SIRT1 Protein, Human (555a.a, His)

SIRT1 is an NAD-dependent protein deacetylase that integrates multiple cellular functions—cell cycle progression, DNA damage response, metabolism, apoptosis, and autophagy—by regulating the acetylation of various target proteins. SIRT1 responds to changes in the NAD(+)/NADH ratio caused by factors such as glucose deprivation, affecting chromatin remodeling through histone deacetylation, resulting in transcriptional regulation. SIRT1 Protein, Human (555a.a, His) is the recombinant human-derived SIRT1 protein, expressed by E. coli , with N-His labeled tag. The total length of SIRT1 Protein, Human (555a.a, His) is 555 a.a., with molecular weight of ~62.8 kDa.

SIRT1, a NAD-dependent protein deacetylase, orchestrates the integration of various cellular functions, including cell cycle progression, response to DNA damage, metabolism, apoptosis, and autophagy, by modulating the acetylation status of numerous target proteins. Functioning as a sensor of the NAD(+)/NADH ratio, SIRT1 responds to changes in cellular energetics induced by factors such as glucose deprivation and caloric restriction. Its wide-ranging impact encompasses chromatin remodeling through histone deacetylation, ultimately leading to transcriptional regulation. SIRT1 engages in diverse interactions, deacetylating transcription factors, coregulators, and histones, thereby exerting both positive and negative regulation on target gene expression. Additionally, SIRT1 is implicated in critical processes such as DNA damage response, autophagy, circadian rhythm regulation, and metabolic homeostasis. Its multifaceted roles extend to the regulation of various cellular pathways and the maintenance of genomic integrity, highlighting its significance in cellular physiology and stress response.

Human

E. coli

N-His

Q96EB6 (M193-S747)

23411  [NCBI]

Approximately 62.8 kDa

Greater than 80% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.