ubiquitin Protein, Human (His)

Ubiquitin is a multifunctional protein that can form covalently linked isopeptide bonds in various states, including mono- and polyubiquitin chains. ubiquitin Protein, Human (His) is the recombinant human-derived ubiquitin protein, expressed by E. coli , with N-His labeled tag.

Ubiquitin, a versatile protein, exists in either covalently attached forms to other proteins or in a free, unanchored state. In its covalently bound state, ubiquitin forms isopeptide bonds with target proteins, presenting as monoubiquitin, polyubiquitin chains linked through different Lys residues, or linear polyubiquitin chains initiated at the Met residue of ubiquitin. The diverse functions of polyubiquitin chains are dictated by the specific Lys residue involved: Lys-6-linked ubiquitin may play a role in DNA repair, Lys-11-linked in endoplasmic reticulum-associated degradation (ERAD) and cell-cycle regulation, Lys-29-linked in proteotoxic stress response and cell cycle, Lys-33-linked in kinase modification, Lys-48-linked in protein degradation via the proteasome, and Lys-63-linked in endocytosis, DNA damage responses, and NF-kappa-B activation. Linear polyubiquitin chains, initiated at Met, are implicated in cell signaling. While ubiquitin typically conjugates to Lys residues, rare instances involve conjugation to Cys or Ser residues. In its free form, unanchored-polyubiquitin contributes to various cellular processes, including the activation of protein kinases and signaling events. Ubiquitin's multifaceted roles underline its significance in orchestrating diverse cellular functions and regulatory pathways.

Human

E. coli

N-His

P0CG48 (M1-G75)

7316

Partial

MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG

Approximately 11 kDa, based on SDS-PAGE under reducing conditions.

≥ 90%, as determined by reducing SDS-PAGE.

Solution

Supplied as a 0.22 μm filtered solution of 50 mM Tris-HCl, pH 7.5, 200 mM NaCl, 1 mM DTT, 20% glycerol.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

Please use rapid thawing with running water to thaw the protein.

Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.

• [1]. /biology-dictionary/gak-cell.html