U5382
Ubiquitin human
≥95% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal FLAG® tagged), lyophilized powder
Műszaki ügyfélszolgálat
Segítségre van szüksége? Szakértő tudósaink csapata készséggel áll az Ön rendelkezésére.
Segíthetünk?Műszaki ügyfélszolgálat
Segítségre van szüksége? Szakértő tudósaink csapata készséggel áll az Ön rendelkezésére.
Segíthetünk?biológiai forrás
human
Minőségi szint
rekombináns
expressed in E. coli (N-terminal FLAG® tagged)
Teszt
≥95% (SDS-PAGE)
Forma
lyophilized powder
molekulatömeg
10 kDa
technika/technikák
mass spectrometry (MS): suitable
oldhatóság
0.05 M Tris pH 7.5: ≥10 mg/mL, clear to slightly hazy, colorless
0.05 M Tris pH 7.5: ≥10 mg/mL
tárolási hőmérséklet
−20°C
Hasonló termékeket keres? Látogasson el ide Útmutató a termékösszehasonlításhoz
Általános leírás
Research Area: CANCER
Ubiquitin is a highly conserved protein composed of 76 amino acids, and it is expressed universally in all eukaryotes, ranging from yeast to humans.
Ubiquitin is a highly conserved protein composed of 76 amino acids, and it is expressed universally in all eukaryotes, ranging from yeast to humans.
Ubiquitin is a highly conserved globular protein and has lysine in the surface. The C-terminal end comprises the Leu-Arg-Gly-Gly structural motif.
Alkalmazás
Ubiquitin human can be used as a standard for mass spectrometry.
Ubiquitin human has been used in mono-ubiquitination of yeast proliferating cell nuclear antigen (PCNA) and in in vitro ubiquitination assay of defective in mitotic arrest 1 (Dma1)
Ubiquitin, N-terminal FLAG-tagged can replace the ubiquitin in formation of poly-ubiquitin—protein conjugates. The FLAG tag enables separation and enrichment of the protein conjugates on anti-FLAG affinity columns and detection of conjugates in western blot by anti-FLAG antibodies.
Biokémiai/fiziológiai hatások
Ubiquitin interacts with the lysine residue of proteins through its ε-amino group of the C-terminal glycine residue. Proteins interacting with ubiquitin either undergo mono-ubiquitination or multi-mono-ubiquitination via a three-step process. Ubiquitination regulates intracellular trafficking and protein degradation and an imbalance in the pathway is implicated in disorders.
Ubiquitin is a small regulatory protein present in eukaryote tissues. Exogenous ubiquitin can stimulate apoptosis in numerous cell lines. E7 protein of human papilloma virus-16 stimulates Retinoblastoma Protein degradation via Ubiquitin-Proteasome Pathway.
Ubiquitin-mediated proteolysis plays an important role in several basic cellular processes including regulation of cell cycle and division, differentiation and development, modulation of cell-surface receptors, the secretory pathway (protein transport), morphogenesis of neuronal networks, transcriptional regulation and signal transduction, transcriptional silencing, DNA repair, long-term memory, and circadian rhythms.
Kiszerelés
Package size based on protein content
Elkészítési megjegyzés
Ubiquitin human can be dissolved in 0.05 M Tris-HCl at a concentration of 10.00 - 11.00 mg/ml to yield a clear to slightly hazy, colorless solution.
Jogi információk
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
Tárolási osztály kódja
11 - Combustible Solids
WGK
WGK 3
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Egyéni védőeszköz
Eyeshields, Gloves, type N95 (US)
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The ubiquitin-proteasome pathway and the regulation of growth hormone receptor availability
Strous, Ger J and van Kerkhof, Peter
Molecular and cellular endocrinology, 143-151 (2002)
The ubiquitin-proteasome pathway and the regulation of growth hormone receptor availability
Strous, Ger J and van Kerkhof, Peter
Molecular and Cellular Endocrinology, 143-151 (2002)
Ana Camara-Artigas et al.
Acta crystallographica. Section F, Structural biology communications, 72(Pt 1), 29-35 (2016-01-12)
Ubiquitin is a small globular protein that has a considerable number of lysine residues on its surface. This results in a high surface entropy that precludes the formation of crystal-packing interactions. To date, only a few structures of the native
Regulation of NF-kappaB by ubiquitination
Chen J and Chen ZJ
Current Opinion in Immunology, 4-12 (2013)
David Komander
Biochemical Society transactions, 37(Pt 5), 937-953 (2009-09-17)
Protein ubiquitination and protein phosphorylation are two fundamental regulatory post-translational modifications controlling intracellular signalling events. However, the ubiquitin system is vastly more complex compared with phosphorylation. This is due to the ability of ubiquitin to form polymers, i.e. ubiquitin chains
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