Monoclonal mouse anti-Francisella tularensis LPS

498 EUR

1000ug

GEN660087

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Antibodies

Monoclonal

T14, FB11.

Mus musculus

Mnoclonal antibodies

Francesella Tularensis LPS

IgG2a for MAbs FB11 IgG3 for MAb T14

Chromatography on protein G Sepharose

PBS, pH 7.4, 0.1 % sodium azide (NaN3)

Store the antibody at +4 degrees Celsius.

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.

This antibody needs to be stored at + 4°C in a fridge short term in a concentrated dilution. Freeze thaw will destroy a percentage in every cycle and should be avoided.

Monoclonals of this antigen are available in different clones. Each murine monoclonal anibody has his own affinity specific for the clone. Mouse monoclonal antibodies are purified protein A or G and can be conjugated to FITC for flow cytometry or FACS and can be of different isotypes.

Mouse or mice from the Mus musculus species are used for production of mouse monoclonal antibodies or mabs and as research model for humans in your lab. Mouse are mature after 40 days for females and 55 days for males. The female mice are pregnant only 20 days and can give birth to 10 litters of 6-8 mice a year. Transgenic, knock-out, congenic and inbread strains are known for C57BL/6, A/J, BALB/c, SCID while the CD-1 is outbred as strain.

MAb T14 reacts with LPS of Fr. tularensis. There is no cross-reactivity with Y. pestis, Y. pseudotuberculosis, Y. enterdegree Colitica, V. cholera, E Coli, S. typhimurium, Fr. novicida, Br. melitensis, Br. abortus, Br. suis, Br. ovis, and Br. neotomae. MAb FB11 recognizes LPS of virulent and vaccine strains of Fr. tularensis. There is no crossreactivity with Fr. novicida, Br. abortus, Br. suis, Br. melitensis, Br. ovis, Y. pestis, Y. enterdegree Colitica, Y. pseudotuberculosis, E Coli, and V. cholerae. The binding site for MAb FB11 is ldegree Cated on the O-antigen polysaccharide chain which consists of tetrasaccharide fragments and has the following structure: -4)alpha-D-GalpNAcAN-(1-4)-alpha-DGalpNAcAN-(1-3)-beta-D-QuipNAc-(1-2)-beta-Quip4NFm-(1. Tetrasaccharide D-GalpNAcAN-(1-4)-alpha-D-GalpNAcAN-(1-3)-beta-D-QuipNAc-(1-2)-beta-D-Quip4NFm and trisaccharide D-GalpNAcAN-(1-3)-beta-D-QuipNAc-(1-2)-beta-D-Quip4NFm compete in ELISA for binding MAb FB11 with LPS of Fr. 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.