Product nameAnti-Chlamydia trachomatis MOMP antibody (HRP)
See all Chlamydia trachomatis MOMP primary antibodies
DescriptionGoat polyclonal to Chlamydia trachomatis MOMP (HRP)
Tested applicationsSuitable for: WB, ELISAmore details
Species reactivityReacts with Chlamydia Trachomatis. Does not react with C. psittacii or C. pneumoniae in MIF.
Purified MOMP from strain L2.
The antibody is covalently coupled to highly purified preparation of horseradish peroxidase (RZ>3). Care is taken to ensure adequate conjugation while preserving maximum enzyme activity. Free enzyme is absent. Estimated molar HRP:IgG substitution is 2-3.
Storage instructionsShipped at 4°C. Store at +4°C.
Storage bufferPreservative: 0.002% Thimerosal (merthiolate)
Constituents: PBS, 1% BSA
Concentration information loading...
- TMB ELISA Substrate (Highest Sensitivity) (ab171522)
- TMB ELISA Substrate (High Sensitivity) (ab171523)
- TMB ELISA Substrate (Fast Kinetic Rate) (ab171524)
- TMB ELISA Substrate (Slow Kinetic Rate) (ab171525)
- TMB ELISA Substrate (Slower Kinetic Rate) (ab171526)
- TMB ELISA Substrate (Slowest Kinetic Rate) (ab171527)
- 450 nm Stop Solution for TMB Substrate (ab171529)
- 650 nm Stop Solution for TMB Substrate (ab171531)
- Immunoassay Blocking Buffer (ab171534)
- Immunoassay Blocking (BSA Free) (ab171535)
Our Abpromise guarantee covers the use of ab20798 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
WB: 1/20 - 1/200. Dilution optimised using Chromogenic detection.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
RelevanceChlamydia is caused by the bacterium Chlamydia trachomatis. The intracytoplasmic inclusions caused by the bacterium are draped around the infected cell's nucleus. Chlamydia trachomatis is an intracellular organism that has a genome size of approximately 500-1000 kilobases and contains both RNA and DNA. The organism is also extremely temperature sensitive and must be refrigerated at 4°C as soon as a sample is obtained. Colonization of Chlamydia begins with attachment to sialic acid receptors on the eye, throat or genitalia. It persists at body sites that are inaccessible to phagocytes, T cells, and B cells. It also exists as 15 different serotypes. These serotypes cause four major diseases in humans: endemic trachoma (caused by serotypes A and C), sexually transmitted disease and inclusion conjunctivitis (caused by serotypes D and K), and lymphogranuloma venereum (caused by serotypes L1, L2, and L3). Studies reveal that Chlamydia, because of its cell wall, is able to inhibit phagolysosome fusion in phagocytes. The cell wall is proposed to be Gram negative in that it contains an outer lipopolysaccharide membrane, but it lacks peptidoglycan in its cell wall. This lack of peptidoglycan is shown by the inability to detect muramic acid and antibodies directed against it. It may, however, contain a carboxylated sugar other than muramic acid. The proposed structure consists of a major outer membrane protein cross linked with disulfide bonds. It also contains cysteine rich proteins (CRP) that may be the functional equivalent to peptidoglycan. This unique structure allows for intracellular division and extracellular survival (Hatch 1996). Chlamydia usually infects the cervix and fallopian tubes of women and the urethra of men. Chlamydial infections are believed to be one of the most common of all STDs. It is generally thought that in a population of 15 million, there are up to 300,000 cases of chlamydia each year. Thus, there are many undiagnosed cases of chlamydia in the community. It has been estimated that the true prevalence of chlamydia in the sexually active population may be in the order of 5% to 10%. Chlamydia is one of the leading causes of blindness in underdeveloped countries.
Cellular localizationOuter membrane; multi pass membrane protein.
- Major Outer Membrane Protein antibody
- MOMP antibody
- omp1 antibody
ab20798 has not yet been referenced specifically in any publications.