Legionella pneumophila LPS Philadelphia 1 Strain (Biotin)

1105 EUR

1000ug

GEN608375

N/A

N/A

N/A

N/A

IgG3

9L445

strain

Antibodies

legionella

Monoclonal

Biotinylated

ELISA (EL/EIA)

Mnoclonal antibodies

Mouse (Mus musculus)

LPS biosynthesis protein, PseA-like; N/A

Legionella pneumophila LPS Philadelphia 1 Strain

Affinity Purified by Protein G affinity chromatography.

Supplied as a liquid in 0.1M carbonate, pH 9.2, 0.1% sodium azide. Labeled with Biotin.

N/A; Due to limited knowledge and inability for testing each and every species, the reactivity of the antibody may extend to other species which are not listed hereby.

Biotin conjugates can be detected by horseradish peroxidase, alkaline phosphatase substrates or anti biotin conjugated antibodies. Avidin and Streptavidin bind to the small biotin and are couple to HRP or AP for ELISA. To break the streptavidin Biotin bond we suggest to use a 6 molar guanidine HCl solution with acidity of pH 1.6.

Store the antibody at +4 degrees Celsius for short term storage.. Aliquot to avoid repeated freezing and thawing. For optimal long term storage, the antibody should be kept at -20 degrees Celsius. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Recognizes the LPS membrane of Legionella pneumophila. Does not cross-react with Pseudomonas fluorescens, Pseudomonas cepacia, Pseudomonas aerugenose, Bordetella pertusis, Leptospira interrogens (Australia), Leptospira interrogens (Pomona), Leptospira interrogens (Icterogemorrhagia), Toxoplasma gondii, Hemophilus influenza (type B), Brucella abortus, Bacillus anthracis, Yersenia pseudotuberculosis, Salmonella typhi, Escherichia coli K88 and Francisella tularensis.; Since it is not possible to test each and every species our knowledge on the corss reactivity of the antibodies is limited. This particular antibody might cross react with speacies outside of the listed ones.

Bacterial pathogen lipopolysaccharides (LPS) are the major outer surface membrane components present in almost all Gram-negative bacteria and act as extremely strong stimulators of innate or natural immunity in diverse eukaryotic species ranging from insects to humans. LPS consist of a poly- or oligosaccharide region that is anchored in the outer bacterial membrane by a specific carbohydrate lipid moiety termed lipid A. The lipid A component is the primary immunostimulatory center of LPS. With respect to immunoactivation in mammalian systems, the classical group of strongly agonistic (highly endotoxin) forms of LPS has been shown to be comprised of a rather similar set of lipid A types. In addition, several natural or derivative lipid A structures have been identified that display comparatively low or even no immunostimulation for a given mammalian species. Some members of the latter more heterogeneous group are capable of antagonizing the effects of strongly stimulatory LPS/lipid A forms. Agonistic forms of LPS or lipid A trigger numerous physiological immunostimulatory effects in mammalian organisms, but--in higher doses--can also lead to pathological reactions such as the induction of septic shock. Cells of the myeloid lineage have been shown to be the primary cellular sensors for LPS in the mammalian immune system. During the past decade, enormous progress has been obtained in the elucidation of the central LPS/lipid A recognition and signaling system in mammalian phagocytes. According to the current model, the specific cellular recognition of agonistic LPS/lipid A is initialized by the combined extracellular actions of LPS binding protein (LBP), the membrane-bound or soluble forms of CD14 and the newly identified Toll-like receptor 4 (TLR4)*MD-2 complex, leading to the rapid activation of an intracellular signaling network that is highly homologous to the signaling systems of IL-1 and IL-18. The elucidation of structure-activity correlations in LPS and lipid A has not only contributed to a molecular understanding of both immunostimulatory and toxic septic processes, but has also re-animated the development of new pharmacological and immuno-stimulatory strategies for the prevention and therapy of infectious and malignant diseases.