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K27 Diubiquitin Probes Catalog Number U2401 Lyophilized Purity≥95%

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.

Poly K63 Diubiquitin Probes Catalog Number U2801

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

K11 Diubiquitin Probes Polyubiquitination Catalog Number U2301

K11-Diubiquitin,Catalog Number: U2301,Lyophilized,Purity95% This K11 linked di-ubiquitin was obtained by chemical synthesis. K11 linked polyubiquitination increase when the metazoan anaphase-promoting complex APC/C is active during mitosis, and APC/C has been shown to assemble K11-linked ubiquitin chains to drive proteasomal degradation and exit from mitosis. Main Sales Markets: North America,Central/South America,Western Europe,Eastern Europe,Australia,Asia,Middle East

K29 Diubiquitin Probes Catalog Number U2501

K29-Diubiquitin,Catalog Number: U2501,Lyophilized,Purity95% This K29 linked di-ubiquitin was obtained by chemical synthesis. K29 linked polyubiquitination has been shown to be an inhibitor of Wnt signaling, which plays an important role in embryogenesis, and its deregulation has been shown to play a role in tumorigenesis.

Histone modifications

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

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