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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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About This Item

Empirical Formula (Hill Notation):
C53H93N2O15Ni
CAS Number:
231615-77-3
Molecular Weight:
1057.00
UNSPSC Code:
12352211
NACRES:
NA.25

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

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Description
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Storage Class Code

11 - Combustible Solids

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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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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
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
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
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
Elizabeth M Wilson-Kubalek et al.
Methods in enzymology, 481, 45-62 (2010-10-05)
Helical protein arrays offer unique advantages for structure determination by cryo-electron microscopy (cryo-EM). A single image of such an array contains a complete range of equally spaced molecular views of the underlying protein subunits, which allows a low-resolution, isotropic three-dimensional
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