Recombinant Human FABP1 Protein (N-6His)

Name: Recombinant Human FABP1 Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-0335NP
Availability: InStock

BL-0335NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Fatty Acid-Binding Protein 1 is produced by our E.coli expression system and the target gene encoding Met1-Ile127 is expressed with a 6His tag at the N-terminus.
Accession	P07148
Synonym	Fatty Acid-Binding Protein Liver; Fatty Acid-Binding Protein 1; Liver-Type Fatty Acid-Binding Protein; L-FABP; FABP1; FABPL
Gene Background	Human Fatty Acid-Binding Protein 1 (FABP1) is a cytoplasm protein, which belongs to the calycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids. FABP1 forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. FABP1 can bind free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm, so it can be involved in intracellular lipid transport.
Molecular Mass	16.37 KDa
Apmol Mass	15 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 0.5M Argine, 50% Glycerol, 2mM EDTA, 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
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes. Binds cholesterol. Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport.
Subcellular Location	Cytoplasm.
Protein Families	Calycin superfamily, Fatty-acid binding protein (FABP) family
Database References	HGNC: 3555 OMIM: 134650 KEGG: hsa:2168 STRING: 9606.ENSP00000295834 UniGene: PMID: 27761670 Both peak oxygen consumption and grip strength were inversely associated with urinary L-FABP levels in middle-aged and older individuals without chronic kidney disease. PMID: 28197733 Nonrenal conditions and systemic severity should be considered for improved AKI prediction by NGAL and L-FABP as biomarkers. PMID: 27605390 urine L-FABP/C is permanently elevated in chronic kidney disease patients. PMID: 28745927 Our data suggests that the polymorphism in genes IL-1beta, IL-1Ra and FABP1 included in this study are not associated with PCOS development, but can influence important biochemical and metabolic parameters in PCOS. PMID: 28405733 On PICU day 1, interleukin-18 predicted acute kidney injury with area under the curve=0.82, but neutrophil gelatinase-associated lipocalin and liver fatty acid binding protein predicted acute kidney injury with area under the curve of less than or equal to 0.69; on PICU day 2, area under the curve was higher. Interleukin-18 and liver fatty acid binding protein on day 1 predicted prolonged acute kidney injury. PMID: 28430754 In total, 68 miRNAs potentially targeting FABP1 were selected; of these, miR-3941, miR-4517, and miR-4672 directly targeted the FABP1 3' untranslated region. Mimics of the three miRNAs substantially repressed FABP1 expression at translational level and led to HepG2 cell resistance to steatosis and cell injury induced by free fatty acids mixture, which rescue of FABP1 overexpression reversed. PMID: 29258109 This study demonstrated that the loss of FABP1 expression is associated with MSI carcinomas and that interferon gamma stimulation plays a role in this process via its interaction with PPARgamma. PMID: 27687006 Hepatic adenomas co-occurring with fibrolamellar carcinomas show LFABP loss and are negative for PRKACA rearrangements, indicating they are genetically distinct lesions. These data also demonstrate that LFABP loss, which characterizes HNF1-alpha inactivation, is a consistent feature of fibrolamellar carcinoma, indicating HNF1-alpha inactivation is an important event in fibrolamellar carcinoma pathogenesis. PMID: 27015136 studies indicate that FABP1 is essential for proper lipid metabolism in differentiated enterocytes, particularly concerning fatty acids uptake and its basolateral secretion. PMID: 28919479 CDH5 and FABP1 expression levels were both elevated in drug-induced liver injury. PMID: 27224670 A high resolution NMR comparative molecular analysis of L-FABP T94T and L-FABP T94A in their unbound states and in the presence of representative ligands of the fatty acid and bile acid classes showed that threonine to alanine replacement did not result in strongly perturbed structural and dynamic features, although differences in oleic acid binding by the two variants were detected. PMID: 28668637 Studies show that despite overall tertiary structure similarity, the hFABP1 differs significantly from rat FABP1 in secondary structure, much larger ligand binding cavity, and affinities/specificities for some ligands. Moreover, while both mouse and hFABP1 mediate ligand induction of PPARA, they differ markedly in genes induced. hFABP1 T94A variant is associated with altered body mass index.[review] PMID: 27117865 analysis of structural, dynamic, and binding properties of the liver fatty acid binding protein (LFABP) in crowded solutions PMID: 27457417 Urinary L-FABP, NGAL, Kim-1 and albumin levels increased during the acute phase of kidney injury and were significantly correlated with the degree of tubulointerstitial fibrosis during the chronic phase. These markers could detect higher risk of progression to CKD. PMID: 27028054 L-FABP was found to associate with VEGFR2 on membrane rafts and subsequently activate the Akt/mTOR/P70S6K/4EBP1 and Src/FAK/cdc42 pathways, which resulted in up-regulation of VEGF-A accompanied by an increase in both angiogenic potential and migration activity. L-FABP significantly promoted tumor growth and metastasis in a xenograft mouse model. PMID: 26919097 In chronic kidney disease, high urinary L-FABP correlated with the development of end-stage renal disease and cardiovascular disease. PMID: 26189083 In the association of SNPs in FABP1 gene with PCOS, rs2197076 was more closely associated with its main features than rs2241883 and seemed to play a more important role in the pathogenesis of PCOS. PMID: 26650609 Report interaction of perfluoroalkyl acids with human liver fatty acid-binding protein. PMID: 25370009 Urinary L-FABP appears to be a sensitive biomarker of acute kidney injury in patients undergoing abdominal aortic repair. PMID: 26585768 Urinary levels of NGAL are more sensitive than uKIM-1 and uL-FABP levels in predicting renal scarring in vesicoureteral reflux. PMID: 26324091 Loss of staining for LFABP appears to be common in hepatocellular carcinoma and may be seen in well-differentiated hepatocellular carcinoma. PMID: 26997447 In this study, the effects of hepatitis B virus X protein (HBx) mediated FABP1 regulation on hepatic steatosis and the underlying mechanism were determined. PMID: 26637457 compared with the rs2919872 G allele, the rs2919872 A allele reduces the transcriptional activity of FABP1 promoter, and thereby may link FABP1 gene variation to triglyceride level in humans. PMID: 26439934 Higher urinary L-FABP was found in pregnant with and without gestational diabetes mellitus(GDM), and considerably higher urinary L-FABP was found in the GDM group compared with the non-GDM group. PMID: 26254248 Multivariable regression analysis revealed that urinary L-FABP and urinary albumin/ creatinine ratio were significantly associated with urinary ACE2 levels. PMID: 26067610 Measurement of uL-FABP levels at 48 h after coronary angiography may be useful in detecting renal damage, and in predicting 1-year renal outcome in ischemic heart disease patients undergoing CAG. PMID: 24554034 Measurement of urinary L-FABP and albumin/creatinine ratio should be useful to assess cardiovascular damage reflecting the elevation of cardiac markers and ECG abnormalities in T2DM with CKD. PMID: 24626813 Urinary L-FABP is strongly associated with anemia in non-diabetic patients. PMID: 26010898 L-FABP is a novel biomarker of diverse kidney diseases. (Review) PMID: 25797895 I-FABP and L-FABP are early markers for abdominal injury with limited prognostic value for secondary organ failures in the post-traumatic course PMID: 25324448 Both the MTP I128T and the L-FABP T94A polymorphisms can affect serum lipid levels in the Chinese population. PMID: 25663234 The study investigates the interaction of L-FAB with phospholipid liposomes. PMID: 25198387 The human FABP1 T94A variant protein had 3-fold higher cholesterol-binding affinity than the WT FABP1. PMID: 25732850 In smaller HCC, L-FABP downregulation probably occurs because of phenotypic changes during tumor progression. Moreover, this downregulation correlated with tumor differentiation and intratumoral inflammation. PMID: 25516669 FABP1 and FABP2 have roles in differentially modulating the activation of PPARalpha in a ligand-selective manner PMID: 25847235 Maternal serum LFABP level appears to be correlated with the severity of the preeclampsia and can be used to confirm the diagnosis. PMID: 25399315 Data suggest that up-regulation of urinary levels of LFABP, KIM1 (kidney injury molecule 1), and NGAL (neutrophil gelatinase associated lipocalin) can be used as biomarkers to reflect tubular dysfunction in early-stage type 2 diabetic nephropathy. PMID: 24687388 There is not a significant association between the FABP1 polymorphisms and aspirin-exacerbated respiratory disease(AERD). PMID: 25338211 Urinary L-FABP was an accurate predictor of early renal allograft function. PMID: 25027586 Increased serum L-FABP levels are associated with delayed graft function. PMID: 24750195 Baseline urinary L-FABP levels can be a predictor for occurrence of contrast-induced kidney disease. PMID: 23604313 L-FABP was downregulated in hepatocellular carcinoma and was associated with poor prognosis. PMID: 25436304 It has investigated the interaction between human L-FABP and the soluble domain of Plasmodium falciparum UIS3 by NMR spectroscopy. PMID: 23169100 NGAL, IL-18, KIM-1, L-FABP, and albumin differed between etiologies and were significantly higher in patients adjudicated with acute kidney injury. PMID: 24375576 Human FABP1 T94A variant impacts fatty acid metabolism and PPAR-alpha activation in cultured human female hepatocytes. PMID: 24875102 although the T94A substitution did not alter the affinity of human L-FABP for long chain fatty acids, it significantly altered human L-FABP structure and stability PMID: 24628888 Data suggest that an SNP in FABP1 (T94A) does not alter affinity of FABP1 for PPARalpha agonists (fibrates); this SNP does alter FABP1 secondary structure, stability, and functional response to fibrates (gene expression up-regulation in hepatocytes). PMID: 24299557 L-FABP was not significantly associated with acute kidney injury in adults or children after adjusting for other kidney injury biomarkers (neutrophil gelatinase-associated lipocalin and IL-18). PMID: 23599408 MS and NMR were used to study the ligand binding of human liver fatty acid binding protein. Results are consistent for 2 binding sites with different affinity; results indicate a higher affinity for oleate relative to palmitate at each binding site. PMID: 23893635

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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.

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