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- Table of Contents
Facts about Protein S100-A11.
Human | |
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Gene Name: | S100A11 |
Uniprot: | P31949 |
Entrez: | 6282 |
Belongs to: |
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S-100 family |
Calgizzarin; Metastatic lymph node gene 70 protein; MLN 70; MLN70; protein S100-A11; Protein S100-C; S100 calcium binding protein A11; S100 calcium-binding protein A11 (calgizzarin); S100 calcium-binding protein A11; S100A11; S100C; S100CS100 calcium binding protein A11 (calgizzarin)
Mass (kDA):
11.74 kDA
Human | |
---|---|
Location: | 1q21.3 |
Sequence: | 1; NC_000001.11 (152032506..152037004, complement) |
Cytoplasm. Nucleus.
S100A11 comes from the S100 protein group. This tumor-derived EVP proteins plays a dual role in promoting and inhibiting tumor growth. It is expressed at high levels in GC. Continue reading to learn about this protein and how it can be used best. We'll also examine potential uses for S100A11 as part of cancer research.
21 members make up the S100 protein family. Their molecular weights range from 10 to 14kDa. These proteins have many biological functions, including the regulation of cell growth, enzyme activities, and the inflammatory response. They can be found in many cell types and play an important role in the regulation of many diseases, such as cancers and inflammatory disorders. This article will focus on S100A11 which is a member of S100 protein families.
This protein is part of the S100 protein-kinase kinase familly, but it can be used as a biomarker in cancer. Its role in different cancers is unclear due to the many roles it plays. More research is needed. S100A11, although it is considered a secretory proteins, has been implicated in some cases of cancer. It is believed that the protein is secreted in extracellular vessels cargo and then modified upon its release.
The Cox proportional hazards regression model was used to analyze the data in this study. The data contained both clinical and genomic variants. After adjusting for age, gender, and cytogenetic alterations, the S100 gene expression was compared to the survival rate of MM patients. This study revealed that S100A11 was highly expressed in cancer cells.
Recent research has shown that S100A11 was over-expressed in many human cancers, including stomach cancer, pancreas cancer, and esophageal carcinomas. Despite this, there is no clear mechanistic explanation for S100A11's involvement in tumor cell proliferation and metastasis. We will discuss its roles in tumors. Its exact function can be determined by detailed mechanistic analyses.
We first prepared cDNA by reverse transcription-PCR from the S100A11 gene to isolate S100A11 cells. After that, the cDNA was cloned using reverse transcription-PCR and integrated into pET3a. Next, the protein was purified by differential precipitation and ion-exchange column chromatography. After purification, we prepared dimer S100A11 using HEPES buffer. The protein was then fractionated with gel filtration. Next, we biotinylated S100A11 using Biotin (AC5)2-OSu.
S100A11 is a tumor associated protein that acts as an essential mediator for NHK's growth suppression. S100A11 inhibits NHK cell growth via EGF-mediated protein phosphorylation. It also regulates activity of proteins in the cell, such as NF-kB signalling. In addition to its role in growth regulation, S100A11 is a critical component in the tumor microenvironment.
S100A11 has been associated with anti-cancer cell growth in animal models. This may be due in part to its ability stimulate RAGE (vascular endothelial grow factor) and VEGF. Its phosphorylation, RAGE and Akt may play a significant role in tumor-derived EVPs. S100A11 might have a therapeutic effect in the treatment of pancreatic carcinoma.
In cancer research, the S100A11 protein has a dual role as a tumor promoter and inhibitor. The protein is highly expressed by the sWAT, lung and kidneys, but only moderately in the small intestinale, heart and spleen. Further studies will be needed to determine the exact roles and functions of S100A11.
The S100A11 protein, also known as calgazzarin, belongs to a family of calcium-binding proteins that have two EF-hands. It is a small acidic protein with broad intracellular and extracellular roles. It has been linked to cancer stem cells. It has also been found to be highly expressed within a variety solid tumors.
The S100A11 Protein is also important for the early endosome. The tumour cells were unable, for 14 amino acids, to interact with Annexin A1 by deleting the S100A11 protein. This resulted a restriction in membrane structure and endosomal distribution. Because ANXA1 has been shown to be associated with internal vesiculation, binding to S100A11 may have the potential of modulating its properties.
S100A11 protein is expressed at higher levels in tumor tissue. Poor survival rates in patients suffering from GC are associated with the expression of this protein. S100A11 is thought to play a positive function in the progression of GC. This protein is an important marker to monitor the progression of tumors. Its dysregulation has been associated with various oncogenic activities.
S100A11 can be described as a cytoplasmic and highly expressed protein. It is found in the nucleus of many cells. It performs many functions, including controlling gene expression. The GC contains high amounts of S100A11.
The expression patterns of S100A11 are different in different tissues and under different physiological conditions. In normal kidney tissue, it is located in the nucleus while in cervical squamous cell carcinoma and ovarian adenocarcinoma, S100A11 is distributed in the cytoplasm. S100A11 is also expressed in high levels in several other cancers, including those of the kidney and ovary.
The level S100A11 could be measured by qPCR. Infected cells were incubated for 2 mg/ml puromycin in a medium. S100A11GC cell lines that showed stable silencing were kept in a medium containing 1.5 mg/ml puromycin. S100A11 is known to be a key player in inflammatory diseases, but further research is needed to determine if it is a clinical target for patients with GC.
S100A11, in addition to controlling cell growth, promotes the formation neonatima in response arterial injury. S100A11 has been found in neurons of rats brains. This may be due to S100A11's dual roles in neurological diseases. S100A11 is also thought to play a dual role during the development and progression cancers.
Several members of the S100 subfamily are known biomarkers of sepsis, and their downregulation is thought to exert protective effects on the body. For example, pentamidine prevents gliosis and ameliorates brain damage caused by cecal ligation and puncture. Alamandine inhibits MAPKs and attenuates S100A8 and S100A9 expression in sepsis-induced cells.
Boster Bio S100A11 antibody, an anti-S100A11 monoclonal antibody, binds specifically to the S100A11 epitope. This epitope includes residues 41-93 and 36-89 in S100A8, respectively, and 41-53 and S100B. These epitopes could be targeted therapeutically to prevent the growth of cancerous cells.
This antibody is designed in order to block RAGE's receptor. It inhibits RAGE either by differential competition or direct binding to it. The S100A11 marker may also be targeted therapeutically in a subset of patients with cancer, pre-cachexia, or cachexia. Therapeutic antibodies are designed to target both S100A11 and RAGE. They target both the soluble form and the RAGE receptor.
The antibody binds to V region of RAGE receptor. These residues are 23-116 in human RAGE. It mimics the interaction between RAGE's V-region and helix A2 in S100A7 as well as residues 43 to 78 in S100B. The antibody does not bind the S100B epitope.
PMID: 7889529 by Tanaka M., et al. Human calgizzarin; one colorectal cancer-related gene selected by a large scale random cDNA sequencing and northern blot analysis.
PMID: 7490069 by Tomasetto C.L., et al. Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17.