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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

329.00

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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 belongs to the sirtuin family of enzymes, which are involved in regulating cellular processes such as metabolism, DNA repair, and aging. SIRT2 is a nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase, meaning it removes acetyl groups from proteins using NAD+ as a co-substrate. In this article, we will explore the structure, activity, and applications of Recombinant Human SIRT2.

Structure of Recombinant Human SIRT2

Recombinant Human SIRT2 is a 39 kDa protein that is encoded by the SIRT2 gene located on chromosome 19 in humans. It contains 356 amino acids and has a conserved catalytic domain known as the Sirtuin core domain. This domain is responsible for the deacetylase activity of SIRT2. In addition, SIRT2 also has a NAD+ binding domain and a C-terminal domain that is involved in protein-protein interactions.

Activity of Recombinant Human SIRT2

Recombinant Human SIRT2 is a highly conserved enzyme that is found in various organisms, including humans. It plays a crucial role in regulating cellular processes by deacetylating a wide range of substrates, including histones, transcription factors, and metabolic enzymes. By removing acetyl groups from these proteins, SIRT2 can alter their activity, stability, and localization, thereby modulating cellular functions.

One of the main functions of SIRT2 is its involvement in the regulation of cell cycle progression. It has been shown to deacetylate and activate the tumor suppressor protein p53, which plays a crucial role in cell cycle arrest and apoptosis. SIRT2 has also been implicated in DNA repair mechanisms by deacetylating and activating the DNA repair protein XRCC6. In addition, SIRT2 has been shown to regulate metabolism by deacetylating and activating enzymes involved in glucose and lipid metabolism.

Applications of Recombinant Human SIRT2

Recombinant Human SIRT2 has a wide range of applications in both basic research and drug development. Its role in regulating cell cycle progression and DNA repair makes it an attractive target for cancer therapy. In fact, SIRT2 inhibitors have been developed as potential anti-cancer drugs, as they can induce cell cycle arrest and apoptosis in cancer cells.

In addition, SIRT2 has also been implicated in neurodegenerative diseases such as Parkinson’s and Alzheimer’s. Studies have shown that SIRT2 can regulate the activity of proteins involved in these diseases, making it a potential target for drug development.

Furthermore, SIRT2 has been shown to play a role in metabolic diseases such as diabetes and obesity. By regulating the activity of metabolic enzymes, SIRT2 can modulate glucose and lipid metabolism, making it a potential target for the treatment of these diseases.

Conclusion

Recombinant Human SIRT2 is a highly conserved enzyme that plays a crucial role in regulating cellular processes. Its structure, activity, and applications make it an attractive target for drug development in various diseases. As research on SIRT2 continues, we can expect to uncover more functions and potential therapeutic applications of this important protein.

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