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Key Documents

L6638

Sigma-Aldrich

Lipid A, monophosphoryl from Escherichia coli F583 (Rd mutant)

lyophilized powder

Synonyme(s) :

E. coli Monophosphoryl Lipid A

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About This Item

Numéro MDL:
Code UNSPSC :
12352211
Nomenclature NACRES :
NA.25

Source biologique

Escherichia coli (F583 Rd mutant)

Niveau de qualité

Forme

lyophilized powder

Impuretés

<0.2% Ketodeoxyoctonate (KDO)

Conditions d'expédition

ambient

Température de stockage

2-8°C

Actions biochimiques/physiologiques

Lipid A molecules compose the lipid membrane anchoring core components of endotoxins produced by Gram-negative bacteria. Lipid A molecules induce immune responses. Structually, lipid A molecules are composed of two glucosamine unites with varied, species dependent, fatty acyl chain number and identity and degree of phosphorylation.
Lipid A, monophosphoryl from Escherichia coli F583 may be used in comparative assessment of the antigenicity of specific structures within different LPA molecules and analogues.
Lipid A has immunostimulatory adjuvant activity including macrophage, T-cell, and B-cell activation. Research has shown Lipid A has greater Th1 than Th2 stimulation.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Mark B Stoddard et al.
Clinical and vaccine immunology : CVI, 17(1), 98-107 (2009-11-20)
Bacterial endotoxin interacts with the human immune system via complex immunological pathways. The evaluation of endotoxicity is important in the development of safe vaccines and immunomodulatory therapeutics. The Limulus amebocyte lysate (LAL) assay is generally accepted by the FDA for
Vincent J Venditto et al.
Clinical and vaccine immunology : CVI, 21(8), 1086-1093 (2014-05-30)
Broadly neutralizing monoclonal antibodies (bNAbs) 2F5 and 4E10 bind to the membrane proximal external region (MPER) of gp41 and also cross-react with phospholipids. In this study, we investigated if chemical modifications on the MPER adjacent to 2F5 and 4E10 epitopes
Vincent J Venditto et al.
Clinical and vaccine immunology : CVI, 20(1), 39-45 (2012-11-02)
The inability to generate broadly neutralizing antibody (bnAb) responses to the membrane proximal external region (MPER) of HIV-1 gp41 using current vaccine strategies has hampered efforts to prevent the spread of HIV. To address this challenge, we investigated a novel
Douglas S Watson et al.
Clinical and vaccine immunology : CVI, 18(2), 289-297 (2010-12-17)
Particulate delivery systems enhance antibody responses to subunit antigens. However, covalent attachment of protein antigens can disrupt protein structure and mask critical epitopes, altering the antibody response to the antigen. In this report, we evaluate noncovalent metal chelation via nitrilotriacetic
K Olson et al.
Vaccine, 28(2), 548-560 (2009-10-20)
Herpes simplex virus type 2 (HSV2) is the most common causative agent of genital herpes, with infection rates as high as 1 in 6 adults. The present studies were done to evaluate the efficacy of a liposomal HSV2 gD(1-306) vaccine

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