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AntibodySystem
Recombinant Proteins
Recombinant Human SIAH2 Protein, also known as Seven In Absentia Homolog 2, is a highly conserved protein that plays a crucial role in various cellular processes such as cell cycle regulation, apoptosis, and tumorigenesis. It is a member of the SIAH family of E3 ubiquitin ligases and is involved in the degradation of target proteins by tagging them with ubiquitin for proteasomal degradation. In this article, we will discuss the structure, activity, and applications of Recombinant Human SIAH2 Protein.
The human SIAH2 gene is located on chromosome 3 and encodes a protein of 321 amino acids. The protein consists of an N-terminal RING finger domain, two zinc fingers, and a C-terminal substrate-binding domain. The RING finger domain is responsible for the E3 ubiquitin ligase activity of SIAH2, while the zinc fingers are involved in protein-protein interactions. The substrate-binding domain recognizes and binds to specific target proteins for ubiquitination. The structure of SIAH2 is highly conserved among different species, indicating its essential role in cellular processes.
Recombinant Human SIAH2 Protein has been shown to have multiple activities, including E3 ubiquitin ligase activity, transcriptional regulation, and protein-protein interactions. The E3 ubiquitin ligase activity of SIAH2 is crucial for the degradation of target proteins, such as transcription factors and tumor suppressors, by the ubiquitin-proteasome system. This activity is regulated by the binding of specific adaptor proteins, such as SIAH-interacting protein (SIP), to the substrate-binding domain of SIAH2. SIAH2 has also been reported to regulate the activity of transcription factors, such as p53 and HIF-1α, by promoting their degradation.
In addition to its E3 ubiquitin ligase activity, SIAH2 has also been shown to have transcriptional regulatory functions. It can act as a co-activator or co-repressor of gene expression by interacting with transcription factors and modulating their activity. SIAH2 has been reported to regulate the expression of genes involved in cell cycle progression, apoptosis, and angiogenesis.
SIAH2 is also involved in protein-protein interactions, which are crucial for its various activities. It has been shown to interact with a wide range of proteins, including other E3 ubiquitin ligases, transcription factors, and signaling molecules. These interactions play a crucial role in the regulation of SIAH2 activity and its downstream effects.
Recombinant Human SIAH2 Protein has been widely used in research as a tool to study its role in cellular processes and its potential as a therapeutic target. It has been shown to play a critical role in tumorigenesis, making it a potential target for cancer therapy. Inhibition of SIAH2 activity has been shown to suppress tumor growth in various cancer types, highlighting the potential of SIAH2 as a therapeutic target.
SIAH2 has also been implicated in neurodegenerative diseases, such as Alzheimer’s and Parkinson’s, making it a potential target for the development of treatments for these conditions. In addition, SIAH2 has been shown to play a role in viral infections, making it a potential target for antiviral therapies.
Recombinant Human SIAH2 Protein has also been used in various in vitro and in vivo studies to elucidate its role in different cellular processes. It has been used to study its interactions with other proteins, its effects on gene expression, and its role in cell cycle regulation and apoptosis. In addition, SIAH2 has been used in drug
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