|Tested species reactivity||Human, Mouse|
|Published species reactivity||Rabbit, Fruit fly, Mouse, Human|
|Host / Isotype||Mouse / IgG1, kappa|
|Immunogen||Full-length, His-tagged murine FOXP3.|
|Storage buffer||50mM sodium borate|
|Contains||0.05% sodium azide|
|Storage Conditions||4° C, store in dark|
|Tested Applications||Dilution *|
|Flow Cytometry (Flow)||1:10-1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Immunoprecipitation (IP)||See 10 publications below|
MA1-41628 is derived from full-length His-tagged mouse FOXP3. The precise epitope is not known, but it has been mapped to the N-terminal portion of the protein.
One of the many immunotolerance mechanisms that the immune system has developed to distinguish between self and non-self antigens is regulatory T cells or Tregs. Several elegant experiments using transgenic mice and retrovirus-mediated over expression studies, have led to the identification of FoxP3, a trascription factor, as a specific molecular marker essential for the development and function of Tregs. The primary evidence regarding the involvement of FoxP3 in the development of Tregs was provided in patients suffering from IPEX, a rare and fatal human autoimmune disease. The emergence of Tregs and the role of FoxP3 as a critical palyer in the negative control of various normal and pathological immune responses holds great promise for the development of novel therapies for autoimmune diseases.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
MA1-41628 was used in immunoprecipitation to identify PP5 as an important component of glucocorticoid receptor-hsp90 complexes and investigate its functional properties
|Silverstein AM,Galigniana MD,Chen MS,Owens-Grillo JK,Chinkers M,Pratt WB||The Journal of biological chemistry (272:16224)||1997|
Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation.
MA1-41628 was used in immunoprecipitation to study the folding of hormone binding domain of glucocorticoid receptor in vitro using reconstituted receptor-hsp90 heterocomplex assembly system with purified components
|Dittmar KD,Pratt WB||The Journal of biological chemistry (272:13047)||1997|
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
MA1-41628 was used in immunoprecipitation to show HIF-1a is associated with the molecular chaperone hsp90 in vitro
|Gradin K,McGuire J,Wenger RH,Kvietikova I,fhitelaw ML,Toftgård R,Tora L,Gassmann M,Poellinger L||Molecular and cellular biology (16:5221)||1996|
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
MA1-41628 was used in immunoprecipitation to study the mechanisms of immunophilin-mediated protein targeting
|Owens-Grillo JK,Czar MJ,Hutchison KA,Hoffmann K,Perdew GH,Pratt WB||The Journal of biological chemistry (271:13468)||1996|
|Fruit fly||Not Cited||
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
MA1-41628 was used in immunoprecipitation to study the interaction between Sim and hsp90
|McGuire J,Coumailleau P,Whitelaw ML,Gustafsson JA,Poellinger L||The Journal of biological chemistry (270:31353)||1995|
Identification of functional domains of the aryl hydrocarbon receptor.
MA1-41628 was used in immunoprecipitation to investigate the functional domains of mouse aryl hydrocarbon receptor
|Fukunaga BN,Probst MR,Reisz-Porszasz S,Hankinson O||The Journal of biological chemistry (270:29270)||1995|
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
MA1-41628 was used in immunoprecipitation to detect the interaction between the dioxin receptor and Hsp90
|Coumailleau P,Poellinger L,Gustafsson JA,Whitelaw ML||The Journal of biological chemistry (270:25291)||1995|
A tyrosine kinase-dependent pathway regulates ligand-dependent activation of the dioxin receptor in human keratinocytes.
MA1-41628 was used in immunoprecipitation to investigate the role of a tyrosine kinase-dependent pathway during ligand-dependent activation of the dioxin receptor in human keratinocytes
|Gradin K,Whitelaw ML,Toftgård R,Poellinger L,Berghard A||The Journal of biological chemistry (269:23800)||1994|
Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex.
MA1-41628 was used in immunoprecipitation to investigate the interaction of different protein components of the heat shock protein heterocomplex
|Czar MJ,Owens-Grillo JK,Dittmar KD,Hutchison KA,Zacharek AM,Leach KL,Deibel MR,Pratt WB||The Journal of biological chemistry (269:11155)||1994|
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
MA1-41628 was used in immunoprecipitation to investigate the role of Arnt for release of hsp90 from the dioxin receptor in the presence of dioxin
|McGuire J,Whitelaw ML,Pongratz I,Gustafsson JA,Poellinger L||Molecular and cellular biology (14:2438)||1994|