Recombinant Human FABP5 Protein

Beta LifeScience SKU/CAT #: BLPSN-1955

Recombinant Human FABP5 Protein

Beta LifeScience SKU/CAT #: BLPSN-1955
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Product Overview

Tag N/A
Host Species Human
Accession Q01469
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

  1. FABP5 promotes tumor angiogenesis via activation of the IL6/STAT3/VEGFA signaling pathway in hepatocellular carcinoma. PMID: 29957468
  2. FABP5 promotes lipolysis of lipid droplets, de novo fatty acid synthesis and activation of NF-kappaB signaling in cancer cells. PMID: 29906613
  3. Although FABP5 facilitates brain endothelial cell uptake of fatty acids, it has limited effects on brain endothelial cell uptake. PMID: 29247738
  4. 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
  5. the critical role of FABP5 in activating the TGF-beta signaling pathway during radiation-induced human skin fibrosis PMID: 29215326
  6. 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
  7. 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
  8. 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
  9. 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
  10. 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
  11. FABP5 promoted VEGF expression and angiogenesis through PPARgamma which was activated by fatty acids transported by FABP5. PMID: 26814431
  12. FABP5 is associated with increased subclinical atherosclerosis PMID: 27055964
  13. the balance between FABP4 and FABP5 in endothelial cells may be important in regulation of angiogenic versus quiescent phenotypes in blood vessels. PMID: 26625874
  14. Long chain fatty acids suppress the oncogenic properties of FABP5-expressing carcinoma cells in cultured cells. PMID: 26592976
  15. 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
  16. FABP5 may contribute to the airway remodeling and inflammation in asthma by fine-tuning the levels of CysLTs, which induce VEGF production. PMID: 26020772
  17. CRABP-II and FABP5 expression patterns are neither related to the tumor grades nor correlated with RA sensitivity. PMID: 25797252
  18. 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
  19. 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
  20. Both C-FABP and PPARg are suitable as prognostic factors to predict the clinical outcome of prostatic cancer patients. PMID: 24189640
  21. 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
  22. Our findings establish that FABP5 is critical for mammary tumor development PMID: 23722546
  23. 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
  24. FABP5 is significantly overexpressed in intrahepatic cholangiocarcinoma combined lymph node metastasis and is involved in cell proliferation and invasion PMID: 22825302
  25. 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
  26. 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
  27. High FABP5 is associated with pancreatic ductal adenocarcinoma. PMID: 22010213
  28. 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
  29. 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
  30. These results validate the differential expressions of SOD2, S100A8 and FABP5 between mycosis fungoides tissues and normal skins. PMID: 20833513
  31. Overexpression of FABP5 in oral cancer cells increased cell proliferation and invasiveness by increasing expression of MMP-9. PMID: 20040021
  32. Fatty acid-binding protein 5 and PPARbeta/delta are critical mediators of epidermal growth factor receptor-induced carcinoma cell growth PMID: 20424164
  33. 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
  34. FABP5 could be a regulated target of Nurr1. PMID: 19861119
  35. Solution structure and backbone dynamics PMID: 12049637
  36. S100A7 expression appears to stabilize epidermal fatty acid binding protein level in keratinocytes PMID: 12839573
  37. the overexpression of FABP in cultured senescent dermal microvascular endothelial cells is closely related to skin aging. PMID: 15335354
  38. Metastasis of squamous cell carcinoma of the oral tongue is associated with down-regulation of epidermal fatty acid binding protein (E-FABP). PMID: 16759896
  39. E-FABP may play a key role in the progress of invasiveness and metastasis in human breast cancer. PMID: 17428383
  40. 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
  41. 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
  42. epidermal-fatty acid binding protein is upregulated in Human papillomavirus related oral squamous cell carcinoma PMID: 19337991
  43. 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


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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.

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