790404P
Avanti
18:1 DGS-NTA(Ni)
Avanti Research™ - A Croda Brand
Synonym(s):
1,2-di-(9Z-octadecenoyl)-sn-glycero-3-[(N-(5-amino-1-carboxypentyl)iminodiacetic acid)succinyl] (nickel salt); DOGS NTA
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All Photos(1)
About This Item
Empirical Formula (Hill Notation):
C53H93N2O15Ni
CAS Number:
Molecular Weight:
1057.00
UNSPSC Code:
12352211
NACRES:
NA.25
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description
1,2-dioleoyl-sn-glycero-3-[(N-(5-amino-1-carboxypentyl)iminodiacetic acid)succinyl] (nickel salt)
Assay
>99% (TLC)
form
powder
packaging
pkg of 1 × 10 mg (790404P-10mg)
pkg of 1 × 25 mg (790404P-25mg)
pkg of 1 × 5 mg (790404P-5mg)
manufacturer/tradename
Avanti Research™ - A Croda Brand
shipped in
dry ice
storage temp.
−20°C
General description
1,2-dioleoyl-sn-glycero-3-[(N-(5-amino-1-carboxypentyl)iminodiacetic acid)succinyl] nitrilotriacetic acid (NTA) (18:1 DGS-NTA(Ni)) is a conjugated phospholipid that contains nickel. NTA chelates with four of the six coordination sites present in nickel ion.
Application
1,2-dioleoyl-sn-glycero-3-[(N-(5-amino-1-carboxypentyl)iminodiacetic acid)succinyl] (nickel salt) (18:1 DGS-NTA(Ni)) has been used:
- in the preparation of liposomes with porphyrin-phospholipid (PoP) conjugate for protein and peptide binding studies
- in the preparation of nanosize multillamelar vesicles (NMVs) for antigen delivery studies
- as a component of small unilamellar vesicle (SUV) for planar lipid membrane (PM) preparation
Biochem/physiol Actions
1,2-dioleoyl-sn-glycero-3-[(N-(5-amino-1-carboxypentyl)iminodiacetic acid)succinyl] nitrilotriacetic acid (NTA) (18:1 DGS-NTA(Ni)) is useful in structural biology especially to bind recombinant histidine tagged proteins. Though useful, being nanoparticulate it has stability problems in biological samples. So NTA-lipid conjugate is majorly used as liposomes or as a coating to nanoparticle. DGS-NTA (Ni) based nanosize multillamelar vesicles (NMVs) are potent vaccine delivery system.
Packaging
5 mL Clear Glass Sealed Ampule (790404P-10mg)
5 mL Clear Glass Sealed Ampule (790404P-25mg)
5 mL Clear Glass Sealed Ampule (790404P-5mg)
Legal Information
Avanti Research is a trademark of Avanti Polar Lipids, LLC
also commonly purchased with this product
Storage Class Code
11 - Combustible Solids
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Kelly A Dryden et al.
Protein science : a publication of the Protein Society, 18(12), 2629-2635 (2009-10-22)
Bacterial microcompartments (BMCs) are large intracellular bodies that serve as simple organelles in many bacteria. They are proteinaceous structures composed of key enzymes encapsulated by a polyhedral protein shell. In previous studies, the organization of these large shells has been
Samuel A Merrill et al.
The Journal of biological chemistry, 285(46), 35428-35438 (2010-09-02)
VPS4 proteins are AAA(+) ATPases required to form multivesicular bodies, release viral particles, and complete cytokinesis. They act by disassembling ESCRT-III heteropolymers during or after their proposed function in membrane scission. Here we show that purified human VPS4A is essentially
David J Montefusco et al.
Methods in enzymology, 423, 267-298 (2007-07-05)
The reconstitution of membrane-associated protein complexes poses significant experimental challenges. The core signaling complex in the bacterial chemotaxis system is an illustrative example: The soluble cytoplasmic signaling proteins CheW and CheA bind to heterogeneous clusters of transmembrane receptor proteins, resulting
Priyanka D Abeyrathne et al.
Methods in enzymology, 481, 25-43 (2010-10-05)
Electron crystallography is a powerful technique for the structure determination of membrane proteins as well as soluble proteins. Sample preparation for 2D membrane protein crystals is a crucial step, as proteins have to be prepared for electron microscopy at close
John Monsey et al.
The Journal of biological chemistry, 285(10), 7035-7044 (2009-12-22)
Her4 (ErbB-4) and Her2/neu (ErbB-2) are receptor-tyrosine kinases belonging to the epidermal growth factor receptor (EGFR) family. Crystal structures of EGFR and Her4 kinase domains demonstrate kinase dimerization and activation through an allosteric mechanism. The kinase domains form an asymmetric
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