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- Table of Contents
Facts about Flotillin-2.
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Human | |
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Gene Name: | FLOT2 |
Uniprot: | Q14254 |
Entrez: | 2319 |
Belongs to: |
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band 7/mec-2 family |
Epidermal surface antigen; ESA1Membrane component chromosome 17 surface marker 1; ESAchromosome 17, surface marker 1 (35kD protein identified bymonoclonal ECS-1); flotillin 2
Mass (kDA):
47.064 kDA
Human | |
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Location: | 17q11.2 |
Sequence: | 17; NC_000017.11 (28879339..28897733, complement) |
In skin, expressed in epidermis and epidermal appendages but not in dermis. Expressed in all layers of the epidermis except the basal layer. In hair follicles, expressed in the suprabasal layer but not the basal layer. Also expressed in melanoma and carcinoma cell lines, fibroblasts and foreskin melanocytes.
Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Endosome. Membrane; Lipid-anchor. Membrane-associated protein of caveolae.
A FLOT2 marker is a useful tool for research. A FLOT2 marker can be useful in many different applications. Many antibodies are available that can test for this protein. We will be discussing the validation and application of this marker in this article. We will also talk about its safety. We will discuss some of the most common applications of this protein. Let's get started.
Boster Bio provides an Anti-Flotillin 2/Flot2 Antibody which reacts to Human, Mouse, or Rat. This antibody can be obtained in PBS with 0.09% of sodium azide. A protein A column purification is used to purify it. It is made by immunizing rabbits with a synthetic protein peptide. The immunogen's length determines the price.
The flotillins Ludwig A and flotillin-2 have diverse functions. They regulate uropod production and neutrophil recruitment. Hazarika P and colleagues discovered that flotillin-2 was positively correlated with the level of ErbB2. The increased expression of flotillin-2 in breast cancer cell lines reduced the lung metastases in mouse models of the disease.
This protein could be associated in lymphatic metastasis of NPC. It may promote cell metastasis through interaction with Src. This intracellular signal transduction proteins can be used to stimulate it. In vitro and vivo, the protein promotes neurite cell growth. The level of HER2 protein in gastric carcinoma was also associated to flotillin-2 expression.
Three siRNAs against Flot2 sequences were designed and tested with Quantitative real-time PCR to validate them. The siRNAs did NOT affect the expression of EMT Maker or TGF-b receptor 1. The expression of other proteins, TGF-b, was not affected by silencing flot2.
The FLOT2 protein encodes Flotillin 2. Also known as ESA1 (or M17S1). The protein copurifies along with Flot1 & Caveolin-1. Li et al. Quantitative proteomic analyses revealed that FLOT2 had been identified in cultured neuronal stem cells from mice. The results revealed that FLOT2 is a useful marker to diagnose many types of brain cancers.
In addition, siRNA-mediated FLOT2 gene RNA-interference can inhibit cell proliferation and invasion in CRC cells. This research provides a scientific framework for clinical treatment. However, further work is required to determine whether siRNA-mediated FLOT2 inhibits CRC growth and metastasis. To this end, researchers used a silicon nanoparticle modified to contain PLL to study FLOT2 expression.
The elevated expression of Flot2 in tumor tissues is an independent prognostic factor. 181 NPC patients had shorter overall survival rates due to higher Flot2 levels. TGF-b's antimetastasis effects are significantly blocked by silencing Flot2. FLOT2 knockdown significantly inhibited Srcphosphorylation. E-cadherin, and the signal transducer, b-catenin were also reduced by Flot2-knockdown. It is possible that Flot2 may be an essential component of TGFb signaling and plays a significant role in NPC metastasis.
FLOT2 is a protein found on lipid-rafts in humans and plays an important part in maintaining their homeostasis. It regulates many processes. FLOT2 dysregulation can lead to dysregulations of lipidrafts. This in turn promotes downstream process that are connected to pathological conditions, such as cancer. FLOT2 upregulation in cancer cells promotes migratory andinvasive abilities.
High FLOT2 expression was associated to lower overall survival. In a study of 109 patients with advanced non-proliferative cancer, the association between FLOT2 and OS was also confirmed. Furthermore, patients with high levels of FLOT2 expression had a shorter OS than those with low levels. FLOT2 expression is a reliable marker that patients with advanced NPC will survive without any disease.
To confirm that FLOT2 is an accurate marker of neural differentiation, we used a cell culture method that detected Flot2 protein in the stroma of human multipotent stromal cells. After neural differentiation, Flot2 levels increased and were correlated with Octamer transcript factor-3, a marker for stem cells. In addition, we found that the FLOT2 protein is localized in plasma membrane and neurites and soma.
It is a candidate biomarker in CRC. However, it also suppresses the miR-33b-5p expression in NPC cells. These two factors together could provide a unique therapeutic target NPC. We propose that the FLOT2 marker be validated as an additional biomarker for this disease. We thank the authors for submitting this study to the journal. This research led to a new method to express FLOT2 in the human body.
Data regarding FLOT2 knockdown in NPC cell lines was previously published. We found that FLOT2 knockdown lowered BCAT1 expression, while FLOT2 ex-expression increased BCAT1 in 6-10B and NPC cells. Moreover, we also found that FLOT2 knockdown and overexpression of FLOT2 did not affect the expression of BCAT1. This study indicates that FLOT2 regulates BCAA metabolism.
The human FLOT2 genome encodes the protein flotillin-2. It is also known as reggie-1. This protein is abundantly distributed throughout the body, however it is missing from the skeletal muscular. It belongs to the flotillin group and consists of HflK/C, and the prohibitin heterology domain. Flotillin-2 acts as a functional component for cell-cell adhesion. This is an essential process for intestinal physiology.
Researchers have shown that Flot2 is colocalized with lipid raft markers in Neu and UD cells. Fyn, however, showed a scattered distribution in both cell types. Fyn colocalized both in UD and Neu cells with c–Src. CTB, Fyn, and CTB could also colocalize within neurites.
PMID: 8051082 by Schroeder W.T., et al. Cloning and characterization of a novel epidermal cell surface antigen (ESA).
PMID: 20682791 by Gorbea C., et al. A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components.