- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
CYT-767
Synonyms
Apolipoprotein A-V, Apo-AV, ApoA-V, Apolipoprotein A5, Regeneration-associated protein 3, APOA5, RAP3, APOAV.
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.
APOA5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile filtered colorless solution.
Formulation
APOA5 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
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.
Safety Data Sheet
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
ProSpec'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.
Background
Apolipoprotein A-V Human Recombinant: Unleashing the Power of Lipid Regulation
Abstract:
Apolipoprotein A-V (ApoA-V), a fascinating player in the intricate world of lipid metabolism, has emerged as a promising therapeutic target for lipid disorders. Produced primarily in the liver, ApoA-V exerts a profound influence on triglyceride metabolism. Dysregulation of ApoA-V has been implicated in various lipid-related disorders, including hypertriglyceridemia and cardiovascular diseases (CVDs). This research paper offers a concise yet comprehensive exploration of ApoA-V human recombinant, shedding light on its physiological functions, production methods, and potential therapeutic applications.
Introduction:
In the face of the soaring global burden of lipid disorders and cardiovascular ailments, novel therapeutic approaches are urgently needed. Apolipoproteins, the guardians of lipid transport, present promising targets for intervention. Among them, ApoA-V, a master regulator of triglyceride metabolism, holds great promise.
Structure and Function of Apolipoprotein A-V:
ApoA-V boasts an elegant molecular architecture, comprising specific domains that enable its interaction with lipoproteins engaged in lipid transport. Through its intricate mechanisms, ApoA-V fine-tunes triglyceride levels by modulating lipoprotein lipase activity and enhancing the clearance of triglyceride-rich lipoproteins.
Genetic Variations and Lipid Disorders:
Exploring the fascinating realm of genetics has uncovered ApoA-V gene polymorphisms linked to dyslipidemia, including hypertriglyceridemia. These genetic variations influence ApoA-V expression and function, thereby contributing to the development of lipid disorders and heightened cardiovascular risk.
Production of Apolipoprotein A-V Human Recombinant:
Harnessing the power of biotechnology, scientists have devised various expression systems, encompassing mammalian cells and bacteria, to produce recombinant ApoA-V. These techniques enable large-scale production, purification, and meticulous characterization of the recombinant protein, opening doors to potential therapeutic applications.
Therapeutic Applications of Apolipoprotein A-V Human Recombinant:
The prospect of targeting ApoA-V beckons as a promising avenue for managing lipid disorders, particularly hypertriglyceridemia. By manipulating ApoA-V expression or function, it becomes possible to reduce triglyceride levels, improve lipid profiles, and mitigate the risk of cardiovascular complications.
Conclusion:
Apolipoprotein A-V human recombinant represents a beacon of hope in the quest to conquer lipid disorders. Understanding the intricate interplay between ApoA-V's structure, function, and genetic variations offers profound insights into its potential role in personalized medicine. Unleashing the full therapeutic potential of ApoA-V human recombinant requires further scientific exploration and clinical studies, paving the way for effective interventions in lipid-related disorders.