Recombinant Human APOB, His-tagged

• Cat.No.: APOB-27149TH
• Product Overview: Recombinant fragment, corresponding to amino acids 1406-1606 of Human Apolipoprotein B, fused to a His tag at N-terminal end, 31kDa.

Specification

• Description: This gene product is the main apolipoprotein of chylomicrons and low density lipoproteins. It occurs in plasma as two main isoforms, apoB-48 and apoB-100: the former is synthesized exclusively in the gut and the latter in the liver. The intestinal and the hepatic forms of apoB are encoded by a single gene from a single, very long mRNA. The two isoforms share a common N-terminal sequence. The shorter apoB-48 protein is produced after RNA editing of the apoB-100 transcript at residue 2180 (CAA->UAA), resulting in the creation of a stop codon, and early translation termination. Mutations in this gene or its regulatory region cause hypobetalipoproteinemia, normotriglyceridemic hypobetalipoproteinemia, and hypercholesterolemia due to ligand-defective apoB, diseases affecting plasma cholesterol and apoB levels.
• Conjugation: HIS
• Source: E. coli
• Form: Liquid
• Storage buffer: Preservative: NoneConstituents: PBS
• Storage: Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
• Sequence Similarities: Contains 1 vitellogenin domain.
• Protein length: 1406-1606 a.a.

Gene Information

• Gene Name: APOB apolipoprotein B (including Ag(x) antigen) [ Homo sapiens ]
• Official Symbol: APOB
• Synonyms: APOB; apolipoprotein B (including Ag(x) antigen); apolipoprotein B-100
• Gene ID: 338
• mRNA Refseq: NM_000384
• Protein Refseq: NP_000375
• Uniprot ID: P04114
• Chromosome Location: 2p24-p23
• Pathway: Cell surface interactions at the vascular wall, organism-specific biosystem; Chylomicron-mediated lipid transport, organism-specific biosystem; FOXA1 transcription factor network, organism-specific biosystem; Fat digestion and absorption, organism-specific biosystem; Fat digestion and absorption, conserved biosystem
• Function: cholesterol transporter activity; enzyme binding; heparin binding; lipid transporter activity; low-density lipoprotein particle receptor binding