linear penta-ubiquitin human

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biological source




mol wt

43 kDa (His Tagged)


pkg of 100 μg

shipped in

dry ice

storage temp.


General description

Ubiquitin is an evolutionary highly conserved 76-residue protein with a molecular weight of 8.6kDa. Linear ubiquitination is a post-translational protein modification essential in innate and adaptive immune signaling. C-terminal of the ubiquitin molecule attaches itself to the ε-amino group of lysine side chains on target proteins, through the actions of activating and conjugating enzymes. Major ubiquitin modification involves the linking of a lysine side chain on the proximal ubiquitin and the C-terminal of the neighboring distal ubiquitin to form lengthened chains of ubiquitin molecule. Linear ubiquitin chains are formed by LUBAC (linear ubiquitin chain assembly complex) which contains HOIP (HOIL-1L interacting protein), HOIL-1L (heme-oxidized IRP2 ubiquitin ligase 1), and SHARPIN SH3 and multiple ankyrin repeat domains protein (SHANK)-associated RBCK1 homology (RH) domain interactor.
Recombinant linear chains of defined length are expressed in Escherichia coli and purified to homogeneity. Amide linkages join the N- and C-terminus of each ubiquitin molecule to each other. This molecule is HIS-tagged at the N-terminus of the most distal ubiquitin.

Biochem/physiol Actions

Ubiquitin is essential in post-translational modifications that regulate a variety of cellular pathways, such as response to viral infections. Ubiquitin molecules link together through lysine residues to form elongated lysine chains, and the ubiquitin lysine residue participating in the formation of these chains is responsible for the complexity linked with ubiquitin modifications. Almost all the seven lysine residues (Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, and Lys63) on ubiquitin are thought to be capable of forming homotypic chains that drive different linkage-dependent cellular pathways. The most common modification is K48-based chain which drives the modified protein to proteasomal degradation. Another well characterized modification is the K63-based chain which is linked with endocytic process-regulation, DNA-damage response, and innate immune response signaling. Linear ubiquitin chains also play a role in NFκB (nuclear factor) signaling activation when stimulated by various signals, where these chains link with NEMO (NF-κB essential modulator).

Physical form

In 20 mM Tris-HCl, pH 7.5, 0.15 M NaCl and 1 mM EDTA.

Preparation Note

Centrifuge the vial prior to opening.


NONH for all modes of transport

WGK Germany


Flash Point F

Not applicable

Flash Point C

Not applicable

Certificado de Análisis
Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating activity of SARS-CoV papain-like protease.
Ratia K et al
PLoS Pathogens, 10(5), e1004113-e1004113 (2014)
Linear ubiquitination in immunity.
Shimizu Y et al
Immunological Reviews, 266(1), 190-207 (2015)
Gliotoxin suppresses NF-?B activation by selectively inhibiting linear ubiquitin chain assembly complex (LUBAC).
Sakamoto H et al
ACS Chemical Biology, 10(3), 675-681 (2015)
Identification of the major ubiquitin-binding domain of the Pseudomonas aeruginosa ExoU A2 phospholipase.
Anderson DM et al
The Journal of Biological Chemistry, 288(37), 26741-26752 (2013)

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