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SRP0441

Sigma-Aldrich

UBE3A active human

recombinant, expressed in baculovirus infected Sf9 cells, ≥72% (SDS-PAGE)

Synonym(s):

HPVE6A, ubiquitin protein ligase E3A

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in baculovirus infected Sf9 cells

Assay

≥72% (SDS-PAGE)

form

aqueous solution

mol wt

99.8 kDa

packaging

pkg of 20 μg

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... UBE3A(7337)

General description

Human UBE3A (var1) (GenBank Accession No. NM_130838) amino acids 2-end with N-terminal His-FLAG-tag, MW=99.8 kDa, expressed in a Baculovirus infected Sf9 cell expression system.

Application

Useful in conjunction with E1and E2 for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Physical form

Formulated in 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 250mM imidazole, 20% Glycerol and 3mM DTT.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Eui-Man Jung et al.
International journal of molecular medicine, 28(5), 697-704 (2011-08-13)
Some human embryonic stem cell lines have shown genomic instabilities over long-term culture. To study the controversial origin of the SCNT-hES-1 line, which was derived from autologous somatic cell nuclear transfer (SCNT), we compared the expression and methylation patterns of
Stefania Corvaglia et al.
Scientific reports, 4, 5366-5366 (2014-06-21)
Intrinsically Disordered Proteins (IDPs) are characterized by the lack of well-defined 3-D structure and show high conformational plasticity. For this reason, they are a strong challenge for the traditional characterization of structure, supramolecular assembly and biorecognition phenomena. We show here
Laura Caldinelli et al.
BMC biotechnology, 13, 32-32 (2013-04-06)
Human α-synuclein is a small-sized, natively unfolded protein that in fibrillar form is the primary component of Lewy bodies, the pathological hallmark of Parkinson's disease. Experimental evidence suggests that α-synuclein aggregation is the key event that triggers neurotoxicity although additional
Yunden Jinsmaa et al.
The Journal of pharmacology and experimental therapeutics, 372(2), 157-165 (2019-11-21)
Lewy body diseases such as Parkinson's disease involve intraneuronal deposition of the protein α-synuclein (AS) and depletion of nigrostriatal dopamine (DA). Interactions of AS with DA oxidation products may link these neurohistopathologic and neurochemical abnormalities via two potential pathways: spontaneous
Lisa Fellner et al.
Glia, 61(3), 349-360 (2012-10-31)
Alpha-synucleinopathies (ASP) are neurodegenerative disorders, characterized by accumulation of misfolded α-synuclein, selective neuronal loss, and extensive gliosis. It is accepted that microgliosis and astrogliosis contribute to the disease progression in ASP. Toll-like receptors (TLRs) are expressed on cells of the

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