MOUSE Anti-CHLAMYDIA LPS Antibody

636 EUR

1000ug

GEN214481

N/A

N/A

N/A

N/A

N/A

512F

IgG2b

chlamydia

anticorps

Antibodies

Monoclonal

Mus musculus

CHLAMYDIA LPS

Mnoclonal antibodies

Mouse (Mus musculus)

IgG concentration 0.95mg/ml

Purified (Purified IgG - liquid)

ELISA (EIA), Immunofluorescence (IF), Western Blot (WB)

Cervix, urethra an eye infection by Chlamydia trachomatis can form inclusion bodies in humans.

If you buy Antibodies supplied by MBS Monoclonals they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.

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.

Bacterial; 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.

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.

Store the antibody at +4 degrees Celsius for short-term storage and at -20 degrees Celsius for long-term.Storage in frost-free freezers is not recommended. the antibody should be stored undiluted. Repeated freeze - thaw cycles may denature the peptide chains of the antibody and therefore should be maximally avoided. If there is a precipitate in the vial we recommend you to briefly microcentrifugate it prior to use. Shelf Life: 18 months from date of dispatch.

CHLAMYDIA LPS This item recognises a genus specific epitope within Chlamydia lipopolysaccharide (LPS). _x000D__x000D_LPS is a common feature of the outer envelope of gram negative bacteria, which acts as a potent endotoxin, triggering an innate immune response. Studies have shown however, that whilst the LPS of Chlamydia trachomatis does evoke an immune response, it displays only weak endotoxic activity when compared to that of other bacteria such as Salmonella Minnesota or Neisseria gonorrhoeae.; 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.