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- Table of Contents
Facts about Protein S100-A7.
Human | |
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Gene Name: | S100A7 |
Uniprot: | P31151 |
Entrez: | 6278 |
Belongs to: |
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S-100 family |
HID 5; HID5; HID-5; protein S100-A7; PSOR1; psoriasin 1; Psoriasin; S100 calcium binding protein A7 (psoriasin 1); S100 calcium binding protein A7; S100 calcium-binding protein A7 (psoriasin 1); S100 calcium-binding protein A7; S100A7; S100A7c
Mass (kDA):
11.471 kDA
Human | |
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Location: | 1q21.3 |
Sequence: | 1; NC_000001.11 (153457744..153460651, complement) |
Fetal ear, skin, and tongue and human cell lines. Highly up-regulated in psoriatic epidermis. Also highly expressed in the urine of bladder squamous cell carcinoma (SCC) bearing patients.
Cytoplasm. Secreted. Secreted by a non-classical secretory pathway.
This article will discuss the Anti-Psoriasin/S100A7 Marker. You will also learn about ICC and Immunofluorescence applications. Whether you're in the lab or performing a clinical study, you'll find the information you need in this article. Using this marker for your research is a great way to make sure your experiments are as effective as possible.
The anti-Psoriasin/S-100A7 marker is an important tool in the treatment of psoriasis. The protein is a small calcium-binding protein, and has been implicated in psoriasis and ductal carcinoma-in-situ. It is also expressed in breast cancer and various tumors with squamous differentiation.
Psoriasin is part of the S-100 gene family. It is a secreted protein that exerts chemotactic effects on inflammatory cells. It is thought to play a general role in inflammatory skin disease, as its expression is related to alterations in keratinocyte differentiation. Some studies have also suggested that psoriasin is expressed in squamous cell carcinoma.
The anti-Psoriasin/S-100A7 Marker in Boster Bio is derived from the same bacterium that causes atopic dermatitis. It reacts with Human, Mouse, and Rat psoriasis. The protein has also been linked to several other common erythrosquamous skin diseases.
The anti-Psoriasin/S-100A7 Marker in Boster Bio is a member of the S100 family. It is associated with preinvasive DCIS and with a poor prognosis in breast cancer. It has also been shown to increase EGF mRNA levels in MDA-MB-231 cells. However, it is not known whether S100A7 has any role in regulating EGF-induced EGFR signaling.
Its expression is elevated in psoriasis skin lesions. However, it has not been shown to be involved in metastatic bone lesions. However, this marker could be a useful biomarker for the disease. It could be a potential target for future drugs. It might play an amplifier role in the TNFa and IL-17 pathways.
The S100A7 gene contains multiple functional isoforms and has been implicated in various human diseases. Its ancestral homolog, psoriasin, is poorly conserved and has not been fully characterized. Its expression in squamous cells and under skin inflammation has been studied and is believed to regulate numerous downstream functions. For these reasons, psoriasin/S100A7 is a promising candidate for clinical applications.
The S100 gene family contains several members that encode small proteins with EF-hand helix-loop-helix domains. These proteins have a diverse range of biological functions, and altered expression of several of them has been implicated in a number of cancers. The S100A7 gene, for example, was first identified as an overexpressed protein in psoriasis and squamous cell carcinoma. Although psoriasin is not expressed in normal breast epithelium, it is expressed in invasive cancers of the breast.
In addition to human disease, the S100A7 gene is also implicated in a number of autoimmune diseases and cardiovascular disorders. Its use as a biomarker in laboratory studies is a step towards better diagnosis and more specific therapies for patients. Its role in cardiac disease has also been linked with ventricular tachycardia and arrhythmia. Further, it has been shown to have a role in the progression of cancer.
Using the S100A7 marker from Boster Bio, you can easily detect S100A7 expression in a variety of cells and tissues. Its antigen-binding domains bind to residues forty to ninety-three of S100A7, S100A8, and S100B. Depending on your sample, you may also use it in conjunction with a radioactive label or cytotoxic agent.
The S100A7 antibody is a monoclonal polyclonal antibody that binds to an epitope on the RAGE receptor. It mimics the interaction between the RAGE V-region and the helix A2 of S100A7 and S100B residues 43-78. The monoclonal antibody has high affinity for RAGE-bound epitopes and is suitable for studies of RAGE-mediated inflammatory diseases.
S100 proteins belong to the S100 family, a group of small acidic regulatory metal-binding proteins. Approximately twenty-four members of the family are present in a cell, divided into three main subgroups: S100A7, S100B1 and S100C. The S100 proteins are known to have broad functional diversity and are capable of adapting to various targets.
In a recent study, scientists found that miR-26b-5p inhibits S100A7, an important gene in cancer cells. This miRNA also affects invasive behavior of ICC cells. To explore this interaction, the authors used miR-26b-5p mimics and non-sense controls to transfect iRBE and HCCC-9810 cells. The results of these experiments demonstrate that miR-26b-5p inhibits ICC cells' invasiveness and migration.
The S100A7 marker is not only highly specific, but also can detect a wider range of tumors. Its antigen-binding ability makes it a valuable ICC marker for thoracic tumors. It is not only specific for invasive tumors, but also detects other types of cancer, including cervical and lipomas. It is available in multiple versions. To determine whether it is a good ICC marker, the corresponding ICC staining method should be determined.
S100A7, or psoriasin, is a member of the S100 protein family. It is encoded within the epidermal differentiation complex, which contains genes that encode markers for epidermal differentiation. It is overexpressed in hyperproliferative skin diseases, and is thought to have antimicrobial activities, chemotaxis, and NF-?B signalling.
S100A7 is a member of the S100 protein family and belongs to the EF-hand superfamily. It regulates many fundamental biological processes. It functions as a transglutaminase substrate, a chemokine, and an antibacterial protein. Several S100 proteins have been associated with the progression of cancer. Psoriasin (S100A7) is found to be overexpressed in acne inversa lesions, and exerts pore-forming activity in low pH conditions. Psoriasin may be a key in human tongue resistance to E. coli. Additionally, a psoriasin assay has potential to detect pulmonary involvement in systemic sclerosis.
IHC uses of the S100A7 protein are expanding rapidly, and this new marker is one of the most promising candidates. This protein has been associated with high-grade invasive breast cancer. It is also thought to activate prometastatic and angiogenic molecules. These properties may explain the plethora of applications in the field of cancer immunotherapy. Here, we review some of these applications.
The S100A7 protein is associated with ER-positive BCs. Estrogens have been found to enhance the expression of S100A7 in ER-positive MCF-7 cells through multiple mechanisms, including inhibition of DNA methylation. This suggests that S100A7 expression in ER-positive vs. ER-negative BCs may be regulated by multiple events. Further, we discuss potential applications of the S100A7 marker in cytology.
It has been shown that the S100A7 protein is involved in the actions of IGF-1 on BC cells. It may be the underlying signaling mechanism of the IGF-1R in cancers. It is considered to be an early orchestrator of invasive actions and elicits angiogenic effects via binding to RAGE. These roles suggest that S100A7 may have therapeutic potential as an anti-angiogenic agent.
In addition to its anti-tumor properties, S100A7 also has immunofluorescent properties. In addition to displaying the expression of tumor cells, this marker also helps identify tumor-related proteins. However, the IHC uses of the S100A7 marker in tumors are not yet well understood. It is difficult to predict which cancer cells will respond to the drug. However, studies have indicated that STAT3 may be a significant regulatory pathway in tumor growth.
Detection of psorisin in breast cancer cells using the S101A7 marker is a promising new strategy for screening and monitoring breast cancers. Previous studies have shown that psoriasin is associated with inflammatory skin diseases, including psoriasis. However, psoriasin expression does not correlate with the intensity of inflammatory cell infiltrates. Further, psoriasin expression in breast cancer cells does not correspond to the intensity of dermal inflammatory cell infiltrates.
Using an automated tissue immunostainer, psoriasin expression was evaluated using a semi-quantitative scoring method. The intensity of psoriasin expression and the proportion of epithelial cells that were positively stained were used to calculate psoriasin expression scores. Psoriasin expression was then analyzed using Graphpad software and Mann Whitney and Wilcoxon rank sum tests.
These results suggest that psoriasin may represent a potential therapeutic target in the treatment of GCs. Additionally, psoriasin could serve as a potential molecular marker for preoperative chemotherapy. Thus, detection of psoriasin in breast cancer cells with S100A7 expression may be a promising strategy for predicting patient responses to preoperative chemotherapy.
Molecular profiling of psoriasin in invasive ductal carcinomas revealed that higher levels of psoriasin were associated with increased estrogen and progesterone receptor-negative tumors. In addition, higher expression was associated with decreased invasiveness and nodal metastasis in all tumors except medullary carcinomas. This suggests that psoriasin acts as a chemoattractant for tumors.
PMID: 1940442 by Madsen P., et al. Molecular cloning, occurrence, and expression of a novel partially secreted protein 'psoriasin' that is highly up-regulated in psoriatic skin.
PMID: 8526920 by Burgisser D.M., et al. Amino acid sequence analysis of human S100A7 (psoriasin) by tandem mass spectrometry.