Recombinant Human FABP5 Protein
Beta LifeScience
SKU/CAT #: BLPSN-1955
Recombinant Human FABP5 Protein
Beta LifeScience
SKU/CAT #: BLPSN-1955
Collections: Other recombinant proteins, Recombinant proteins
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Tag | N/A |
Host Species | Human |
Accession | Q01469 |
Synonym | E-FABP, EFABP, KFABP, PA-FABP, PAFABP |
Background | Fatty acid-binding protein, also known as Epidermal-type fatty acid-binding protein, Fatty acid-binding protein 5, Psoriasis-associated fatty acid-binding protein homolog, E-FABP and FABP5, is a cytoplasm protein which Belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid-binding proteins ( FABPs ) are postulated to serve as lipid shuttles that solubilize hydrophobic fatty acids and deliver them to appropriate intracellular sites. E-FABP / FABP5 is predominantly expressed in keratinocytes and is overexpressed in the actively proliferating tissue characteristic of psoriasis and wound healing. E-FABP / FABP5 exhibits an important role in binding free fatty acids, as well as regulating lipid metabolism and transport. E-FABP / FABP5 has high specificity for fatty acids. It has highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity of FABP5. E-FABP / FABP5 may be involved in keratinocyte differentiation. |
Description | A DNA sequence encoding the human FABP5 (Q01469) (Met 1-Glu 135) was expressed and purified. |
Source | E.coli |
Predicted N Terminal | Met 1 |
AA Sequence | Met 1-Glu 135 |
Molecular Weight | The recombinant human FABP5 consisting of 135 a.a. and has a calculated molecular mass of 15.2 kDa as estimated in SDS-PAGE under reducing conditions. |
Purity | >92% as determined by SDS-PAGE |
Endotoxin | Please contact us for more information. |
Bioactivity | Please contact us for detailed information |
Formulation | Lyophilized from sterile 50mM Tris, pH 8.0. |
Stability | The recombinant proteins are stable for up to 1 year from date of receipt at -70°C. |
Usage | For Research Use Only |
Storage | Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
Target Details
Target Function | Intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids, that regulate the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors. Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation. May be involved in keratinocyte differentiation. |
Subcellular Location | Cytoplasm. Nucleus. Cell junction, synapse. Cell junction, synapse, postsynaptic density. Secreted. |
Protein Families | Calycin superfamily, Fatty-acid binding protein (FABP) family |
Database References | |
Tissue Specificity | Keratinocytes; highly expressed in psoriatic skin. Expressed in brain gray matter. |
Gene Functions References
- FABP5 promotes tumor angiogenesis via activation of the IL6/STAT3/VEGFA signaling pathway in hepatocellular carcinoma. PMID: 29957468
- FABP5 promotes lipolysis of lipid droplets, de novo fatty acid synthesis and activation of NF-kappaB signaling in cancer cells. PMID: 29906613
- Although FABP5 facilitates brain endothelial cell uptake of fatty acids, it has limited effects on brain endothelial cell uptake. PMID: 29247738
- Results show that circulating FABP5 is associated with decreased cholesterol efflux capacity (CEC) and carotid atherosclerosis, suggesting that FABP5 level is a regulatory factor of CEC and a potential biomarker for residual risk of atherosclerosis. PMID: 28303004
- the critical role of FABP5 in activating the TGF-beta signaling pathway during radiation-induced human skin fibrosis PMID: 29215326
- Study identified FABP5 to be involved in the progressive intestinal injury associated with the development of Crohn's Disease complications via their effects on intestinal innate immunity. PMID: 28490445
- Findings show that FABP5 expression is up-regulated in hepatocellular carcinoma (HCC), and provide evidence that that it could play a crucial role of tumor progression, invasion and metastasis in HCC through EMT induction. PMID: 28374947
- A high expression ratio between FABP5 and CRABPII may be related to CP tumor recurrence and ATRA could be a potential therapeutic agent for CP chemotherapy. PMID: 27418530
- Data suggest that antinociceptive agent SBFI-26 binds at a portal site as well as at the canonical site in the substrate pocket of FABP5 and FABP7; only the S form of SBFI-26 binds to both FABP5 and FABP7 in their co-crystal structures; SBFI-26 induces conformational changes in FABP5 and FABP7. PMID: 28632393
- FABP5 plays an important role in the carcinogenesis and metastasis of cervical cancer, and FABP5 may be a novel predictor for prognostic assessment of cervical cancer patients. PMID: 27644245
- FABP5 promoted VEGF expression and angiogenesis through PPARgamma which was activated by fatty acids transported by FABP5. PMID: 26814431
- FABP5 is associated with increased subclinical atherosclerosis PMID: 27055964
- the balance between FABP4 and FABP5 in endothelial cells may be important in regulation of angiogenic versus quiescent phenotypes in blood vessels. PMID: 26625874
- Long chain fatty acids suppress the oncogenic properties of FABP5-expressing carcinoma cells in cultured cells. PMID: 26592976
- silencing of Sp1, c-Myc or FABP5 expression led to a significant decrease in cell proliferation, indicating that up-regulation of FABP5 expression by Sp1 and c-Myc is critical for the proliferation of prostate cancer cells PMID: 26614767
- FABP5 may contribute to the airway remodeling and inflammation in asthma by fine-tuning the levels of CysLTs, which induce VEGF production. PMID: 26020772
- CRABP-II and FABP5 expression patterns are neither related to the tumor grades nor correlated with RA sensitivity. PMID: 25797252
- peripheral uptake of FA via capillary endothelial FABP4/5 is crucial for systemic metabolism and may establish FABP4/5 as potentially novel targets for the modulation of energy homeostasis. PMID: 24244493
- Data indicate that fatty acid-binding protein 5 (FABP5) is tuned to selectively stimulate peroxisome proliferation-activated receptor beta/delta transactivation in response to specific fatty acids based on their structural features. PMID: 24692551
- Both C-FABP and PPARg are suitable as prognostic factors to predict the clinical outcome of prostatic cancer patients. PMID: 24189640
- E-FABP showed high exp ression in NSCLC, and the increased E-FABP expression may involved in the occurrence and development of NSCLC PMID: 23327868
- Our findings establish that FABP5 is critical for mammary tumor development PMID: 23722546
- E-FABP is highly expressed in psoriatic epidermis, and it is mainly localized in stratum spinosum. Psoriatic keratinocytes overexpress E-FABP as compared to the same population in normal epidermis. PMID: 23528210
- FABP5 is significantly overexpressed in intrahepatic cholangiocarcinoma combined lymph node metastasis and is involved in cell proliferation and invasion PMID: 22825302
- E-FABP levels in skin-strippings, but not in serum, were higher in psoriatic patients than in healthy individuals. E-FABP was abundant in patients not only in lesions but also in uninvolved skin. PMID: 23039948
- The most significant discovery of the integrated validation is the down-regulation of FABP5 and PDCD4 in KRAS-activated human tumor bronchial epithelial cells. PMID: 22761399
- High FABP5 is associated with pancreatic ductal adenocarcinoma. PMID: 22010213
- Co-expression of E- and A-FABP is detected in cultured human aortic endothelial cells, which is the critical cellular component in the development of atherosclerosis. PMID: 20452069
- The purpose of this study was to investigate the clinicopathological significance of FABP5 in breast cancer and to evaluate FABP5 as a prognostic marker and a possible novel therapeutic target in breast cancer. PMID: 21356353
- These results validate the differential expressions of SOD2, S100A8 and FABP5 between mycosis fungoides tissues and normal skins. PMID: 20833513
- Overexpression of FABP5 in oral cancer cells increased cell proliferation and invasiveness by increasing expression of MMP-9. PMID: 20040021
- Fatty acid-binding protein 5 and PPARbeta/delta are critical mediators of epidermal growth factor receptor-induced carcinoma cell growth PMID: 20424164
- FABP5 plays a critical role in lipid metabolism in retinal pigment epithetlial cells; knockdown results in accumulation of cellular triglycerides, decreased cholesterol levels, and reduced secretion of apoB100 protein and lipoproteins PMID: 19434059
- FABP5 could be a regulated target of Nurr1. PMID: 19861119
- Solution structure and backbone dynamics PMID: 12049637
- S100A7 expression appears to stabilize epidermal fatty acid binding protein level in keratinocytes PMID: 12839573
- the overexpression of FABP in cultured senescent dermal microvascular endothelial cells is closely related to skin aging. PMID: 15335354
- Metastasis of squamous cell carcinoma of the oral tongue is associated with down-regulation of epidermal fatty acid binding protein (E-FABP). PMID: 16759896
- E-FABP may play a key role in the progress of invasiveness and metastasis in human breast cancer. PMID: 17428383
- study found levels of nuclear & cytoplasmic C-FABP expression in prostate cancer cells were significantly higher than those in normal & benign prostatic hyperplasia tissues & increased C-FABP was significantly associated with reduced patient survival time PMID: 18360704
- Results demonstrated the ubiquitous overexpressions of E-FABP and CAPS in EC and the correlations to the clinicopathologic parameters. CAPS might be a potential prognostic factor for survival in patients with endometrial cancer PMID: 18729184
- epidermal-fatty acid binding protein is upregulated in Human papillomavirus related oral squamous cell carcinoma PMID: 19337991
- fatty acid-binding protein-5, squamous cell carcinoma antigens 2, alpha-enolase, annexin II, apolipoprotein A-I and albumin were detected at a high level in Atopic dermatitis skin lesions, but scarcely in the normal controls PMID: 19339807