FABP5 Antibodies

Fatty acid-binding protein 5 (FABP5)

Intracellular carrier for long-chain fatty acids and related active lipids, like the endocannabinoid, that regulates the metabolism and activities of the ligands they bind. Along with the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they trigger nuclear receptors (PubMed:22170058).

Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; that promotes proliferation and survival. May also function as a synaptic provider of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling.

Gene Information

Human
Gene Name:	FABP5
Uniprot:	Q01469
Entrez:	2171

Family

Belongs to:
calycin superfamily

Alternative Names

EFABP; E-FABP; E-FABPPAFABP; FABP5; fatty acid binding protein 5 (psoriasis-associated); Fatty acid-binding protein 5; PA-FABPepidermal; Psoriasis-associated fatty acid-binding protein homolog

Molecular Weight

Mass (kDA):
15.164 kDA

Genomic Context

Human
Location:	8q21.13
Sequence:	8; NC_000008.11 (81280536..81284775)

Tissue Specificity

Keratinocytes; highly expressed in psoriatic skin.

Subcellular Localizations

Cytoplasm. Nucleus. Cell junction, synapse. Cell junction, synapse, postsynaptic density. Secreted. Localizes primarily to the cytoplasm. Upon certain ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into nucleus (PubMed:24692551). Secreted by astrocytes, but not by neurons (By similarity).

Diseases

• Fatty Liver
• Neoplasms
• Malignant Neoplasms
• Obesity
• Carcinoma
• Insulin Resistance
• Inflammation
• Diabetes Mellitus
• Malignant Squamous Cell Neoplasm
• Atherosclerosis
• Insulin Sensitivity
• Diabetes Mellitus, Non-insulin-dependent
• Nervousness

• Psoriasis
• Cell Transformation, Neoplastic
• Malignant Paraganglionic Neoplasm
• Neoplasm Metastasis
• Cell Invasion
• Intestinal Schistosomiasis
• Skin Neoplasms

Pathways

• Transport
• Localization
• Cell Growth
• Lipid Binding
• Secretion
• Cell Differentiation
• Cell Proliferation
• Fatty Acid Transport
• Pathogenesis
• Cytokine Production
• Regulation Of Gene Expression
• Cellular Localization
• Immune Response

• Neurogenesis
• Fatty Acid Oxidation
• Rna Interference
• Cell Cycle
• Keratinocyte Differentiation
• Phagocytosis
• Lipid Homeostasis

PTMs

• Phosphorylation
• Oxidation
• Acetylation
• Methylation
• Cleavage
• Carboxylation

• Biotinylation
• Reduction
• Phosphorothioation
• Glycosylation
• Ubiquitination
• Iodination

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/FABP5

The Boster Bio: Best Uses Of The FABP5 Marker

You've come to the right spot for those who want to know more about FABP5. This article will provide you with an information about the marker, its clinical applications as well as current research. We'll also touch on future directions for FABP5 research. Read on to learn more! This article will assist you in establishing your own FABP5 immunoassays. The Boster Bio: Best Uses Of The FABP5 Marker

Information about FABP5.

A number of recent studies have revealed that FABP5 is involved in the regulation of airway epithelial cell (AEC) migration and invasion. FABP5 and FASN both work together to increase the metastatic potential of LNCaP cell. In order to investigate whether FABP5 and FASN are involved in this manner we employed the previously mentioned lentiviral constructs. These lentiviral structures comprised human FABP5 as well as human.

FABP5 is an important inhibitor of Il-17aexpression , which is responsible for TH27 polarization within AM. Furthermore, FABP5 reduces the expression of IL-17a, which is a key cytokine for proinflammatory purposes. The results of the study could also lead to an entirely new approach to treating PH. This study has many implications for the treatment and diagnosis of this disease. The findings could help predict how patients will progress from the beginning until the end of the disease.

FABP5 is also involved in pulmonary blood vessel remodeling that is a hallmark of PH–LHD. Incredibly, inhibition of FABP5 in animal models of PHLD reduced the pulmonary vascular remodelling. This suggests that therapy for reducing PH-LHD could target FABP5. Further, these results were confirmed in an animal model of PH-LHD with the FABP5 antagonist SBFI-26. Western blots were employed to test the results.

A new study conducted in mice found that FABP5 inhibits PCa metastasis via binding to enzymes that metabolize lipids, referred to as PPARg. Thus, inhibiting FABP5 would effectively suppress PCa metastasis. However, FABP5 inhibition may not be a successful treatment for metastatic PCa. This study has implications for cancer research. It's an exciting new direction in treatment.

As a crucial player in the skin barrier, FABP5 modulates fatty acid transport and uptake. It also aids in the establishment of the skin barrier. FABP5 expression is increased in patients with psoriasis. This is associated with abnormal differentiation and hyperproliferation. Additionally, it has been linked to AD by mass spectrometry. It is also a key component in the inflammatory reaction and metabolism of lipids.

Clinical applications

The FABP5 gene was first discovered in cancer tissue samples in 2001. There are a variety of cancers that the FABP gene is found in. Three of the most commonly encountered forms are prostate, breast and renal carcinomas. This marker can be used in diagnostic and prognostic situations. In a recent study the FABP5 gene was found in 129 urological carcinomas. However, it is important to note that FABP protein expression patterns differ from cell line to cell culture.

FABP5 expression was associated with ccRCC and other normal tissues. There were strong associations between FABP5 mRNA and prognostic factors. In vitro studies indicated that FABP5 expression was linked to an increase in cell viability and movement in HUVECs, and decreased IL6/STAT3/VEGFA signalsing. Tumor angiogenesis was also inhibited by FABP5 downregulation.

FABP5 is also an important factor for lymph node metastasis. In cervical cancer, FABP5 promotes tumor cell growth. FABP5 gene silencing in hepatocellular cancer decreased cell growth. FABP5 could have an impact on cells of ccRCC via the PI3K/AKT pathway. Therefore, FABP5 could provide an interesting perspective on the biology of tumors.

FABP5 is present in a variety of kinds and varieties of human cancers. It is also overexpressed in a variety of cancer types. Its promoter region includes a typical CpG islands, hypomethylation of which contributes in the increase of. The significant reduction in cell proliferation was achieved by silencing FABP5. FABP5 is also essential for cancer-causing potential, malignant progression and the growth of prostate cancer cells.

Cell viability has increased by exogenous FABP5 expression in 786O cells as well as Caki-1 cells. Treatment with LY294002 decreases the viability of cells FABP5-overexpressing cells. In a different study, FABP5 overexpression decreased cell viability. In the same study, LY294002 decreased cell viability in the group LV-FABP5. In both instances FABP5 was expressed in excess and was associated with higher expression of p–AKT.

FABP5 is produced by cells and then released into the blood. Although the mechanism by the production of FABP5 is not fully understood however, it has been linked to a variety of metabolic syndrome components, including coronary artery disease and carotid. Therefore, it is vital to identify the exact mechanism behind the action of FABP5. The discovery of FABP5 could be a catalyst for the development of new therapies.

Current research

In prostate cancer, dysregulated lipid signaling is implicated in the upregulation of protumoral gene expression, and fatty acid-binding proteins (FABPs) are involved in transporting fatty acids to the PPARs. Recent research has demonstrated that silencing FABP5 in vivo slows the growth of tumors and also reduces cell growth. It has been shown that FABP5 can be used to inhibit metastasis and growth of tumors and that it could be synergistically used with taxanes.

FABP5 is a tumor-specific marker. It may also be a biomarker of CCa. However further research is required to determine if it is a biomarker for high-GS prostate cancer. To validate this marker's existence further studies of a larger scale are needed. The future of FABP5 is still unclear. It is essential to remain open-minded.

Researchers have found that the expression of FABP5 is higher in CCa cells derived from metastatic and primary sites. FABP5-overexpression can also increase the invasiveness of ccRCC cells. A recent study conducted by the University of California, Berkeley and Harvard Medical School found that FABP5-RNAi reduced the PC3-Luc cell's migration. However, overexpression of FASN, MAGL, or FAGL boosts the metastatic potential of PC3 cells.

Recent studies have also shown that FABP5 silencing does not inhibit invasion and migration of ccRCC or gastric cancer cells. Future studies are required to investigate the effects of FABP5 on the progression of cell cycles and cell proliferation, as well as colony formation. Future studies will investigate the possible connection between FABP5 as well as phosphorylated AKT. These studies are an essential component of cancer research.

The molecular characterization of the FABP5 gene has revealed that FABP5 is involved in lipid-mediated metastasis. It is also believed that FABP5 might be a novel target for chemotherapy. Its function is not fully understood even though it is a significant. The FABP5 gene product has been linked with the progression of cancer and could act as a marker for diagnosis. In addition, it may be a way to determine which agents are effective in suppressing PCa metastasis.

Future directions

We have previously demonstrated that FABP5 is localized to lung tissue, airway epithelial cell cells, and fibroblasts. We also demonstrated that the expression of FABP5 is associated with survival rates. Future directions for the FABP5 marker include analyzing its role in tumorgenesis and determining its effect on patient outcomes. To achieve these goals, we synthesized a lentiviral construct expressing FABP5.

FABP5 is responsible for translocating exogenous fatty acids into nuclear PPAR. Thus, FABP5 inhibitors would inhibit PCa metastasis caused by lipids. FABP5 inhibition could also be a druggable element of the PCa lipid signaling. More research is required in this area to establish its role as a metastasis mediated by lipids.

Recent studies have proven that FABP5 is a potential diagnostic and therapeutic marker for CCa. The International Agency for Research on Cancer and the United States National Cancer Institute have convened a panel with experts to discuss the future of ovarian cancer research. Although serum FABP5 isn't a cancer marker, it plays a crucial role in the patient's prognosis. The protein is a complement to the function of the endogenous FABP5 in HCC cells. This biomarker is not linked with treatment success. The panel also found that young HCC patients had a poor prognosis because of altered gene expression.

We also discovered that FABP5 overexpression increased the proportion of proliferating Caki-1 and 786O cell lines, which suggests that FABP5 is a novel biomarker of IL-17A's expression. These findings could provide new insights into how IL-17A can be expressed in AD, and can lead to new therapies for the disease. We are also planning to study the possible role of FABP5 in the regulation of TH27 polarization in AD.

The FABP5 gene silencing technique slowed the growth of human gastric cancer cells, which could be a biomarker for lymph node metastasis. Additionally, it slowed the growth of cervical cancer cells once silenced. Our study also showed that FABP5 interferes with PI3K/AKT pathways, which gives us an entirely new understanding of tumor biology. These findings suggest the possibility for the use in clinical trials of FABP5 in patients suffering from ccRCC.