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K27-Diubiquitin Catalog Number U2401 Lyophilized Purity95% This K27 linked di-ubiquitin was obtained by chemical synthesis. K27-linkage poly-ubiquitination plays important roles in DNA damage repair and autoimmunity. Recently reports have emerged that place K27 chains mainly in the intracellular innate immune response pathway, where they regulate several essential infection sensors, such as STING, cGAS, MAVS, and MDA5, or effectors such as NEMO and Beclin.

Dha-K27-Diubiquitin,Catalog Number:UD2401,Lyophilized,Purity95% Dha-K27-Diubiquitin. At the isopeptide-bonding site, the distal ubiquitin-76 glycine mutates into dehydroalanine, which is used to trap the deubiquitinating enzyme. Main Sales Markets: North America,Central/South America,Western Europe,Eastern Europe,Australia,Asia,Middle East,Africa

K63-Diubiquitin,Catalog Number: U2801,Lyophilized,Purity95% This K63 linked di-ubiquitin was obtained by chemical synthesis. K63-linked polyubiquitin chains exert nonproteolytic functions in vivo, such as protein trafficking, kinase/phosphatase activation, and DNA damage control, all of which might be important in regulation of cancer survival and development. The array of cellular processes initiated and regulated by ubiquitin has been partially explained by the structural

Ubiquitin (Ub) is ubiquitous. This small, 76-residue protein is used to mark cellular proteins for degradation by the ubiquitin proteasome system (UPS). Two key enzyme families, Ub ligases and deubiquitylation enzymes (DUBs), are responsible for putting on and taking off these Ub units and controlling the overall protein population of the cell. As you might imagine, this dynamic process is important, and dysregulation can lead to an array of bad things. Thus, understanding

Types of histone modification Chromatin architecture, nucleosomal positioning, and ultimately access to DNA for gene transcription, is largely controlled by histone proteins. Each nucleosome is made of two identical subunits, each of which contains four histones: H2A, H2B, H3, and H4. Meanwhile, the H1 protein acts as the linker histone to stabilize internucleosomal DNA and does not form part of the nucleosome itself. Histone proteins undergo post-translational modification