM) wherein a phosphate group is added to a histone protein, predominantly occurring on serine, threonine, and tyrosine residues. In combination with other PTMs, histone phosphorylation constitutes the “histone code,” acting as a language read by proteins to regulate chromatin structure and gene expression. Histone phosphorylation is involved in chromatin remodeling and compaction associated with diverse cellular processes, including DNA damage repair, transcription regulation, cell division, and apoptosis [1]. Recombinant mononucleosomes containing phosphorylated histones can be used to study the biological functions of histone phosphorylation. H3T3phos (histone H3 threonine 3 phosphorylation) Recombinant Nucleosome, Biotinylated consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3.2, and H4) to form a nucleosome, the basic repeating unit of chromatin. The 147 bp

Histone phosphorylation is a post-translational modification (PTM) wherein a phosphate group is added to a histone protein, predominantly occurring on serine, threonine, and tyrosine residues. In combination with other PTMs, histone phosphorylation constitutes the “histone code,” acting as a language read by proteins to regulate chromatin structure and gene expression. Histone phosphorylation is involved in chromatin remodeling and compaction associated with diverse cellular processes, including DNA damage repair, transcription regulation, cell division, and apoptosis [1]. Recombinant mononucleosomes containing phosphorylated histones can be used to study the biological functions of histone phosphorylation. H3T6phos (histone H3 threonine 6 phosphorylation) Recombinant Nucleosome, Biotinylated consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3.2, and H4) to form a nucleosome, the basic repeating unit of chromatin. The 147 bp

Histone phosphorylation is a post-translational modification (PTM) wherein a phosphate group is added to a histone protein, predominantly occurring on serine, threonine, and tyrosine residues. In combination with other PTMs, histone phosphorylation constitutes the “histone code,” acting as a language read by proteins to regulate chromatin structure and gene expression. Histone phosphorylation is involved in chromatin remodeling and compaction associated with diverse cellular processes, including DNA damage repair, transcription regulation, cell division, and apoptosis [1]. Recombinant mononucleosomes containing phosphorylated histones can be used to study the biological functions of histone phosphorylation. H3T11phos (histone H3 threonine 11 phosphorylation) Recombinant Nucleosome, Biotinylated consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3.2, and H4) to form a nucleosome, the basic repeating unit of chromatin. The 147 b

Histone phosphorylation is a post-translational modification (PTM) wherein a phosphate group is added to a histone protein, predominantly occurring on serine, threonine, and tyrosine residues. In combination with other PTMs, histone phosphorylation constitutes the “histone code,” acting as a language read by proteins to regulate chromatin structure and gene expression. Histone phosphorylation is involved in chromatin remodeling and compaction associated with diverse cellular processes, including DNA damage repair, transcription regulation, cell division, and apoptosis [1]. Histone phosphorylation is also observed on non-canonical histones, particularly H3.3, where it plays roles in transcriptional regulation. Recombinant mononucleosomes containing phosphorylated histones can be used to study the biological functions of histone phosphorylation. H3.3S31phos,K36me3 (histone H3.3 serine 31 phosphorylation, lysine 36 trimethylation) Recombinant Nucleosome, Biotinylated consists of 147 base

Heterotypic nucleosomes, also referred to as “asymmetric nucleosomes,” contain sister histones with distinct histone variants and/or post-translational modifications (PTMs). In homotypic nucleosomes, or “symmetric nucleosomes,” each pair of sister histones bears the same PTM, set of PTMs, or histone variant. Histone-modifying enzymes, chromatin remodelers, and histone chaperones differentially modify sister histones or exchange unique histone variants to form heterotypic nucleosomes. Heterotypic nucleosomes have been found at promoters of developmental genes in undifferentiated embryonic stem cells and transcription start sites (TSSs) of approximately half of the genes in budding yeast [1]. Heterotypic nucleosomes represent an additional layer of the histone code, acting as substrates for multivalent reader proteins, participating in PTM crosstalk mechanisms, and influencing reader protein binding affinity through varying local target concentration. Recombinant heterotypic nucleosomes