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L6638

Sigma-Aldrich

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

lyophilized powder

Synonym(s):

E. coli Monophosphoryl Lipid A

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About This Item

MDL number:
UNSPSC Code:
12352211
NACRES:
NA.25

biological source

Escherichia coli (F583 Rd mutant)

Quality Level

form

lyophilized powder

impurities

<0.2% Ketodeoxyoctonate (KDO)

shipped in

ambient

storage temp.

2-8°C

Biochem/physiol Actions

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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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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