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Recombinant Mouse FABP4 cell lysate

Cat.No. : FABP4-2379MCL
Product Overview : Mouse FABP4 / ALBP derived in Human Cells. The whole cell lysate is provided in 1X Sample Buffer.Browse all transfected cell lysate positive controls
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Source : Human cells
Species : Mouse
Preparation method : Transfected cells were cultured for 48hrs before collection. The cells were lysed in modified RIPA buffer with cocktail of protease inhibitors. Cell debris was removed by centrifugation and then centrifuged to clarify the lysate. The cell lysate was boiled for 5 minutes in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 5% b-mercaptoethanol, and lyophilized.
Lysis buffer : Modified RIPA Lysis Buffer: 50 mM Tris-HCl pH 7.4, 150 mM NaCl, 1mM EDTA, 1% Triton X-100, 0.1% SDS, 1% Sodium deoxycholate, 1mM PMSF
Quality control Testing : 12.5% SDS-PAGE Stained with Coomassie Blue
Recommended Usage : 1. Centrifuge the tube for a few seconds and ensure the pellet at the bottom of the tube.2. Re-dissolve the pellet using 200μL pure water and boiled for 2-5 min.3. Store it at -80°C. Recommend to aliquot the cell lysate into smaller quantities for optimal storage. Avoid repeated freeze-thaw cycles.Notes:The lysate is ready to load on SDS-PAGE for Western blot application. If dissociating conditions are required, add reducing agent prior to heating.
Stability : Samples are stable for up to twelve months from date of receipt at -80°C
Storage Buffer : 50 mM Tris-HCl pH 7.4, 150 mM NaCl, 1mM EDTA, 1% Triton X-100, 0.1% SDS, 1% Sodium deoxycholate, 1mM PMSF
Storage Instruction : Lysate samples are stable for 12 months from date of receipt when stored at -80°C. Avoid repeated freeze-thaw cycles. Prior to SDS-PAGE fractionation, boil the lysate for 5 minutes.
Tag : Non
Gene Name : Fabp4 fatty acid binding protein 4, adipocyte [ Mus musculus ]
Official Symbol : FABP4
Synonyms : FABP4; fatty acid binding protein 4, adipocyte; fatty acid-binding protein, adipocyte; P15; ALBP; AFABP; A-FABP; protein 422; P2 adipocyte protein; adipocyte protein aP2; myelin P2 protein homolog; 3T3-L1 lipid-binding protein; fatty acid-binding protein 4; adipocyte lipid-binding protein; adipocyte-type fatty acid-binding protein; Ap2; Lbpl; 422/aP2; ALBP/Ap2;
Gene ID : 11770
mRNA Refseq : NM_024406
Protein Refseq : NP_077717
Pathway : Adipogenesis, organism-specific biosystem; Developmental Biology, organism-specific biosystem; Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis, organism-specific biosystem; Lipid digestion, mobilization, and transport, organism-specific biosystem; Metabolism, organism-specific biosystem; Metabolism of lipids and lipoproteins, organism-specific biosystem; PPAR (Peroxisome proliferator-activated receptor) signaling pathway, organism-specific biosystem;
Function : binding; lipid binding; transporter activity;

Not For Human Consumption!

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Customer Reviews (3)

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06/05/2021

    Unveiling a realm beyond the reaches of research, this wondrous reagent stands as the sacred partner.

    07/30/2020

      Experimentation surges forward with unrivaled celerity, guided by the efficiency of this remarkable reagent.

      10/28/2017

        The price of the reagent is relatively low, making it highly cost-effective.

        Q&As (7)

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        How is FABP4 involved in the development and progression of metabolic diseases? 05/31/2023

        FABP4 is implicated in the development and progression of metabolic diseases due to its influence on lipid metabolism and inflammation. Elevated FABP4 expression is observed in adipose tissue and macrophages in obese individuals. FABP4 promotes lipid accumulation, insulin resistance, and the production of pro-inflammatory cytokines, leading to adipose tissue dysfunction and systemic metabolic abnormalities. Inhibition or genetic depletion of FABP4 has been shown to improve metabolic parameters in animal models, highlighting its potential as a therapeutic target for metabolic diseases.

        an FABP4 be used as a biomarker for metabolic disorders? 11/10/2021

        FABP4 has been investigated as a potential biomarker for metabolic disorders, including obesity and type 2 diabetes. Studies have shown that circulating levels of FABP4 are elevated in individuals with these conditions. Increased FABP4 levels have also been associated with insulin resistance, dyslipidemia, and cardiovascular risk factors. However, further research is needed to validate FABP4 as a reliable biomarker and to determine its clinical utility in the diagnosis, prognosis, and monitoring of metabolic diseases.

        How does FABP4 interact with other proteins and signaling pathways? 05/05/2021

        FABP4 interacts with various proteins and signaling pathways to regulate lipid metabolism and inflammation. For instance, FABP4 interacts with PPARγ, a key transcription factor involved in adipogenesis and lipid metabolism. This interaction influences the expression of genes involved in lipid uptake and storage. FABP4 also interacts with inflammatory signaling pathways, such as NF-κB and JNK, modulating the production of pro-inflammatory cytokines. Understanding the molecular interactions of FABP4 can provide insights into its functional roles and potential targets for therapeutic intervention.

        What is the role of genetic variants in FABP4 in metabolic disorders? 12/20/2019

        Genetic variants in the FABP4 gene have been associated with metabolic disorders. Single nucleotide polymorphisms (SNPs) in the FABP4 gene have been linked to obesity, insulin resistance, and dyslipidemia. These genetic variants may alter FABP4 expression, protein structure, or function, leading to dysregulated lipid metabolism and increased susceptibility to metabolic diseases. Further investigation is needed to elucidate the functional consequences of these genetic variants and their potential as predictive markers for metabolic disorders.

        What are the potential therapeutic strategies targeting FABP4? 02/15/2019

        Various therapeutic strategies targeting FABP4 have been explored. Small molecule inhibitors of FABP4 have shown promising results in preclinical studies, attenuating lipid accumulation, improving insulin sensitivity, and reducing inflammation. Additionally, gene silencing approaches, such as RNA interference, have been investigated to suppress FABP4 expression. Furthermore, modulation of FABP4 activity through natural compounds and lifestyle interventions, such as exercise and dietary modifications, may also hold therapeutic potential. However, more research is required to evaluate the safety and efficacy of these strategies in human subjects.

        What is the biological function of FABP4 in cellular processes and metabolism? 06/13/2017

        FABP4, also known as fatty acid-binding protein 4, plays a crucial role in lipid metabolism and cellular processes. It functions as an intracellular transporter for fatty acids, facilitating their uptake, storage, and utilization. Additionally, FABP4 modulates inflammation, insulin sensitivity, and adipocyte differentiation. Its expression is regulated by various factors such as PPARγ and C/EBPα. FABP4 dysregulation has been associated with metabolic disorders, such as obesity and type 2 diabetes, making it an important target for therapeutic interventions.

        How does FABP4 contribute to the pathogenesis of cardiovascular diseases? 01/14/2016

        FABP4 has been implicated in the pathogenesis of cardiovascular diseases due to its involvement in lipid metabolism, inflammation, and atherosclerosis. Elevated FABP4 levels have been observed in individuals with coronary artery disease, and FABP4 has been shown to promote foam cell formation, a key step in atherosclerotic plaque development. FABP4 also influences vascular endothelial function and thrombosis. Inhibition of FABP4 has demonstrated beneficial effects on atherosclerosis progression and cardiovascular outcomes in experimental models. Further research is needed to fully understand the mechanisms underlying the contribution of FABP4 to cardiovascular diseases.

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