Recombinant Human UBE2I/UBC9, N-His

Reference: YHF60801
Product nameRecombinant Human UBE2I/UBC9, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight16.73 kDa
Protein delivered with Tag?N-Terminal His Tag
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeAsp33-Ser158
Aliases /SynonymsUBE2I, UBC9, p18, UBCE9, Ubiquitin carrier protein 9, RING-type E3 SUMO transferase UBC9, SUMO-conjugating enzyme UBC9, Ubiquitin carrier protein I, Ubiquitin-protein ligase I, Ubiquitin-conjugating enzyme E2 I, SUMO-protein ligase
ReferenceYHF60801
NoteFor research use only.

Description of Recombinant Human UBE2I/UBC9, N-His

Introduction

Recombinant Human UBE2I/UBC9 is a protein that plays a crucial role in the process of protein modification and degradation. It is a member of the ubiquitin-conjugating enzyme family and is involved in the attachment of the small protein ubiquitin to target proteins, a process known as ubiquitination. This protein has gained significant interest in the scientific community due to its diverse functions and potential applications in various fields.

Structure of Recombinant Human UBE2I/UBC9

Recombinant Human UBE2I/UBC9 is a 17-kDa protein that consists of 158 amino acids. It has a conserved catalytic domain at the N-terminus, which is responsible for its enzymatic activity. The C-terminus of the protein contains a highly flexible tail that allows for interaction with various binding partners.

Enzymatic Activity of Recombinant Human UBE2I/UBC9

The main function of Recombinant Human UBE2I/UBC9 is to catalyze the transfer of ubiquitin from the E1 activating enzyme to the target protein. This process involves the formation of a thioester bond between the catalytic cysteine residue of UBE2I/UBC9 and the C-terminus of ubiquitin. This is followed by the transfer of ubiquitin to the target protein, which is facilitated by the interaction between the flexible tail of UBE2I/UBC9 and the target protein.

Role of Recombinant Human UBE2I/UBC9 in Protein Modification

The ubiquitination process is a crucial mechanism for regulating protein activity, stability, and localization. Recombinant Human UBE2I/UBC9 is involved in various types of ubiquitination, including monoubiquitination, multi-monoubiquitination, and polyubiquitination. These different forms of ubiquitination have distinct effects on the target proteins, such as altering their function, promoting their degradation, or targeting them for specific cellular processes.

Applications of Recombinant Human UBE2I/UBC9

The diverse functions of Recombinant Human UBE2I/UBC9 make it a valuable tool in various research fields. One of its main applications is in studying the ubiquitination process and its role in protein regulation. Recombinant Human UBE2I/UBC9 can be used to investigate the effects of ubiquitination on specific target proteins and to identify potential binding partners.

In addition, Recombinant Human UBE2I/UBC9 has potential therapeutic applications. Dysregulation of the ubiquitination process has been linked to various diseases, including cancer and neurodegenerative disorders. By targeting Recombinant Human UBE2I/UBC9, it may be possible to modulate the ubiquitination of specific proteins and potentially treat these diseases.

Furthermore, Recombinant Human UBE2I/UBC9 has been used in the development of diagnostic tools. Its ability to specifically interact with target proteins makes it a useful tool for detecting and quantifying specific antigens in biological samples. This has potential applications in disease diagnosis and monitoring.

Conclusion

Recombinant Human UBE2I/UBC9 is a crucial protein involved in the ubiquitination process. Its structure and enzymatic activity make it a valuable tool for studying protein modification and regulation. Its potential applications in research, therapy, and diagnostics make it a highly sought-after protein in the scientific community. Further studies and developments in this field may lead to new insights and potential treatments for various diseases.

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