S. cerevisiae Ubiquitin (DAG2659)

S. cerevisiae Ubiquitin, recombinant protein from E. coli

Product Overview
Ubiquitin, yeast recombinant
Nature
Recombinant
Tag/Conjugate
Unconjugated
Procedure
None
Purity
> 95% by SDS-PAGE
Format
5 mg, lyophilized powder
Preservative
None
Storage
2-8°C short term, -20°C long term
Introduction
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. Similarity: Belongs to the ubiquitin family. Contains 3 ubiquitin-like domains.
Antigen Description
Highly purified ubiquitin free of glycine and buffer salts which can interfere with chemical and in vitro reactions. Ubiquitin is a 76 amino acid, highly conserved nuclear and cytoplasmic eukaryotic protein. It is covalently attached to substrate proteins by enzymes in the Ubiquitin-Proteasome Pathway (UPP). The major role of ubiquitination is to target cellular proteins for the ATP-dependent degradation by the 26S proteasome and proteasome-independent or regulatory events such as protein localization, activity and function. This protein sequence is for S.cerevisiae (P61864) and is exactly the same for S.pombe.
Keywords
FLJ25987; MGC8385; Polyubiquitin B; RPS 27A; RPS27A; UBA 52; UBA 80; UBA52; UBA80; UBB; UBB; UBC; UBCEP 1; UBCEP 2; UBCEP1; UBCEP2; Ubiquitin; ubiquitin B;

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