k biotin w histone h2b (108 125) (trifluoroacetate salt)

Histone H2B (108-125) is a peptide fragment of histone H2B that corresponds to amino acid residues 109-126 of the human histone H2B sequence. It contains an N-terminal biotinylated lysine followed by a tryptophan linker. Histone H2B can be modified by addition of an O-linked N-acetylglucosamine (GlcNAc) moiety to the serine residue at position 112, which promotes monoubiquitination of the lysine at position 120.1 Both of these modifications are associated with active transcription. Histone H2B also has lysine residues at positions 108, 116, and 120 that are subject to acetylation.2References1. Fujiki, R., Hashiba, W., Sekine, H., et al. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480(7378), 557-560 (2011).2. Portela, A., and Esteller, M. Epigenetic modifications and human disease. Nat. Biotechnol. 28(10), 1057-1068 (2010). Histone H2B (108-125) is a peptide fragment of histone H2B that corresponds to amino acid residues 109-126 of the human histone H2B sequence. It contains an N-terminal biotinylated lysine followed by a tryptophan linker. Histone H2B can be modified by addition of an O-linked N-acetylglucosamine (GlcNAc) moiety to the serine residue at position 112, which promotes monoubiquitination of the lysine at position 120.1 Both of these modifications are associated with active transcription. Histone H2B also has lysine residues at positions 108, 116, and 120 that are subject to acetylation.2 References1. Fujiki, R., Hashiba, W., Sekine, H., et al. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480(7378), 557-560 (2011).2. Portela, A., and Esteller, M. Epigenetic modifications and human disease. Nat. Biotechnol. 28(10), 1057-1068 (2010).

Cbl-b-IN-2 is an orally active biological compound that inhibits the E3 enzyme Casitas b lineage lymphoma proto-oncogene b (Cbl-b) in the ubiquitin proteasome pathway and can be used in the study of diseases that modulate the immune system and are susceptible to regulation by the immune system. Cbl-b-IN-2 can also be used in cancer research alone or in combination with one or more immune checkpoint inhibitors, antitumour agents and radiopharmaceuticals.

N-(Biotin-PEG4)-N-bis(PEG4-acid) HCl salt is a PEG Linker which may be useful in the development of antibody drug conjugates.

Biotin-PEG3-(CH2)3-NH2 TFA salt is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.

Histone H3 (21-44)-GK-biotin is a peptide fragment of histone H3 that corresponds to amino acid residues 22-45 of the human histone H3.1 and 3.2 sequences and is biotinylated via a C-terminal GK linker. Histone H3 (21-44) contains a lysine residue at position 23 that is subject to acetylation, an arginine at position 26 subject to methylation, and a serine at position 28 subject to phosphorylation, as well as lysine residues at positions 27 and 36 that are subject to methylation and acetylation. Histone H3 (21-44)-GK-biotin has been used as a substrate for the primate-specific histone methyltransferase PR domain-containing protein 7 (PRDM7) to determine substrate specificity.

K-Ras ligand-Linker Conjugate 2 is a chemical compound that includes a ligand for K-Ras and a PROTAC linker, capable of recruiting E3 ligases like VHL, CRBN, MDM2, and IAP. It is utilized in synthesizing PROTAC K-Ras Degrader-1, a highly effective PROTAC K-Ras degrader with a degradation efficacy of ≥70% in SW1573 cells[1].

2-(Biotin-amido)-13-bis(carboxylethoxy)propane is a polyethylene glycol (PEG)-based PROteolysis TArgeting Chimera (PROTAC) linker used in the synthesis of PROTACs[1].

Histone H3 (21-44)-GK-biotin is a peptide fragment of histone H3 that corresponds to amino acid residues 22-45 of the human histone H3.3 sequence and is biotinylated via a C-terminal GK linker. Unlike histone H3.1 and H3.2, the histone H3.3 variant contains a serine residue at position 31 that is phosphorylated during late prometaphase and metaphase of mitosis. Histone H3 (21-44) also contains lysine residues at positions 23, 27, and 36 that are subject to methylation and acetylation, all of which have a role in the regulation of gene expression, and a serine residue at position 28 that is subject to phosphorylation during mitosis.