Recombinant Human Polyubiquitin-B (UBB), partial

Baculovirus
Mammalian cell

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

UBB

Uniprot NO.

P0CG47

Alternative Names

UBB; UBB_HUMAN; Ubiquitin

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

1-76

Target Protein Sequence

MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Buffer

Lyophilized from Tris/PBS-based buffer, 6% Trehalose, pH 8

Storage

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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.

Gene References into Functions

This study demonstrated that the Deposition of mutant ubiquitin in parkinsonism-dementia complex of Guam. PMID:29122008
The polyubiquitinated forms of the neurodegenerative ubiquitin mutant UBB have been characterized. PMID:27861798
The C-terminal five residues of Ub, RLRGG, are responsible for the interaction with the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease. PMID:27245450
A new crystallographic structure of human ubiquitin solved from crystals grown in the presence of magnesium. PMID:26750481
Data suggest that both human ubiquitin and HFBII (hydrophobin-II from Trichoderma reesei) exhibit a critical surface hydration level (or effective hydrophobic interface at the surface) at which percolation transition of water network occurs. PMID:25204743
UbB was significantly increased in prolonged Trichostatin A-selected HeLa cells and it played a key role in the maintenance of cervical cancer stem-like cells PMID:24367661
downregulation of ubiquitin through Ubb-KD is a potential anti-cancer treatment by inhibiting ubiquitination at multiple sites related to oncogenic pathways and by weakening the ability of cancer cells to overcome increased stress. PMID:24022007
A significant decrease in amyloid beta deposition and plaque formation suggests a role for the ubiquitin-proteasome system in the amyloid pathology of Alzheimer's disease. PMID:22797007
age-dependent accumulation of Ubb(+1) , and how Ubb(+1) -mediated proteasome inhibition may contribute to Alzheimer's disease. [review] PMID:22082077
Studies indicate that biomedical research on ubiquitin moves into translational research and drug discovery. PMID:21544573
Studies indicate that DUBs recycle ubiquitin by processing polyubiquitin chains to generate free ubiquitin, and can be regulated by ubiquitination or phosphorylation. PMID:21480003
analysis of orexin receptor 1 and 2 -arrestin-ubiquitin complexes PMID:21378163
The results of this study demonstrated that the UBB mutation caused the subtle defect in spatial reference memory formation, caused by a decrease in forebrain proteasome activity. PMID:21059367
Studies indicate that indicating that the inhibition of the ubiquitin-proteasome system could be used as a novel approach for cancer therapy. PMID:20491623
Results suggest that the interaction between E2-25K and UBB(+1) is critical for the synthesis and accumulation of UBB(+1)-anchored polyubiquitin, which results in proteasomal inhibition and neuronal cell death. PMID:20826778
Molecular misreading of the ubiquitin B gene and hepatic mallory body formation. PMID:12055595
expression of UBB+1 causes proteasome inhibition and induces expression of heat-shock proteins; although UBB+1-expressing cells have a compromised ubiquitin-proteasome system, they are protected against oxidative stress PMID:12871580
The temporal localization of frame-shift ubiquitin-B and amyloid precursor protein, and complement proteins in the brain of non-demented control patients with increasing Alzheimer's disease pathology. PMID:12893422
In sporadic inclusion-body myositis, UBB+1 may be pathogenic by inhibiting proteasome, thereby promoting accumulation of cytotoxic misfolded amyloid-beta and phosphorylated-tau. PMID:15452314
UBB+1, a mutant form of ubiquitin was present in the majority of NFTs, whereas co-existence of alpha-synuclein and UBB+1 was found in only a few neurons in cases of combined multiple system atrophy and Alzheimer's disease. PMID:17237936
K63-polyubiquitination guards against chemical carcinogenesis by preventing mutagenesis and thus contributing to genomic stability PMID:17395554
UBB(+1), at low expression levels, is efficiently degraded by the proteasome, but at high levels, the proteasome failed to degrade UBB(+1), causing its accumulation. PMID:17405812
analyse the expression of mutant ubiquitin (UBB+1), in muscle biopsies from patients suffering from myotilinopathy and desminopathy PMID:17931355
The expression a mutant human UBB analogous (UB14) in yeast markedly enhanced cellular susceptibility to toxic protein aggregates. PMID:19214209