Recombinant Human FABP5 Protein (N-6His)

Name: Recombinant Human FABP5 Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-0339NP
Availability: InStock

BL-0339NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other 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.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Fatty Acid-Binding Protein 5 is produced by our E.coli expression system and the target gene encoding Ala2-Glu135 is expressed with a 6His tag at the N-terminus.
Accession	Q01469
Synonym	Fatty Acid-Binding Protein Epidermal; Epidermal-Type Fatty Acid-Binding Protein; E-FABP; Fatty Acid-Binding Protein 5; Psoriasis-Associated Fatty Acid-Binding Protein Homolog; PA-FABP; FABP5
Gene Background	Fatty acid-binding protein 5 (FABP5) is a cytoplasm protein that belongs to the fatty-acid binding protein (FABP) family of calycin superfamily. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids. FABP5 can be expressed in keratinocytes, and is highly expressed in psoriatic skin. FABP5 has been shown to be involved in keratinocyte differentiation. FABP5 has high specificity for fatty acids, the highest affinity for C18 chain length. FABP5 can decrease the chain length or introduce double bonds to reduce the affinity.
Molecular Mass	17.33 KDa
Apmol Mass	16 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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	HGNC: 3560 OMIM: 605168 KEGG: hsa:2171 STRING: 9606.ENSP00000297258 UniGene: 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

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.