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790404P

Avanti

18:1 DGS-NTA(Ni)

Avanti Research - A Croda Brand

Synonyme(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

Formule empirique (notation de Hill):
C53H93N2O15Ni
Numéro CAS:
Poids moléculaire :
1057.00
Code UNSPSC :
12352211
Nomenclature NACRES :
NA.25

Description

1,2-dioleoyl-sn-glycero-3-[(N-(5-amino-1-carboxypentyl)iminodiacetic acid)succinyl] (nickel salt)

Pureté

>99% (TLC)

Forme

powder

Conditionnement

pkg of 1 × 10 mg (790404P-10mg)
pkg of 1 × 25 mg (790404P-25mg)
pkg of 1 × 5 mg (790404P-5mg)

Fabricant/nom de marque

Avanti Research - A Croda Brand

Conditions d'expédition

dry ice

Température de stockage

−20°C

Catégories apparentées

Description générale

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

Actions biochimiques/physiologiques

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.

Conditionnement

5 mL Clear Glass Sealed Ampule (790404P-10mg)
5 mL Clear Glass Sealed Ampule (790404P-25mg)
5 mL Clear Glass Sealed Ampule (790404P-5mg)

Informations légales

Avanti Research is a trademark of Avanti Polar Lipids, LLC

Souvent commandé avec ce produit

Code de la classe de stockage

11 - Combustible Solids


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Consulter la Bibliothèque de documents

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
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
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
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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