UBE2G Human
Ubiquitin-Conjugating Enzyme E2G Human Recombinant
Cat. No.
BT18154
Source
Escherichia Coli.
Synonyms
E217K, UBC7, UBE2G, Ubiquitin-conjugating enzyme E2 G1, E2
ubiquitin-conjugating enzyme G1, E217K, UBC7, Ubiquitin carrier protein G1, Ubiquitin-protein
ligase G1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs 
In Stock 
Description
UBE2G Human Recombinant produced in E.Coli is a single,
non-glycosylated polypeptide chain containing 193 amino acids (1-170 a.a) and
having a molecular mass of 21.9kDa.UBE2G is fused
to a 23 amino acid His-tag at N-terminus & purified by proprietary
chromatographic techniques.
Product Specs
Introduction
Protein modification with ubiquitin is a crucial cellular process for marking abnormal or short-lived proteins for degradation. This process involves at least three types of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin-protein ligases (E3s). Ubiquitin-Conjugating Enzyme E2G (UBE2G1), a member of the E2 ubiquitin-conjugating enzyme family, facilitates the attachment of ubiquitin to other proteins. UBE2G1 is specifically involved in the breakdown of muscle-specific proteins.
Description
Recombinant human UBE2G, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 193 amino acids (1-170 a.a.) with a molecular weight of 21.9 kDa. This protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The UBE2G protein solution (0.5mg/ml) is supplied in phosphate buffered saline (pH 7.4) containing 30% glycerol and 1mM DTT.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
Purity exceeds 95.0% as determined by SDS-PAGE analysis.
Synonyms
E217K, UBC7, UBE2G, Ubiquitin-conjugating enzyme E2 G1, E2
ubiquitin-conjugating enzyme G1, E217K, UBC7, Ubiquitin carrier protein G1, Ubiquitin-protein
ligase G1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTELQSA LLLRRQLAEL NKNPVEGFSA GLIDDNDLYR WEVLIIGPPD
TLYEGGVFKA HLTFPKDYPL RPPKMKFITE IWHPNVDKNG DVCISILHEP GEDKYGYEKP EERWLPIHTV
ETIMISVISM LADPNGDSPA NVDAAKEWRE DRNGEFKRKV ARCVRKSQET AFE.
Product Science Overview
Introduction to Ubiquitin-Conjugating Enzymes
Ubiquitin-conjugating enzymes, also known as E2 enzymes, play a crucial role in the ubiquitination process, which is a post-translational modification that regulates various cellular processes. These enzymes are responsible for the transfer of activated ubiquitin from the E1 ubiquitin-activating enzyme to the substrate proteins, facilitated by E3 ubiquitin ligases .
Ubiquitin-Conjugating Enzyme E2G
Mechanism of Action
The ubiquitination process involves a three-step enzyme cascade:
- Activation: The E1 enzyme activates ubiquitin in an ATP-dependent manner, forming a ubiquitin-E1 complex.
- Conjugation: The activated ubiquitin is transferred to the E2 enzyme (in this case, UBE2G) via a thioester bond, forming the E2-ubiquitin complex.
- Ligation: The E3 ubiquitin ligase facilitates the transfer of ubiquitin from the E2 enzyme to the lysine residues on the substrate protein, completing the ubiquitination process .
Biological Significance
UBE2G is involved in various cellular processes, including:
- Protein Degradation: Ubiquitination marks proteins for degradation by the proteasome, thus regulating protein levels within the cell.
- Cell Cycle Regulation: UBE2G plays a role in the progression of the cell cycle by targeting specific cell cycle regulators for degradation.
- Stress Response: The enzyme is involved in the cellular response to stress by regulating the stability of stress-responsive proteins .
Disease Associations
Abnormalities in the function or expression of UBE2G have been linked to several diseases, including:
- Cancer: Dysregulation of ubiquitination can lead to the accumulation of oncogenic proteins, contributing to tumorigenesis.
- Neurodegenerative Diseases: Impaired ubiquitination can result in the accumulation of misfolded proteins, which is a hallmark of neurodegenerative diseases such as Parkinson’s and Alzheimer’s .
Human Recombinant UBE2G
Quick Inquiry
Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
