Recombinant Mouse Fatty Acid-Binding Protein, Liver Protein (FABP1), Active

Name: Recombinant Mouse Fatty Acid-Binding Protein, Liver Protein (FABP1), Active
Brand: Beta LifeScience
SKU: BLC-05669P
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Fatty Acid-Binding Protein, Liver Protein (FABP1), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 95% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The binding affinity of rMuFABP1 for the synthetic ligand cis-parinaric acid has been measured by fluorescence titration. Half maximal fluorescence of 2.5 μM rMuFABP1 is achieved with approximately 5 μM cis-paranaric acid.
Uniprotkb	P12710
Target Symbol	FABP1
Synonyms	Fabp1; FabplFatty acid-binding protein; liver; 14 kDa selenium-binding protein; Fatty acid-binding protein 1; Liver-type fatty acid-binding protein; L-FABP
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	MNFSGKYQLQ SQENFEPFMK AIGLPEDLIQ KGKDIKGVSE IVHEGKKIKL TITYGPKVVR NEFTLGEECE LETMTGEKVK AVVKLEGDNK MVTTFKGIKS VTELNGDTIT NTMTLGDIVY KRVSKRI
Expression Range	1-127aa
Protein Length	Full Length
Mol. Weight	14.2 kDa
Research Area	Signal Transduction
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 2 trehalose
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	KEGG: mmu:14080 STRING: 10090.ENSMUSP00000064655 UniGene: PMID: 28972119 Ablating both Fabp1 and Scp2/Scpx (TKO) induces hepatic phospholipid and cholesterol accumulation in high fat-fed mice PMID: 29307784 role of Fabp1/Scp-2 in hepatic phytol metabolism PMID: 28411199 Individually ablating SCPx or SCP2/SCPx elicited concomitant upregulation of L-FABP. PMID: 27940000 Lack of a significant decrease in the flux of HDL-[(3)H]CE to biliary FC or bile acids in FABP1(-/-) mice indicates the likely compensation of its function by an as yet unidentified mechanism. Taken together, these studies demonstrate that FABP1 and SCP2 facilitate the preferential movement of HDL-CEs to bile for final elimination PMID: 27381048 data showed that Fabp1 gene ablation markedly diminished the impact of high-fat diet on brain endocannabinoid levels, especially in male mice PMID: 27861894 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. PMID: 27117865 FABP1 knockout increased brain levels of arachidonic acid-containing endocannabinoids PMID: 27167970 L-FABP was more important in hepatic retention of bile acids, while SCP-2/SCP-x more broadly affected biliary bile acid and phospholipid levels. PMID: 26541319 These findings suggest that some of the phenotypic divergence between the two L-Fabp(-/-) lines may reflect unanticipated differences in genetic background, underscoring the importance of genetic background in phenotypic characterization. PMID: 26251469 Loss of L-FABP and SCP-2, or both induces hepatic lipid accumulation in female mice and mimics non-alcoholic fatty liver disease. PMID: 26116377 attenuates tubulointerstitial damage in aldosterone-induced nephropathy by reducing oxidative stress PMID: 25339700 L-FABP appears to function more in hepatic retention of bile acids as well as hepatic uptake and biliary secretion of HDL-cholesterol PMID: 25277800 L-FABP is not required to channel ATGL-hydrolyzed FAs to mitochondria for beta-oxidation or the nucleus for PPAR-alpha regulation PMID: 24610891 Data show that combined deletion of microsomal triglyceride transfer protein (Mttp) and liver fatty acid binding protein 1 (L-Fabp) are protected from lithogenic diet (LD)-induced gallstone formation. PMID: 24474819 L-Fabp has a role in modifying intestinal fatty acid composition and adenoma formation in ApcMin/+ mice PMID: 23921281 The maximum increase in LFABP expression occurs when stimulation with IL-6 and PPARalpha-ligands takes place simultaneously. PMID: 23534555 liver-type fatty acid-binding protein in the proximal tubules may protect against angiotensin II-induced SSHT by attenuating activation of the intrarenal renin-angiotensin system and reducing oxidative stress and tubulointerstitial inflammation. PMID: 23940201 These data establish that L-FABP is an indirect antioxidant protein essential for sequestering FFA and that its impairment could contribute to in the pathogenesis of alcoholic liver disease . PMID: 23359610 CrPic exhibited amelioration alloxan induced oxidative stress in mouse livers. A significant increase in liver fatty acid-binding protein (L-FABP) was observed, which indicates increased fatty acid utilization in liver tissue PMID: 23603011 Liver-type fatty acid-binding protein gene-ablation exacerbated diet-induced weight gain and fat tissue mass gain in mice fed high-fat diet. PMID: 23539345 L-FABP deletion attenuates both diet-induced hepatic steatosis and fibrogenesis, despite the observation that L-Fabp paradoxically promotes fatty acid and lipid droplet accumulation and inhibits hepatic stellate cell activation in vitro. PMID: 23401290 L-FABP's importance in fibrate-induction of hepatic PPARalpha LCFA beta-oxidative genes, especially in the context of high glucose levels. PMID: 23747828 Aged female L-Fabp-/- mice are protected against weight gain and hepatic steatosis. PMID: 22327204 liver fatty acid-binding protein, the single most prevalent hepatic cytosolic protein that binds cholesterol, was upregulated twofold in SCP-2 null hepatocytes PMID: 22241858 L-FABP gene ablation decreased fat oxidation and sensitized all mice to weight gain as whole body fat tissue mass (FTM) and LTM-with the most gain observed in FTM of control vs high-fat fed female L-FABP null mice. PMID: 20035485 enhanced uptake and intracellular targeting of long and medium chain fatty acids to the nucleus PMID: 12023965 L-FABP is an important determinant of hepatic lipid composition and turnover PMID: 12670956 data point to an inducible defect in fatty acid utilization in fasted L-Fabp-/- mice that involves targeting of substrate for use in triglyceride metabolism PMID: 14534295 under fasting conditions, hepatic L-FABP contributes to hepatic long chain fatty acid oxidation and ketogenesis by a nontranscriptional mechanism, whereas L-FABP can activate ketogenic gene expression in fed mice PMID: 14656998 L-FABP may function as a carrier for selectively enhancing the distribution of long-chain fatty acyl CoA (LCFA-CoA), as well as LCFA, to nuclei for potential interaction with nuclear receptors. PMID: 14992586 results with cultured primary hepatocytes isolated from L-FABP (+/+) and L-FABP (-/-) mice demonstrated a physiological role of L-FABP in the uptake and metabolism of branched-chain fatty acids PMID: 15155724 gene expression of liver-type FABP was independent of PPARalpha and may have general implications for the activation of PPARgamma in alveolar macrophages PMID: 15203117 Data show that liver fatty acid protein gene ablation exerts a significant role, especially in female mice, in branched-chain fatty acid metabolism. PMID: 15692150 results suggesting a physiological role for the major cytosolic bile acid-binding protein (L-FABP) in influencing liver bile metabolic phenotype and gall-bladder bile lipids of male mice, especially in response to dietary cholesterol PMID: 15984932 L-FABP is involved in the physiological regulation of cholesterol metabolism, body weight gain, and obesity. PMID: 16123197 reducing both L-FABP and microsomal triglyceride transfer protein is an effective means to reduce very low density lipoprotein secretion without causing hepatic steatosis PMID: 16950764 Inactivation of Gata4 or Hnf1alpha had a partial effect (approximately 50% reduction) on Fabp1 gene expression during cytodifferentiation and suckling. PMID: 17272516 L-FABP can select cargo for and bud PCTV from intestinal ER membranes PMID: 17449472 inhibition of CYP2E1 and regulation of L-FABP by Platycodi radix play an important role in alcohol-induced hepatoprotection PMID: 17587688 L-Fabp(-/-) mice are protected against Western diet-induced obesity and hepatic steatosis. PMID: 18032478 Knockout female C57BL mice exhibit increased obesity in aging. PMID: 18806093 expression of renal hL-FABP was upregulated in the diabetic Tg mice and protective against tubulointerstitial damage of diabetic nephropathy PMID: 18854419 role for L-FABP as an important physiological regulator of PPARalpha PMID: 19104910 Together these data indicate a role for L-FABP in intestinal trafficking of both saturated (SFA),and cholesterol. PMID: 19116776 Data suggest that changes in hepatic cholesterol metabolism and biliary lipid secretion as well as changes in enterohepatic BA metabolism increase gallstone susceptibility in LD fed L-Fabp(-/-) mice. PMID: 19136665 studies support the hypothesis that L-FABP may facilitate ligand (LCFA)-activated PPARalpha transcriptional activity at least in part by increasing total LCFA ligand available to PPARalpha PMID: 19285478 studies consistent with L-FABP regulating PPARalpha transcriptional activity in hepatocytes through direct interaction with PPARalpha; findings suggest role for L-FABP interaction with PPARalpha in long chain fatty acid metabolism PMID: 19289416 renal expression and urinary excretion of hL-FABP significantly reflected the severity of tubulointerstitial damage in FA-induced nephropathy. PMID: 19435794 Data support the hypothesis that L-FABP plays a role in physiological regulation of not only hepatic fatty acid metabolism, but also that of hepatic cholesterol. PMID: 19815623

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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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