Transfected Stable Cell Lines
Reliable | High-Performance | Wide Rage
Precision reporter, kinase, immune receptor, biosimilar, Cas9, and knockout stable cell lines for diverse applications.
| Cat.No. | Product Name | Price |
|---|---|---|
| CSC-DC004093 | Panoply™ Human DCPS Knockdown Stable Cell Line | Inquiry |
| CSC-SC004093 | Panoply™ Human DCPS Over-expressing Stable Cell Line | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| AD04648Z | Human DCPS adenoviral particles | Inquiry |
| LV10404L | human DCPS (NM_014026) lentivirus particles | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| SHG224335 | shRNA set against Mouse Dcps(NM_027030.2) | Inquiry |
| SHG224353 | shRNA set against Rat Dcps(NM_153302.1) | Inquiry |
| SHG224363 | shRNA set against Human DCPS(NM_014026.3) | Inquiry |
| SHH275301 | shRNA set against Human DCPS (NM_014026.3) | Inquiry |
| SHH275305 | shRNA set against Mouse DCPS (NM_027030.2) | Inquiry |
| SHH275309 | shRNA set against Rat DCPS (NM_153302.1) | Inquiry |
| SHW017513 | shRNA set against Danio rerio DCPS (NM_205588) | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| CDCB156399 | Rat DCPS ORF clone (BC105900.1) | Inquiry |
| CDCB159119 | Human DCPS ORF clone (BC014532) | Inquiry |
| CDCB178988 | Danio rerio DCPS ORF Clone (NM_205588) | Inquiry |
| CDFH004844 | Human DCPS cDNA Clone(NM_014026.3) | Inquiry |
| CDFR014582 | Rat Dcps cDNA Clone(NM_153302.1) | Inquiry |
| MiUTR1H-02695 | DCPS miRNA 3'UTR clone | Inquiry |
| MiUTR1R-01392 | DCPS miRNA 3'UTR clone | Inquiry |
| CDCB194536 | Rabbit DCPS ORF clone (XM_002708301.2) | Inquiry |
| CDCR296783 | Human DCPS ORF Clone(NM_014026.3) | Inquiry |
| CDCR381669 | Rat Dcps ORF Clone(NM_153302.1) | Inquiry |
| CDCS413468 | Human DCPS ORF Clone (BC014532) | Inquiry |
The scavenger decapping enzyme (DcpS) is an essential enzyme that plays a crucial role in cellular metabolism, particularly in the degradation of misfolded and aggregated proteins. DcpS is a member of the AAA+ family of ATPases, which are characterized by their ability to hydrolyze ATP and tomediate the degradation of proteins.
The structure of DcpS shares significant similarities with other members of the AAA+ family, such as hexagonal structure and conserved ATP-binding domains. DcpS consists of two main domains: the N-terminal domain (N-DcpS) and the C-terminal domain (C-DcpS). The N-DcpS domain is responsible for substrate recognition and binding, while the C-DcpS domain is involved in ATP hydrolysis and protein degradation.
DcpS functions as a decapping enzyme, meaning that it promotes the removal of the caps from the ends of mRNA molecules. This process is important for the regulation of gene expression, as it allows the cell to control the translation of specific mRNA molecules. In addition to its role in mRNA decapping, DcpS has also been shown to degrade a wide variety of proteins, including misfolded and aggregated proteins.
Figure 1. Model depicting consequence on nuclear splicing in the presence or reduction of DcpS.
Misfolded and aggregated proteins are common in various diseases, including neurodegenerative diseases, metabolic disorders, and cancer. The accumulation of these proteins can lead to the impairment of cellular function and contribute to the pathogenesis of these diseases. Therefore, the degradation of these proteins is an important process for maintaining cellular homeostasis and preventing disease progression.
DcpS has been shown to be involved in the pathogenesis of various diseases, including Alzheimer's disease, Parkinson's disease, and cancer. In Alzheimer's disease, DcpS has been implicated in the degradation of amyloid-beta (Aβ), a key pathological protein in this disease. In Parkinson's disease, DcpS has been shown to be involved in the degradation of α-synuclein, a protein that accumulates in the brains of patients with this disease. In cancer, DcpS has been shown to promote the degradation of oncogenic proteins, suggesting that it may play a role in the development and progression of cancer.
Given the essential role of DcpS in cellular metabolism and disease, targeting this enzyme has the potential to be an effective therapeutic strategy for various diseases. For example, increasing the activity of DcpS has the potential to promote the degradation of misfolded and aggregated proteins, which could help to prevent the progression of neurodegenerative diseases and cancer. On the other hand, inhibiting the activity of DcpS has the potential to be an effective therapeutic strategy for diseases such as Alzheimer's disease and Parkinson's disease, where the accumulation of misfolded proteins is a key pathological feature.
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