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- Table of Contents
3 Q&As
Facts about T-complex protein 1 subunit gamma.
As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Human | |
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Gene Name: | CCT3 |
Uniprot: | P49368 |
Entrez: | 7203 |
Belongs to: |
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TCP-1 chaperonin family |
Cctg; chaperonin containing TCP1, subunit 3 (gamma); hTRiC5; TCP1 (t-complex-1) ring complex, polypeptide 5; TRIC5gamma subunit
Mass (kDA):
60.534 kDA
Human | |
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Location: | 1q22 |
Sequence: | 1; NC_000001.11 (156308961..156338415, complement) |
Cytoplasm.
If you're a biologist, you've likely heard of the Boster Bio. The company's signature products include antibodies and ELISA kits. Recently, they began providing PCR-related molecular biology products. In addition to their ELISA products, Boster Bio also offers a variety of services to help scientists work more effectively. Their 24 hour support team and free technical resources are among the many benefits that Boster Bio provides.
The CCT3 gene encodes an important protein that regulates the maintenance of telomeres. In a variety of biological assays, antibodies specific for CCT3 are used to detect the protein. Boster Bio developed CCT3 antibodies using mouse and rabbit. The protein is involved in folding the WRAP53/TCAB1 molecule and regulates the maintenance of telomeres.
Moreover, this marker is a potential therapeutic target, as it inhibits YAP and TFCP2. These proteins, in turn, may help in the development of new drugs and screening tests for liver cancer. However, it is important to note that serum CCT3 levels may also indicate other types of cancer, and seral-CCT3 is a promising biomarker for liver cancer.
In hepatocellular carcinoma cells, CCT3 is required for proliferation. Knockdown or overexpression of CCT3 resulted in decreased or increased cell proliferation. Conversely, it had opposite effects on caspase 3/7 activity. CCT3 expression was correlated with colony formation and in-vivo xenograft growth. For these reasons, it is essential to understand how the CCT3 gene can be used in hepatocellular carcinoma research.
One of the best ways to study YAP is to knockdown the CCT3 gene. This gene is responsible for regulating the expression of the YAP protein. Knockdown of CCT3 suppresses the transformational phenotypes in human cancer cells. Moreover, it is a transcription factor that functions as a TFCP2 ligase.
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Nanotechnology has had an impact on bioassays by enabling the development of novel nanostructures, nanodevices, and nanomaterials. Nanoparticles are tiny particles that are composed of numerous different components and have distinct optical, electronic, and catalytic properties. As a result, nanoparticles are now considered an alternative to conventional reagents. They can also be used as an alternative in bioassays to detect a variety of analytes.
A new class of fluorescent molecules has emerged in recent years. Among these, lanthanide-doped NPs show the highest LODs. They are the most versatile of the different NPs, and have exceptional photophysical properties. In bioassays, they are easy to synthesize, have good photophysical properties, and are highly compatible with the analytes.
Several different NPs have been developed to detect the targets of several oligonucleotide molecules at once. The target sequences in these NPs are listed in Table 1. Similarly, Au-NPs have been used to detect multiple oligonucleotide targets. Using Au-NPs and magnetic-microparticles to detect complementary nucleotide regions, these NPs were used to screen a range of viral targets in human cells.
Biological assays using the CCT3, a protein of the WRAP53/TCAB1 complex, were developed to identify the levels of a protein in mouse and rabbit tissues. These assays are useful in identifying the levels of telomere maintenance and cell death. Despite their limitations, this marker is an effective biomarker for the identification of cancer cells. The research team hopes that these antibodies will help them in their work.
A number of new studies have also shown that the upstream trigger for YAP is CCT3, as well as TFCP2. In addition, seral-CCT3 has proved to be a potential biomarker for cancer detection, outperforming alpha fetoprotein as the gold standard in liver tumor screening. The discovery of CCT3 as a biomarker will help in the development of targeted therapeutics and therapies.
Although CCT3 has recently been identified as an indicator of cancer, these assays are limited by a large number of other factors. Some of these limitations include non-specific adsorption, NP aggregation, and inherent cross-reactivity of antibodies. These factors can also make the results unreliable. Furthermore, NP immunoassays are difficult to develop because of their inherent cross-reactivity.
Moreover, CCT3 regulates the activity of YAP and TFCP2, allowing it to be selectively suppressed. In addition, it regulates TFCP2 and FYB, which are both targets of CCT3 in various cells. Knocking out CCT3 or TFCP2 can also affect YAP activity and protein expression, while YAP can reverse its effects when overexpressed.
The applications of CCT3 markers have been increasing in recent years, and recent studies have revealed that this gene plays an important role in several types of cancer. In fact, CCT3 is a subunit of the chaperonin-containing TCP-1 complex, which folds several proteins involved in cancer. Although the role of CCT3 in breast cancer is unclear, knockdown of the gene significantly reduced its expression in mouse breast cancer cells. Flow cytometry, Celigo image cytometry, and Western blot analysis were performed to examine cell proliferation and migration in breast cancer cells.
Knockdown of CCT3 reduced expression of the protein LUAD, which inhibits tumor growth. CCT3 deficiency inhibits the progression of LUAD and suppresses protein synthesis. In addition, knockdown of CCT3 decreased protein levels in the lung tissue of LUAD patients. These data indicate that CCT3 may serve as a prognostic marker for LUAD.
Both IQGAP3 and CCT3 are superior to AFP in predicting HCC. They increase the sensitivity and specificity of HCC and improve patient care by predicting tumor size. The markers may be used together with AFP to identify small HCC tumors. These are especially useful in cases when AFP is negative or has no correlation with tumor size. Therefore, these markers can also be used in a combination with AFP to improve patient care.
A study using data from 971 cases of breast cancer found that 51% of the cases had alterations in the CCT3 subunit. Of these, the highest proportion had alterations in CCT3. Additionally, knockdown of CCT3 significantly inhibited breast cancer cell growth and metastasis, a conclusion that suggests that it may play a role in tumor progression. The mechanisms involved are likely to be related to the cell cycle and signal transduction pathways.
Although CCT3 expression is higher in HCC tissues compared to the tissues of non-HCC cells, the protein is also important for tumor progression. In addition, it has been demonstrated to have a prognostic value in HCC. Furthermore, CCT3 is a novel regulator of spindle integrity in cells. It is necessary for proper kinetochore-microtubule attachment during mitosis. Furthermore, CCT3 has been shown to be upregulated in gastric cancer, and its expression levels were higher in tumour tissues compared to non-tumour tissue.
In addition to the above, researchers have also found that plasma CCT3 levels are highly correlated with those of IQGAP3 and CRiC. Further, these markers are useful for studying the folding of protein. However, these findings should be confirmed by studies using human sera. There are many other applications of CCT3 markers in blood. However, there is one important problem that must be addressed before CCT3 markers become widely adopted.
PMID: 8573069 by Walkley N.A., et al. Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT gamma.
PMID: 8001976 by Sevigny G., et al. Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by fluorescence in situ hybridization.