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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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$219.39
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$443.00
25 MG
$629.00

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5 MG
$219.39
10 MG
$443.00
25 MG
$629.00

About This Item

Empirical Formula (Hill Notation):
C53H93N2O15Ni
CAS Number:
231615-77-3
Molecular Weight:
1057.00
MDL number:
MFCD00056438
UNSPSC Code:
12352211
NACRES:
NA.25

$219.39

Please contact Customer Service for Availability
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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[1] that contains nickel.[2] NTA chelates with four of the six coordination sites present in nickel ion.[3]

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[1]
  • in the preparation of nanosize multillamelar vesicles (NMVs) for antigen delivery studies[2]
  • as a component of small unilamellar vesicle (SUV) for planar lipid membrane (PM) preparation[4]

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.[1] 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.[1] DGS-NTA (Ni) based nanosize multillamelar vesicles (NMVs) are potent vaccine delivery system.[2]

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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Storage Class Code

11 - Combustible Solids

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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
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
Anthony L Shrout et al.
Biochemistry, 42(46), 13379-13385 (2003-11-19)
Transmembrane receptors in the signaling pathways of bacterial chemotaxis systems influence cell motility by forming noncovalent complexes with the cytoplasmic signaling proteins to regulate their activity. The requirements for receptor-mediated activation of CheA, the principal kinase of the Escherichia coli
Xuewu Zhang et al.
Cell, 125(6), 1137-1149 (2006-06-17)
The mechanism by which the epidermal growth factor receptor (EGFR) is activated upon dimerization has eluded definition. We find that the EGFR kinase domain can be activated by increasing its local concentration or by mutating a leucine (L834R) in the
Hao Zhang et al.
Molecular & cellular proteomics : MCP, 10(6), M110-M110 (2011-03-23)
Her4 is a transmembrane receptor tyrosine kinase belonging to the ErbB-EGFR family. It plays a vital role in the cardiovascular and nervous systems, and mutations in Her4 have been found in melanoma and lung cancer. The kinase domain of Her4
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