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Brand: ProteoGenix

Recombinant Human SIRT2, N-GST

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
70.02 kDa

$392.00

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Met1–Gln389
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Recombinant Human SIRT2, N-GST

Recombinant Human SIRT2, N-GST

Product name Recombinant Human SIRT2, N-GST
Origin species Human
Expression system Prokaryotic expression
Molecular weight 70.02 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°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)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Met1-Gln389
Aliases /Synonyms NAD-dependent protein deacetylase sirtuin-2, Regulatory protein SIR2 homolog 2, SIR2-like protein 2, SIRT2, SIR2L2, SIR2L
Reference ARO-P13253
Note For research use only.
Molecular Constructor
Met1–Gln389

Introduction

Recombinant Human SIRT2 is a protein that plays a crucial role in regulating cellular processes such as metabolism, stress response, and aging. It is a member of the sirtuin family of proteins, which are enzymes that have been shown to have important functions in maintaining cellular homeostasis. In this article, we will explore the structure, activity, and application of Recombinant Human SIRT2 in detail.

Structure of Recombinant Human SIRT2

The gene encoding for Recombinant Human SIRT2 is located on chromosome 19 and is composed of 10 exons. The protein has a molecular weight of approximately 39 kDa and is composed of 356 amino acids. It contains a highly conserved catalytic core domain, which is responsible for its enzymatic activity. This domain is surrounded by a NAD+ binding domain and a C-terminal domain, which are essential for its substrate specificity and protein-protein interactions, respectively.

Recombinant Human SIRT2 also has several post-translational modifications, including acetylation, phosphorylation, and sumoylation, which can regulate its activity and function. These modifications can also serve as potential targets for therapeutic interventions.

Activity of Recombinant Human SIRT2

Recombinant Human SIRT2 is a NAD+-dependent deacetylase, meaning it requires NAD+ as a cofactor to remove acetyl groups from its target proteins. It has been shown to deacetylate a wide range of substrates, including histones, transcription factors, and metabolic enzymes. This deacetylation activity is crucial for the regulation of cellular processes such as gene expression, protein stability, and metabolism.

One of the key functions of Recombinant Human SIRT2 is its role in maintaining genomic stability. It has been shown to deacetylate and activate the tumor suppressor protein p53, which plays a crucial role in cell cycle regulation and DNA repair. Additionally, Recombinant Human SIRT2 has been implicated in the regulation of cellular metabolism through its deacetylation of metabolic enzymes such as acetyl-CoA synthetase and pyruvate dehydrogenase.

Application of Recombinant Human SIRT2

The unique structure and activity of Recombinant Human SIRT2 make it a valuable tool for various applications in both research and therapeutic settings. Its deacetylation activity allows for the study of acetylation-mediated processes and the identification of potential therapeutic targets. It can also be used to investigate the role of sirtuins in aging and age-related diseases.

Recombinant Human SIRT2 has also shown promising potential as a therapeutic target for various diseases. It has been found to be dysregulated in several types of cancer, making it a potential target for cancer treatment. Additionally, its role in regulating metabolism and cellular stress response makes it a potential target for metabolic disorders and neurodegenerative diseases.

Conclusion

In summary, Recombinant Human SIRT2 is a crucial protein involved in the regulation of cellular processes such as metabolism, stress response, and aging. Its unique structure and activity make it a valuable tool for research and a potential therapeutic target for various diseases. Further studies on this protein and its interactions with other molecules will provide a better understanding of its role in maintaining cellular homeostasis and its potential for therapeutic interventions.

Keywords: Recombinant Human SIRT2, sirtuin, deacetylase, NAD+, post-translational modifications, genomic stability, therapeutic target, cancer, metabolism, neurodegenerative diseases.

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