Bacterial cytokenetic protein
| Catalog# | Product Description | Host Species | Nature | Cross reactivity | Quantity | Volume | Price |
|---|---|---|---|---|---|---|---|
| FtsZ-101AP | FtsZ antiboides | Rabbit | AP | Eukaryotic protein | 100.0 ug | 150-500 ul |
$245.00
|
| FITC-FtsZ | FITC-conjugated antibodies | Rabbit | FITC-AP | Eukaryotic protein | 100.0 ug | 150-500 ul |
$350.00
|
| P-FtsZ | Antigenic blocking peptide | n/a | Synthetic peptide | n/a | 250.0 ug | 100 ul |
$125.00
|
| PC-FtsZ | WB positive control for FtsZ | n/a | Protein in ready-to-use buffer | n/a | 0.0 ug | 150 ul |
$185.00
|
The bacterial cytokinetic protein FtsZ is a tubulin-like protein with GTPase activity and it plays an important role in cell division. The FtsZ protein is conserved throughout the bacteria and archaea where in response to an unknown cell division signal it polymerizes in to a ring which becomes the site of future cell division site. During cell division of B. subtilis, the frequency of cells with FtsZ rings varies 2-3-fold, however, the cellular concentration of FtsZ remain constant irrespective of doubling time (1). The FtsZ is expressed via a constitutive promoter thus eliminating the normal transcription al control. The FtsZ undergo GTP-dependent polymerization in to medial FtsZ ring-formation and separation at cell poles is mediated by several protein partners. The MinCD complex is found concentrated at the cell poles where it inhibits the FtsZ polymerization (2). The FtsZ protein has GTPase activity which correlated with the FtsZ polymerization and FtsZ ring formation in rapid times of approximately 10 seconds (3). GTPase dependent polymerizsation of FtsZ is inhibited by SulA which is further purified as a fusion portien to MalE and staphylococcus protein A. The FtsZ deficient B. subtilis mutants are deficient in the initiation stages of cell division and exhibit long filament like growth when subjected to non-permissive temperature. The free energy of GTP hydrolysis appears not to be used for generation o constriction forces thus the role of GTPase activity in ring formation is still an open question (4).
The Z ring is a very dynamic structure through which subunits of FtsZ cycle with a half time of about 10 seconds. FtsZ is a GTPase that is similar to the eukaryotic tubulins and is essential for cell division in prokaryotes. FtsZ is capable of polymerizing in a GTP-driven process into structures similar to those formed by tubulin. FtsZ forms a ring-shaped septum just prior to cell division. Staphylococcus aureus FtsZ is a 390 amino acid protein with a nucleotide binding site and a SulA interaction site. Disruption in the activity of FtsZ in S aureus affects its growth pattern and may be an important therapeutic target fight against staphylococcus infections,
The Anti-FtsZ-selective antibodies were generated against a synthetic peptide corresponding to a near C-terminal location on S. aureus protein. The FtsZ-selective antibodies are affinity purified against immobilized antigen based affinity chromatography which yielded high affinity epitope-specific antibodies. The FtsZ antibodies label a protein of approximately 47-48kDa protein in Western blot using Western blot positive control for FtsZ (PC-FtsZ). Anti-FtsZ-selective antibodies are also available in various conjugated forms (FITC and Rodamine) for confocal, Western blotting and immunocytochemical analyses. FabGennix Inc. will also conjugate antibodies with fluorescent probes upon request at extra charge. Limited quantities of antigenic peptide is also available (inquire before ordering). FabGennix Inc. also provides antibodies for epigenetics and, cell cycle-related research areas, for a complete listing of these products, please visit www.FabGennix.com. FabGennix Int. Inc., will also provide Western blot positive controls for most of these antibodies in ready-to-use buffer for easy identification of respective proteins. Limited quantities of antigens are also available for blocking studies. Please inquire for their availability before ordering.
For research use only, not for diagnostic or therapeutic use.
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