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Immunofluorescent analysis of Cyclophilin D in HepG2 Cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a Cyclophilin D polyclonal antibody (Product # PA3-022) at a dilution of 1:200 overnight at 4 C, washed with PBS and incubated with a DyLight-488 conjugated secondary antibody (Product # 35552). Cyclophilin D staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Images were taken at 60X magnification.
|Tested species reactivity||Human, Mouse, Rat|
|Published species reactivity||Rabbit, Rat, Primate, Bovine, Mouse, Human, Chicken|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic peptide corresponding to residues C A(356) Q K D K E K A V Y A K M F A(370) of human Cyp-40.|
|Storage buffer||whole serum diluted in PBS|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Flow Cytometry (Flow)||Assay dependent|
|Gel Shift (GS)||Assay dependent|
|Immunocytochemistry (ICC)||Assay dependent|
|Immunohistochemistry (Frozen) (IHC (F))||1:100|
|Immunoprecipitation (IP)||Assay dependent|
|Western Blot (WB)||1:1,000|
* 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.
PA3-022 detect cyclophilin 40 (CyP-40) from human and rat and mouse tissues and cells. This antibody does not cross-react with CyPA.
PA3-022 has been successfully used in Western blot, iF, immunohistochemistry, immunocytochemistry, immunoprecipitation, gel shift and FACS procedures. By Western blot, this antibody detects a 40 kDa protein representing CyP-40 from rat brain extract.
The PA3-022 immunogen is a synthetic peptide corresponding to residues C A(356) Q K D K E K A V Y A K M F A(370) of human Cyp-40.
Immunophilins are a family of soluble cytosolic receptors capable of binding to one of two major immunosuppressant agents: cyclosporin A (CsA) or FK506. Proteins that bind FK506 are termed FK506 Binding Proteins (FKBPs) and those that bind cyclosporin A are called cyclophilins (CyP).
Both CyP:CsA and FKBP:FK506 complexes have been shown to inhibit calcineurin, a calcium and calmodulin dependent protein phosphatase which has been implicated as an important signaling enzyme in T-cell activation, providing a possible mechanism of immunosuppression by CsA and FK506. Immunophilins function as peptidyl prolyl cis-trans-isomerases (PPIase) whose activity is inhibited by their respective immunosuppressant compounds. As PPIase's, immunophilins accelerate folding of some proteins both in vivo and in vitro by catalyzing slow steps in the initial folding and rearrangement of proline containing proteins.
CyP-40, a 40 kDa protein, shares significant homology with smaller CyPA (CyP-18) and FKBP59. CyP-40 exhibits the characteristic CsA binding and isomerase activity of CyP-18, though these activities appear to be less with CyP-40 than with Cyp-18. Like FKBP59, CyP-40 has been found in progesterone receptor complexes. CyP-40 is expressed at similar levels in many tissues.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
FKBP51 controls cellular adipogenesis through p38 kinase-mediated phosphorylation of GRα and PPARγ.
PA3-022 was used in western blot to explore the effects of FK506-binding protein 51 (FKBP51) deletion on adipogenesis
|Stechschulte LA,Hinds TD,Khuder SS,Shou W,Najjar SM,Sanchez ER||Molecular endocrinology (Baltimore, Md.) (28:1265)||2014|
Identification of cyclophilin-40-interacting proteins reveals potential cellular function of cyclophilin-40.
PA3-022 was used in western blot to identify cyclophilin-40-interacting proteins and the cellular functions of cyclophilin-40
|Park MS,Chu F,Xie J,Wang Y,Bhattacharya P,Chan WK||Analytical biochemistry (410:257)||2011|
Susceptibility to diet-induced hepatic steatosis and glucocorticoid resistance in FK506-binding protein 52-deficient mice.
PA3-022 was used in western blot to study the role of FK506-binding protein 52 in hepatic integrity and glucocorticoid responsiveness in mice
|Warrier M,Hinds TD,Ledford KJ,Cash HA,Patel PR,Bowman TA,Stechschulte LA,Yong W,Shou W,Najjar SM,Sanchez ER||Endocrinology (151:3225)||2010|
FKBP51 and Cyp40 are positive regulators of androgen-dependent prostate cancer cell growth and the targets of FK506 and cyclosporin A.
PA3-022 was used in western blot to study the expression of FKBP51 and Cyp40 in prostate cancer tissues and their role in promoting androgen-dependent cell growth
|Periyasamy S,Hinds T,Shemshedini L,Shou W,Sanchez ER||Oncogene (29:1691)||2010|
The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events.
PA3-022 was used in western blot to investigate the role of the heat shock protein 90-FKBP52 complex in the nucleus
|Galigniana MD,Erlejman AG,Monte M,Gomez-Sanchez C,Piwien-Pilipuk G||Molecular and cellular biology (30:1285)||2010|
Targeted ablation reveals a novel role of FKBP52 in gene-specific regulation of glucocorticoid receptor transcriptional activity.
PA3-022 was used in western blot to investigate the role of FKBP52 in regulation of glucocorticoid receptor (GR) activity in vivo
|Wolf IM,Periyasamy S,Hinds T,Yong W,Shou W,Sanchez ER||The Journal of steroid biochemistry and molecular biology (113:36)||2009|
Control of glucocorticoid and progesterone receptor subcellular localization by the ligand-binding domain is mediated by distinct interactions with tetratricopeptide repeat proteins.
PA3-022 was used in western blot to investigate the effect of the ligand-binding domain on glucocorticoid and progesterone receptor subcellular localization and its mechanism
|Banerjee A,Periyasamy S,Wolf IM,Hinds TD,Yong W,Shou W,Sanchez ER||Biochemistry (47:10471)||2008|
The immunophilin ligands cyclosporin A and FK506 suppress prostate cancer cell growth by androgen receptor-dependent and -independent mechanisms.
PA3-022 was used in western blot to study the effect of immunophilin ligands cyclosporin A and FK506 on prostate cancer cell growth and its mechanism
|Periyasamy S,Warrier M,Tillekeratne MP,Shou W,Sanchez ER||Endocrinology (148:4716)||2007|
Essential role for Co-chaperone Fkbp52 but not Fkbp51 in androgen receptor-mediated signaling and physiology.
PA3-022 was used in western blot to study the roles of FKBP52 and FKBP51 in androgen receptor functions.
|Yong W,Yang Z,Periyasamy S,Chen H,Yucel S,Li W,Lin LY,Wolf IM,Cohn MJ,Baskin LS,Sánchez ER,Shou W||The Journal of biological chemistry (282:5026)||2007|
Physiological role for the cochaperone FKBP52 in androgen receptor signaling.
PA3-022 was used in western blot to characterize FKBP52 and study its roles in some male reproductive tissues.
|Cheung-Flynn J,Prapapanich V,Cox MB,Riggs DL,Suarez-Quian C,Smith DF||Molecular endocrinology (Baltimore, Md.) (19:1654)||2005|
Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506.
PA3-022 was used in western blot to investigate the regulatory effects of FK506 and TPR proteins on glucocorticoid receptor hormone-binding function
|Davies TH,Ning YM,Sánchez ER||Biochemistry (44:2030)||2005|
Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria.
PA3-022 was used in western blot to study the role of PKC epsilon in cardiac mitochondria
|Baines CP,Song CX,Zheng YT,Wang GW,Zhang J,Wang OL,Guo Y,Bolli R,Cardwell EM,Ping P||Circulation research (92:873)||2003|
p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules.
PA3-022 was used in western blot to investigate the role of p50(cdc37) in heat shock protein 90 molecular chaperone function
|Hartson SD,Irwin AD,Shao J,Scroggins BT,Volk L,Huang W,Matts RL||Biochemistry (39:7631)||2000|
Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein.
PA3-022 was used in western blot to study the binding site for the association between FKBP52/dimer and hsp90
|Silverstein AM,Galigniana MD,Kanelakis KC,Radanyi C,Renoir JM,Pratt WB||The Journal of biological chemistry (274:36980)||1999|
p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site.
PA3-022 was used in western blot to investigate the mechanism for the interactions among cdc37, Raf, and hsp90
|Silverstein AM,Grammatikakis N,Cochran BH,Chinkers M,Pratt WB||The Journal of biological chemistry (273:20090)||1998|
Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor.
PA3-022 was used in western blot to study the interactions between Hsp90-associated immunophilins and target proteins
|Nair SC,Rimerman RA,Toran EJ,Chen S,Prapapanich V,Butts RN,Smith DF||Molecular and cellular biology (17:594)||1997|
The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant.
PA3-022 was used in western blot to investigate the role of tetratricopeptide repeat (TPR) domain of protein phosphatase 5 (PP5) in GR signaling
|Chen MS,Silverstein AM,Pratt WB,Chinkers M||The Journal of biological chemistry (271:32315)||1996|
A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor.
PA3-022 was used in western blot to show the involvement of Cyp40 in the formation of unactivated progesterone receptor complex
|Nair SC,Toran EJ,Rimerman RA,Hjermstad S,Smithgall TE,Smith DF||Cell stress & chaperones (1:237)||1996|
Reconstitution of the steroid receptor.hsp90 heterocomplex assembly system of rabbit reticulocyte lysate.
PA3-022 was used in western blot to reconstitute a minimal GR-hsp90 heterocomplex assembly system
|Dittmar KD,Hutchison KA,Owens-Grillo JK,Pratt WB||The Journal of biological chemistry (271:12833)||1996|
Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent.
PA3-022 was used in western blot to investigate the assembly pathway of progesterone receptor complexes
|Smith DF,Whitesell L,Nair SC,Chen S,Prapapanich V,Rimerman RA||Molecular and cellular biology (15:6804)||1995|
The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor.
PA3-022 was used in western blot to investigate the role of immunophilins in steroid receptor action
|Owens-Grillo JK,Hoffmann K,Hutchison KA,Yem AW,Deibel MR,Handschumacher RE,Pratt WB||The Journal of biological chemistry (270:20479)||1995|
Interaction of the progesterone receptor with binding proteins for FK506 and cyclosporin A.
PA3-022 was used in western blot to investigate the interaction between progesterone receptor complexes and immunophilins
|Milad M,Sullivan W,Diehl E,Altmann M,Nordeen S,Edwards DP,Toft DO||Molecular endocrinology (Baltimore, Md.) (9:838)||1995|
Cyclophilin-40: evidence for a dimeric complex with hsp90.
PA3-022 was used in western blot to identify the cellular components interacting with CyP-40
|Hoffmann K,Handschumacher RE||The Biochemical journal (307 ( Pt 1):5)||1995|
Inhibition of cyclophilins alters lipid trafficking and blocks hepatitis C virus secretion.
PA3-022 was used in immunocytochemistry to investigate the effect of cyclophilin blockade on HCV release
|Anderson LJ,Lin K,Compton T,Wiedmann B||Virology journal (8:null)||2011|
Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1.
PA3-022 was used in immunoprecipitation to show that CyP40 can not activate heat shock transcription factor 1
|Zou J,Guo Y,Guettouche T,Smith DF,Voellmy R||Cell (94:471)||1998|
Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants.
PA3-022 was used in immunoprecipitation to investigate the interaction of various Hsp90 mutants with PR complexes and Hsp90 accessories in vitro
|Chen S,Sullivan WP,Toft DO,Smith DF||Cell stress & chaperones (3:118)||1998|
The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent.
PA3-022 was used in immunohistochemistry to investigate the mechanisms for the aberrant association of chaperones and mutant p53 and the intracellular accumulation of mutant p53.
|Whitesell L,Sutphin PD,Pulcini EJ,Martinez JD,Cook PH||Molecular and cellular biology (18:1517)||1998|
40 kDa peptidyl-prolyl cis-trans isomerase; 40 kDa peptidyl-prolyl cis-trans isomerase D; cyclophilin 40; Cyclophilin D; cyclophilin-40; cyclophilin-related protein; Cyp 40; CypD; cytoplasmic cyclophilin D; peptidyl-prolyl cis-trans isomerase D; PPIase D; PPID; rotamase D; testicular tissue protein Li 147
4930564J03Rik; CYP-40; CYP40; CYPD; PPID; Ppidl; Ppif