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LearnMA1-41628
antibody from Invitrogen Antibodies
Targeting: FOXP3
AIID, DIETER, IPEX, JM2, PIDX, SCURFIN, XPID
Flow cytometryAntibody data
- Antibody Data
- Antigen structure
- References [24]
- Comments [0]
- Validations
- Flow cytometry [3]
- Other assay [1]
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- Product number
- MA1-41628 - Provider product page
- Provider
- Invitrogen Antibodies
- Product name
- FOXP3 Monoclonal Antibody (3G3), FITC
- Antibody type
- Monoclonal
- Antigen
- Other
- Description
- 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.
- Reactivity
- Human, Mouse
- Host
- Mouse
- Conjugate
- Green dye
- Isotype
- IgG
- Antibody clone number
- 3G3
- Vial size
- 100 µL
- Concentration
- 1.85 mg/mL
- Storage
- 4° C, store in dark
Submitted references Semaphorin 3A contributes to sepsis‑induced immunosuppression by impairing CD4(+) T cell anergy.
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.
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.
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
Compartmentation of alpha-internexin and neurofilament triplet proteins in cultured hippocampal neurons.
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
Identification of functional domains of the aryl hydrocarbon receptor.
Identification of functional domains of the aryl hydrocarbon receptor.
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90.
A tyrosine kinase-dependent pathway regulates ligand-dependent activation of the dioxin receptor in human keratinocytes.
All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome".
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex.
Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000.
Gao Y, Wang C, Wang Z, Li W, Liu Y, Shou S, Chai Y
Molecular medicine reports 2021 Apr;23(4)
Molecular medicine reports 2021 Apr;23(4)
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.
Dittmar KD, Pratt WB
The Journal of biological chemistry 1997 May 16;272(20):13047-54
The Journal of biological chemistry 1997 May 16;272(20):13047-54
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.
Dittmar KD, Pratt WB
The Journal of biological chemistry 1997 May 16;272(20):13047-54
The Journal of biological chemistry 1997 May 16;272(20):13047-54
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
Silverstein AM, Galigniana MD, Chen MS, Owens-Grillo JK, Chinkers M, Pratt WB
The Journal of biological chemistry 1997 Jun 27;272(26):16224-30
The Journal of biological chemistry 1997 Jun 27;272(26):16224-30
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
Silverstein AM, Galigniana MD, Chen MS, Owens-Grillo JK, Chinkers M, Pratt WB
The Journal of biological chemistry 1997 Jun 27;272(26):16224-30
The Journal of biological chemistry 1997 Jun 27;272(26):16224-30
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
Gradin K, McGuire J, Wenger RH, Kvietikova I, fhitelaw ML, Toftgård R, Tora L, Gassmann M, Poellinger L
Molecular and cellular biology 1996 Oct;16(10):5221-31
Molecular and cellular biology 1996 Oct;16(10):5221-31
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
Gradin K, McGuire J, Wenger RH, Kvietikova I, fhitelaw ML, Toftgård R, Tora L, Gassmann M, Poellinger L
Molecular and cellular biology 1996 Oct;16(10):5221-31
Molecular and cellular biology 1996 Oct;16(10):5221-31
Compartmentation of alpha-internexin and neurofilament triplet proteins in cultured hippocampal neurons.
Benson DL, Mandell JW, Shaw G, Banker G
Journal of neurocytology 1996 Mar;25(3):181-96
Journal of neurocytology 1996 Mar;25(3):181-96
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
Owens-Grillo JK, Czar MJ, Hutchison KA, Hoffmann K, Perdew GH, Pratt WB
The Journal of biological chemistry 1996 Jun 7;271(23):13468-75
The Journal of biological chemistry 1996 Jun 7;271(23):13468-75
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
Owens-Grillo JK, Czar MJ, Hutchison KA, Hoffmann K, Perdew GH, Pratt WB
The Journal of biological chemistry 1996 Jun 7;271(23):13468-75
The Journal of biological chemistry 1996 Jun 7;271(23):13468-75
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
Coumailleau P, Poellinger L, Gustafsson JA, Whitelaw ML
The Journal of biological chemistry 1995 Oct 20;270(42):25291-300
The Journal of biological chemistry 1995 Oct 20;270(42):25291-300
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
Coumailleau P, Poellinger L, Gustafsson JA, Whitelaw ML
The Journal of biological chemistry 1995 Oct 20;270(42):25291-300
The Journal of biological chemistry 1995 Oct 20;270(42):25291-300
Identification of functional domains of the aryl hydrocarbon receptor.
Fukunaga BN, Probst MR, Reisz-Porszasz S, Hankinson O
The Journal of biological chemistry 1995 Dec 8;270(49):29270-8
The Journal of biological chemistry 1995 Dec 8;270(49):29270-8
Identification of functional domains of the aryl hydrocarbon receptor.
Fukunaga BN, Probst MR, Reisz-Porszasz S, Hankinson O
The Journal of biological chemistry 1995 Dec 8;270(49):29270-8
The Journal of biological chemistry 1995 Dec 8;270(49):29270-8
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
McGuire J, Coumailleau P, Whitelaw ML, Gustafsson JA, Poellinger L
The Journal of biological chemistry 1995 Dec 29;270(52):31353-7
The Journal of biological chemistry 1995 Dec 29;270(52):31353-7
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
McGuire J, Coumailleau P, Whitelaw ML, Gustafsson JA, Poellinger L
The Journal of biological chemistry 1995 Dec 29;270(52):31353-7
The Journal of biological chemistry 1995 Dec 29;270(52):31353-7
The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90.
Hutchison KA, Stancato LF, Owens-Grillo JK, Johnson JL, Krishna P, Toft DO, Pratt WB
The Journal of biological chemistry 1995 Aug 11;270(32):18841-7
The Journal of biological chemistry 1995 Aug 11;270(32):18841-7
A tyrosine kinase-dependent pathway regulates 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 1994 Sep 23;269(38):23800-7
The Journal of biological chemistry 1994 Sep 23;269(38):23800-7
All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome".
Hutchison KA, Dittmar KD, Pratt WB
The Journal of biological chemistry 1994 Nov 11;269(45):27894-9
The Journal of biological chemistry 1994 Nov 11;269(45):27894-9
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
McGuire J, Whitelaw ML, Pongratz I, Gustafsson JA, Poellinger L
Molecular and cellular biology 1994 Apr;14(4):2438-46
Molecular and cellular biology 1994 Apr;14(4):2438-46
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
McGuire J, Whitelaw ML, Pongratz I, Gustafsson JA, Poellinger L
Molecular and cellular biology 1994 Apr;14(4):2438-46
Molecular and cellular biology 1994 Apr;14(4):2438-46
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
McGuire J, Whitelaw ML, Pongratz I, Gustafsson JA, Poellinger L
Molecular and cellular biology 1994 Apr;14(4):2438-46
Molecular and cellular biology 1994 Apr;14(4):2438-46
Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex.
Czar MJ, Owens-Grillo JK, Dittmar KD, Hutchison KA, Zacharek AM, Leach KL, Deibel MR Jr, Pratt WB
The Journal of biological chemistry 1994 Apr 15;269(15):11155-61
The Journal of biological chemistry 1994 Apr 15;269(15):11155-61
Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000.
Perdew GH, Whitelaw ML
The Journal of biological chemistry 1991 Apr 15;266(11):6708-13
The Journal of biological chemistry 1991 Apr 15;266(11):6708-13
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Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Flow cytometry analysis of FOXP3 using a monoclonal antibody (Product # MA1-41628).
- Conjugate
- Green dye
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Flow cytometry of FOXP3 in human PBMCs stimulated with anti-hCD3 (5 µg/mL) and rhIL-2 (10 ng/mL) for 48 hours. Samples were incubated in FOXP3 monoclonal antibody (Product # MA1-41628) using a dilution of 5 µg/10^6 cells and isotype control (left). Products used: anti-CD4 PE conjugate , anti-CD25 APC conjugate , anti-FOXP3 FITC conjugate.
- Conjugate
- Green dye
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Flow cytometry of FOXP3 in mouse splenocytes stimulated with anti-mCD3 (5 µg/mL) and rmIL-2 (10 ng/mL) for 48 hours using isotype control (left) and (right). Samples were incubated in FOXP3 monoclonal antibody (Product # MA1-41628) using a dilution of 0.5 µg/10^6 cells.
- Conjugate
- Green dye
Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Figure 5. Sema3A-mediated autocrine loop enhances the expression of Foxp-3 in CD4 + T cells during LPS-induced sepsis. (A) Statistical analysis and (B) representative flow cytometry images protein levels of Foxp-3. Data are presented as the mean +- standard deviation, n=4 per group. One-way ANOVA was performed for data analysis. **P
- Conjugate
- Green dye
