Forkhead box protein P3 (FOXP3) Recombinant Protein | FOXP3 recombinant protein

Recombinant Human Forkhead box protein P3 (FOXP3), partial

Cat. Num. AAA1265493

• Gene Names: FOXP3; JM2; AIID; IPEX; PIDX; XPID; DIETER
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Forkhead box protein P3 (FOXP3); Recombinant Human Forkhead box protein P3 (FOXP3); partial; Scurfin; FOXP3 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-260aa; Partial
• Sequence: MPNPRPGKPSAPSLALGPSPGASPSWRAAPKASDLLGARGPGGTFQGRDLRGGAHASSSSLNPMPPSQLQLPTLPLVMVAPSGARLGPLPHLQALLQDRPHFMHQLSTVDAHARTPVLQVHPLESPAMISLTPPTTATGVFSLKARPGLPPGINVASLEWVSREPALLCTFPNPSAPRKDSTLSAVPQSSYPLLANGVCKWPGCEKVFEEPEDFLKHCQADHLLDEKGRAQCLLQREMVQSLEQQLVLEKEKLSAMQAHL

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for FOXP3 recombinant protein

Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2. Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7. Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1. Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development. Inhibits the transcriptional activator activity of RORA. Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4.

Product Categories/Family for FOXP3 recombinant protein

Transcription

References

Disruption of a new forkhead/winged-helix protein, scurfin, results in the fatal lymphoproliferative disorder of the scurfy mouse.Brunkow M.E., Jeffery E.W., Hjerrild K.A., Paeper B., Clark L.B., Yasayko S.-A., Wilkinson J.E., Galas D., Ziegler S.F., Ramsdell F.Nat. Genet. 27:68-73(2001) Cloning and expression of the cDNA for FOXP3.Wang J., Liu Q., Zhang Y., Xu Z., Huang C.Functional characterization of FOXP3 splice variants in human regulatory T cells.Kaur G., Goodall J.C., Jarvis L.B., Gaston J.S.H.Lin L., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Huang B., Zhou G., Yang S.The DNA sequence of the human X chromosome.Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.Nature 434:325-337(2005) Transcription map in Xp11.23.Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A.Foxp3 interacts with nuclear factor of activated T cells and NF-kappa B to repress cytokine gene expression and effector functions of T helper cells.Bettelli E., Dastrange M., Oukka M.Proc. Natl. Acad. Sci. U.S.A. 102:5138-5143(2005) Foxp3 controls regulatory T-cell function by interacting with AML1/Runx1.Ono M., Yaguchi H., Ohkura N., Kitabayashi I., Nagamura Y., Nomura T., Miyachi Y., Tsukada T., Sakaguchi S.Nature 446:685-689(2007) FOXP3 interactions with histone acetyltransferase and class II histone deacetylases are required for repression.Li B., Samanta A., Song X., Iacono K.T., Bembas K., Tao R., Basu S., Riley J.L., Hancock W.W., Shen Y., Saouaf S.J., Greene M.I.Proc. Natl. Acad. Sci. U.S.A. 104:4571-4576(2007) Isoform-specific inhibition of ROR alpha-mediated transcriptional activation by human FOXP3.Du J., Huang C., Zhou B., Ziegler S.F.J. Immunol. 180:4785-4792(2008) TGF-beta-induced Foxp3 inhibits T(H) 17 cell differentiation by antagonizing RORgammat function.Zhou L., Lopes J.E., Chong M.M., Ivanov I.I., Min R., Victora G.D., Shen Y., Du J., Rubtsov Y.P., Rudensky A.Y., Ziegler S.F., Littman D.R.Nature 453:236-240(2008) Foxp3 processing by proprotein convertases and control of regulatory T cell function.de Zoeten E.F., Lee I., Wang L., Chen C., Ge G., Wells A.D., Hancock W.W., Ozkaynak E.J. Biol. Chem. 284:5709-5716(2009) Activation of the aryl hydrocarbon receptor induces human type 1 regulatory T cell-like and Foxp3(+) regulatory T cells.Gandhi R., Kumar D., Burns E.J., Nadeau M., Dake B., Laroni A., Kozoriz D., Weiner H.L., Quintana F.J.Nat. Immunol. 11:846-853(2010) Subcellular localization of FOXP3 in human regulatory and nonregulatory T cells.Magg T., Mannert J., Ellwart J.W., Schmid I., Albert M.H.Eur. J. Immunol. 42:1627-1638(2012) Three novel acetylation sites in the Foxp3 transcription factor regulate the suppressive activity of regulatory T cells.Kwon H.S., Lim H.W., Wu J., Schnolzer M., Verdin E., Ott M.J. Immunol. 188:2712-2721(2012) A novel function for FOXP3 in humans intrinsic regulation of conventional T cells.McMurchy A.N., Gillies J., Gizzi M.C., Riba M., Garcia-Manteiga J.M., Cittaro D., Lazarevic D., Di Nunzio S., Piras I.S., Bulfone A., Roncarolo M.G., Stupka E., Bacchetta R., Levings M.K.Blood 121:1265-1275(2013) Searching for the Achilles Heel of FOXP3.Lozano T., Casares N., Lasarte J.J.Front. Oncol. 3:294-294(2013) Stabilization of the transcription factor Foxp3 by the deubiquitinase USP7 increases Treg-cell-suppressive capacity.van Loosdregt J., Fleskens V., Fu J., Brenkman A.B., Bekker C.P., Pals C.E., Meerding J., Berkers C.R., Barbi J., Grone A., Sijts A.J., Maurice M.M., Kalkhoven E., Prakken B.J., Ovaa H., Pan F., Zaiss D.M., Coffer P.J.Immunity 39:259-271(2013) The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3.Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D., Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J., Gao Z., Tian H., Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J., Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G., Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.Immunity 39:272-285(2013) Cutting Edge a novel, human-specific interacting protein couples FOXP3 to a chromatin-remodeling complex that contains KAP1/TRIM28.Huang C., Martin S., Pfleger C., Du J., Buckner J.H., Bluestone J.A., Riley J.L., Ziegler S.F.J. Immunol. 190:4470-4473(2013) Phosphorylation of FOXP3 controls regulatory T cell function and is inhibited by TNF-alpha in rheumatoid arthritis.Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L., Chen X., Wan B., Chin Y.E., Zhang J.Z.Nat. Med. 19:322-328(2013) The role of FOXP3 in regulating immune responses.Vent-Schmidt J., Han J.M., MacDonald K.G., Levings M.K.Int. Rev. Immunol. 33:110-128(2014) Forkhead box P3 the peacekeeper of the immune system.Passerini L., Santoni de Sio F.R., Roncarolo M.G., Bacchetta R.Int. Rev. Immunol. 33:129-145(2014) FOXP3 and scurfy how it all began.Ramsdell F., Ziegler S.F.Nat. Rev. Immunol. 14:343-349(2014) Post-translational modification networks regulating FOXP3 function.van Loosdregt J., Coffer P.J.Trends Immunol. 35:368-378(2014) JM2, encoding a fork head-related protein, is mutated in X-linked autoimmunity-allergic disregulation syndrome.Chatila T.A., Blaeser F., Ho N., Lederman H.M., Voulgaropoulos C., Helms C., Bowcock A.M.J. Clin. Invest. 106:R75-R81(2000) Novel mutations of FOXP3 in two Japanese patients with immune dysregulation, polyendocrinopathy, enteropathy, X linked syndrome (IPEX) .Kobayashi I., Shiari R., Yamada M., Kawamura N., Okano M., Yara A., Iguchi A., Ishikawa N., Ariga T., Sakiyama Y., Ochs H.D., Kobayashi K.J. Med. Genet. 38:874-876(2001) X-linked neonatal diabetes mellitus, enteropathy and endocrinopathy syndrome is the human equivalent of mouse scurfy.Wildin R.S., Ramsdell F., Peake J., Faravelli F., Casanova J.-L., Buist N., Levy-Lahad E., Mazzella M., Goulet O., Perroni L., Bricarelli F.D., Byrne G., McEuen M., Proll S., Appleby M., Brunkow M.E.Nat. Genet. 27:18-20(2001) The immune dysregulation, polyendocrinopathy, enteropathy, X-linked syndrome (IPEX) is caused by mutations of FOXP3.Bennett C.L., Christie J., Ramsdell F., Brunkow M.E., Ferguson P.J., Whitesell L., Kelly T.E., Saulsbury F.T., Chance P.F., Ochs H.D.Nat. Genet. 27:20-21(2001) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 167466190
• NCBI GeneID: 50943
• NCBI Accession #: NP_001107849.1
• NCBI GenBank Nucleotide #: NM_001114377.1
• UniProt Accession #: Q9BZS1; O60827; Q14DD8; Q4ZH51; A5HJT1; B7ZLG0; B9UN80
• Molecular Weight: 31.7 kDa
• NCBI Official Full Name: forkhead box protein P3 isoform b
• NCBI Official Synonym Full Names: forkhead box P3
• NCBI Official Symbol: FOXP3
• NCBI Official Synonym Symbols: JM2; AIID; IPEX; PIDX; XPID; DIETER
• NCBI Protein Information: forkhead box protein P3
• UniProt Protein Name: Forkhead box protein P3
• Protein Family: Forkhead box protein
• UniProt Gene Name: FOXP3
• UniProt Synonym Gene Names: IPEX
• UniProt Entry Name: FOXP3_HUMAN

NCBI Description

The protein encoded by this gene is a member of the forkhead/winged-helix family of transcriptional regulators. Defects in this gene are the cause of immunodeficiency polyendocrinopathy, enteropathy, X-linked syndrome (IPEX), also known as X-linked autoimmunity-immunodeficiency syndrome. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]

Uniprot Description

FOXP3: Probable transcription factor. Plays a critical role in the control of immune response. Interacts with IKZF3. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: C2H2-type zinc finger protein; DNA-binding; Transcription factor; Cell cycle regulation

Chromosomal Location of Human Ortholog: Xp11.23

Cellular Component: cytoplasm; nucleus; protein complex

Molecular Function: histone acetyltransferase binding; histone deacetylase binding; metal ion binding; NF-kappaB binding; NFAT protein binding; protein binding; protein homodimerization activity; RNA polymerase II transcription factor activity, enhancer binding; sequence-specific DNA binding; transcription corepressor activity; transcription factor activity

Biological Process: anatomical structure morphogenesis; B cell homeostasis; CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment; chromatin remodeling; cytokine production; inhibition of CREB transcription factor; inhibition of NF-kappaB transcription factor; myeloid cell homeostasis; negative regulation of activated T cell proliferation; negative regulation of cell proliferation; negative regulation of chronic inflammatory response; negative regulation of cytokine biosynthetic process; negative regulation of cytokine secretion; negative regulation of histone acetylation; negative regulation of histone deacetylation; negative regulation of immune response; negative regulation of interferon-gamma biosynthetic process; negative regulation of interferon-gamma production; negative regulation of interleukin-10 production; negative regulation of interleukin-17 production; negative regulation of interleukin-2 biosynthetic process; negative regulation of interleukin-2 production; negative regulation of interleukin-4 production; negative regulation of interleukin-5 production; negative regulation of interleukin-6 production; negative regulation of isotype switching to IgE isotypes; negative regulation of T cell cytokine production; negative regulation of T cell proliferation; negative regulation of transcription factor activity; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of tumor necrosis factor production; positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; positive regulation of histone acetylation; positive regulation of immature T cell proliferation in the thymus; positive regulation of interleukin-4 production; positive regulation of peripheral T cell tolerance induction; positive regulation of T cell anergy; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; positive regulation of transforming growth factor-beta1 production; regulation of isotype switching to IgG isotypes; regulation of T cell anergy; regulation of transcription, DNA-dependent; response to virus; T cell activation; T cell homeostasis; T cell mediated immunity; T cell receptor signaling pathway; tolerance induction to self antigen; transcription, DNA-dependent

Disease: Diabetes Mellitus, Insulin-dependent; Immunodysregulation, Polyendocrinopathy, And Enteropathy, X-linked