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Human FABP3, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Human FABP3, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Human FABP3, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.

Human FABP3 / H-FABP Protein, His Tag

Research Use Only
FA3-H5128
ACRObiosystems
Product group Molecular Biology
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Overview

  • Supplier
    ACRObiosystems
  • Product Name
    Human FABP3 / H-FABP Protein, His Tag
  • Delivery Days Customer
    4
  • Category Supplier
    Bio-Markers & CD Antigens
  • Certification
    Research Use Only
  • Scientific Description
    Characteristics: This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 15.7 kDa. The protein migrates as 15-17 kDa under reducing (R) condition (SDS-PAGE). Description: Fatty acid-binding protein 3 (FABP3) is also known as Heart-type fatty acid binding protein (H-FABP), Mammary-derived growth inhibitor (MDGI), Muscle fatty acid-binding protein (M-FABP), FABP11, which belongs to the calycin superfamily and fatty-acid binding protein (FABP) family. FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. H-FABP / FABP3 is involved in active fatty acid metabolism where it transports fatty acids from the cell membrane to mitochondria for oxidation. FABP3 may also contribute to AS160 phosphorylation by maintaining insulin-dependent Akt activation in the cells under a lipotoxic condition.
  • Shelf life instruction
    ● -20°C to -70°C for 12 months in lyophilized state; ● -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.
  • Storage Instruction
    -20℃
  • UNSPSC
    41116133