APOA5 Human

Apolipoprotein A-V Human Recombinant
Cat. No.
BT11359
Source
Escherichia Coli.
Synonyms
Apolipoprotein A-V, Apo-AV, ApoA-V, Apolipoprotein A5, Regeneration-associated protein 3, APOA5, RAP3, APOAV.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

APOA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (24-366 a.a.) and having a molecular mass of 41.3kDa.
APOA5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Description
Recombinant human APOA5 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It encompasses amino acids 24 to 366, resulting in a protein of 366 amino acids with a molecular weight of 41.3 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus, and the protein is purified using proprietary chromatographic techniques.
Physical Appearance
A clear and colorless solution that has been sterilized by filtration.
Formulation
The APOA5 protein solution is provided at a concentration of 0.25 mg/ml. The solution is buffered with 20mM Tris-HCl at a pH of 8.0 and contains 10% glycerol and 0.4M Urea.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the protein is determined by SDS-PAGE analysis and is greater than 85.0%.
Synonyms
Apolipoprotein A-V, Apo-AV, ApoA-V, Apolipoprotein A5, Regeneration-associated protein 3, APOA5, RAP3, APOAV.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRKGFWDY FSQTSGDKGR VEQIHQQKMA REPATLKDSL EQDLNNMNKF LEKLRPLSGS EAPRLPQDPV GMRRQLQEEL EEVKARLQPY MAEAHELVGW NLEGLRQQLK PYTMDLMEQV ALRVQELQEQ LRVVGEDTKA QLLGGVDEAW ALLQGLQSRV VHHTGRFKEL FHPYAESLVS GIGRHVQELH RSVAPHAPAS PARLSRCVQV LSRKLTLKAK ALHARIQQNL DQLREELSRA FAGTGTEEGA GPDPQMLSEE VRQRLQAFRQ DTYLQIAAFT RAIDQETEEV QQQLAPPPPG HSAFAPEFQQ TDSGKVLSKL QARLDDLWED ITHSLHDQGH SHLGDP.

Product Science Overview

Discovery and Structure

Apolipoprotein A-V was first identified in 2001 through comparative genomics. It is encoded by the APOA5 gene, located on chromosome 11q23. The protein consists of 366 amino acids and has a molecular weight of approximately 40 kDa. The recombinant form of ApoA-V is often produced in HEK 293 cells, ensuring high purity and functionality .

Function and Mechanism

ApoA-V is a potent regulator of serum triglyceride concentrations. It exerts its effects through several mechanisms:

  1. Enhancing Lipoprotein Lipase (LPL) Activity: ApoA-V promotes the hydrolysis of triglycerides in very low-density lipoproteins (VLDL) by activating LPL, an enzyme critical for triglyceride breakdown.
  2. Inhibiting Hepatic VLDL Secretion: ApoA-V reduces the secretion of VLDL particles from the liver, thereby lowering the amount of triglycerides released into the bloodstream.
  3. Facilitating Receptor-Mediated Uptake: ApoA-V enhances the clearance of triglyceride-rich lipoproteins by promoting their uptake via hepatic receptors.
Clinical Significance

Mutations or variations in the APOA5 gene are associated with hypertriglyceridemia, a condition characterized by elevated levels of triglycerides in the blood. This condition is a risk factor for cardiovascular diseases, including coronary artery disease and pancreatitis. Understanding the role of ApoA-V in lipid metabolism has significant implications for developing therapeutic strategies to manage hypertriglyceridemia and related disorders.

Recombinant ApoA-V

Recombinant human ApoA-V is produced using advanced biotechnological methods. The protein is expressed in HEK 293 cells, which are human embryonic kidney cells commonly used for protein production due to their high transfection efficiency and ability to perform post-translational modifications. The recombinant protein is purified to a high degree, with a purity of over 70% as determined by SDS-PAGE .

Applications

Recombinant ApoA-V is used in various research applications, including:

  • Studying Lipid Metabolism: Researchers use recombinant ApoA-V to investigate its role in lipid metabolism and its potential as a therapeutic target for hypertriglyceridemia.
  • Drug Development: The protein is used in the development of drugs aimed at regulating triglyceride levels and preventing cardiovascular diseases.
  • Biochemical Assays: Recombinant ApoA-V is employed in assays to study its interaction with other proteins and lipids, providing insights into its mechanism of action.

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