Immunofluorescent analysis of Phalloidin (orange) and PDI (green) in NIH 3T3 cells. Formalin fixed cells were permeabilized with 0.1% Triton X-100 in PBS for 10 minutes at room temperature and blocked with 2% BSA (Product # 37525) in PBS + 0.1% Triton X-100 for 30 minutes at room temperature. Cells were probed with a PDI monoclonal antibody (Product # MA3-019) at a dilution of 1:75 for at least 1 hour at room temperature, washed with PBS, and incubated with DyLight 488 goat anti-mouse IgG secondary antibody (Product # 35502) at a dilution of 1:250 for 30 minutes at room temperature. Actin was stained with DyLight 550 Phalloidin (Product # 21835) at a dilution of 1:120 (2.5 units/ml final concentration) and nuclei (blue) were stained with Hoechst (Product # 62249) at a concentration of 1ug/ml for 30 minutes. Images were taken on a Zeiss Axio Observer Z1 microscope at 20X magnification.
|Tested species reactivity||Hamster, Human, Mouse, Pig, Rat|
|Published species reactivity||Rat, Non-human primate, Hamster, Human, Mouse, Not Applicable, Rhesus monkey|
|Host / Isotype||Mouse / IgG2a|
|Immunogen||Purified rat PDI protein.|
|Storage buffer||1mg/ml BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Flow Cytometry (Flow)||0.5-1 ug/test|
|Immunohistochemistry (Frozen) (IHC (F))||1:100|
|Immunohistochemistry (Paraffin) (IHC (P))||1:100|
|Immunomicroscopy (IM)||Assay Dependent|
|Immunoprecipitation (IP)||Assay dependent|
|Western Blot (WB)||1:200-1:2000|
* 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.
|Immunocytochemistry (ICC)||See 16 publications below|
|Miscellaneous PubMed (MISC)||See 1 publications below|
|Western Blot (WB)||See 10 publications below|
|Immunohistochemistry (IHC)||See 5 publications below|
|Flow Cytometry (Flow)||See 1 publications below|
|Immunoprecipitation (IP)||See 2 publications below|
|Blocking Assay (BLOCK)||See 2 publications below|
MA3-019 detects protein disulphide-isomerase (PDI) from human, rat, porcine and mouse tissues as well as hamster cells.
MA3-019 has been successfully used in Western blot, immunofluorescence, immunohistochemical, flow cytometry, and immunoprecipitation procedures. By Western blot, this antibody detects a protein at 59 kDa representing PDI from rat liver extract or a slightly higher protein at 61 kDa representing PDI from human liver extract. Immunohistochemical staining of PDI in rat intestine with MA3-019 yields a pattern consistent with cytoplasmic staining. In immunoprecipitation procedures MA3-019 has been shown to inhibit the activity of PDI in vitro. MA3-019 has also been found to inhibit disulfide bond reduction of the HIV protein, gp120, at the cell surface of CHO cells and human lymphoid cells.
In immunohistochemistry procedures, formalin-fixed paraffin-embedded tissue sections are recommended.
The MA3-019 antigen is purified rat PDI.
The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide-Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
|Not Applicable||Not Cited||
Optogenetic acidification of synaptic vesicles and lysosomes.
MA3-019 was used in immunocytochemistry to analyze synaptic vesicles and lysosomes and optogenetic acidification
|Rost BR,Schneider F,Grauel MK,Wozny C,Bentz CG,Blessing A,Rosenmund T,Jentsch TJ,Schmitz D,Hegemann P,Rosenmund C||Nature neuroscience (18:1845)||2015|
Biogenesis and cytotoxicity of APOL1 renal risk variant proteins in hepatocytes and hepatoma cells.
MA3-019 was used in immunocytochemistry to study the trafficking behavior of circulating APOL1 from the liver
|Cheng D,Weckerle A,Yu Y,Ma L,Zhu X,Murea M,Freedman BI,Parks JS,Shelness GS||Journal of lipid research (56:1583)||2015|
|Rhesus monkey||Not Cited||
Optogenetic control of organelle transport and positioning.
MA3-019 was used in immunocytochemistry to establish a method of optical control of intracellular transport using light-sensitive heterodimerization to recruit specific cytoskeletal motor proteins to selected cargoes and test how local positioning of recycling endosomes contributes to axon
|van Bergeijk P,Adrian M,Hoogenraad CC,Kapitein LC||Nature (518:111)||2015|
Characterization of N-glycosylation sites on the extracellular domain of NOX1/NADPH oxidase.
MA3-019 was used in immunocytochemistry to identify N-glycosylation sites on the NOX1 subunit of NADPH oxidase
|Matsumoto M,Katsuyama M,Iwata K,Ibi M,Zhang J,Zhu K,Nauseef WM,Yabe-Nishimura C||Free radical biology and medicine (68:196)||2014|
NLRP7, a nucleotide oligomerization domain-like receptor protein, is required for normal cytokine secretion and co-localizes with Golgi and the microtubule-organizing center.
MA3-019 was used in immunocytochemistry to investigate the role of NLRP7 in normal cytokine secretion and its colocalization with Golgi
|Messaed C,Akoury E,Djuric U,Zeng J,Saleh M,Gilbert L,Seoud M,Qureshi S,Slim R||The Journal of biological chemistry (286:43313)||2011|
Elimination of hepatitis C virus from hepatocytes by a selective activation of therapeutic molecules.
MA3-019 was used in immunocytochemistry to evaluate the efficacy of gene transfer therapy in clearing hepatitis C virus from hepatocytes
|Wen X,Abe T,Kukihara H,Taguwa S,Mori Y,Tani H,Kato N,Suzuki T,Tatsumi M,Moriishi K,Matsuura Y||PloS one (6:null)||2011|
Production of anti-carbohydrate antibodies by phage display technologies: potential impairment of cell growth as a result of endogenous expression.
MA3-019 was used in immunocytochemistry to investigate production of anti-carbohydrate antibodies by phage display technology
|Yuasa N,Zhang W,Goto T,Sakaue H,Matsumoto-Takasaki A,Kimura M,Ohshima H,Tsuchida Y,Koizumi T,Sakai K,Kojima T,Yamamoto K,Nakata M,Fujita-Yamaguchi Y||The Journal of biological chemistry (285:30587)||2010|
Characterization of the expression, localization, and secretion of PANDER in alpha-cells.
MA3-019 was used in immunocytochemistry to investigate the properties of PANDER in alpha-cells
|Carnegie JR,Robert-Cooperman CE,Wu J,Young RA,Wolf BA,Burkhardt BR||Molecular and cellular endocrinology (325:36)||2010|
Membrane topology of human AGPAT3 (LPAAT3).
MA3-019 was used in immunocytochemistry to investigate the structural arrangement of AGPAT3 in membrane and its significance in the enzymatic activity
|Schmidt JA,Yvone GM,Brown WJ||Biochemical and biophysical research communications (397:661)||2010|
DC-STAMP interacts with ER-resident transcription factor LUMAN which becomes activated during DC maturation.
MA3-019 was used in immunocytochemistry to study the interaction between DC-STAMP interacts and estrogen receptor-resident transcription factor LUMAN
|Eleveld-Trancikova D,Sanecka A,van Hout-Kuijer MA,Looman MW,Hendriks IA,Jansen BJ,Adema GJ||Molecular immunology (47:1963)||2010|
Biomechanical stress induces novel arterial intima-enriched genes: implications for vascular adaptation to stress.
MA3-019 was used in immunocytochemistry to study the role of biomechanical stress in vascular pathologies
|Pyle AL,Li B,Maupin AB,Guzman RJ,Crimmins DL,Olson S,Atkinson JB,Young PP||Cardiovascular pathology : the official journal of the Society for Cardiovascular Pathology (19:e13)||2010|
Calsyntenins mediate TGN exit of APP in a kinesin-1-dependent manner.
MA3-019 was used in immunocytochemistry to study the role kinesisn-1 in the calsyntenin-mediated trans-Golgi network exit of amyloid precursor protein
|Ludwig A,Blume J,Diep TM,Yuan J,Mateos JM,Leuthäuser K,Steuble M,Streit P,Sonderegger P||Traffic (Copenhagen, Denmark) (10:572)||2009|
Dynamics of somatostatin type 2A receptor cargoes in living hippocampal neurons.
MA3-019 was used in immunocytochemistry to investigate the intracellular trafficking of somatostatin type 2A receptor cargoes in living hippocampal neurons.
|Lelouvier B,Tamagno G,Kaindl AM,Roland A,Lelievre V,Le Verche V,Loudes C,Gressens P,Faivre-Baumann A,Lenkei Z,Dournaud P||The Journal of neuroscience : the official journal of the Society for Neuroscience (28:4336)||2008|
The dendritic cell-derived protein DC-STAMP is highly conserved and localizes to the endoplasmic reticulum.
MA3-019 was used in immunocytochemistry to characterize the dendritic cell-derived protein DC-STAMP
|Eleveld-Trancikova D,Triantis V,Moulin V,Looman MW,Wijers M,Fransen JA,Lemckert AA,Havenga MJ,Figdor CG,Janssen RA,Adema GJ||Journal of leukocyte biology (77:337)||2005|
Structural requirements for the apical sorting of human multidrug resistance protein 2 (ABCC2).
MA3-019 was used in immunocytochemistry to perform structural analysis to identify the necessary components for apical sorting of human MRP2
|Nies AT,König J,Cui Y,Brom M,Spring H,Keppler D||European journal of biochemistry (269:1866)||2002|
|Human||5 ul/100 ul||
Sulfhydryl regulation of L-selectin shedding: phenylarsine oxide promotes activation-independent L-selectin shedding from leukocytes.
MA3-019 was used in immunocytochemistry to study the expression and the function of protein-disulfide isomerase.
|Bennett TA,Edwards BS,Sklar LA,Rogelj S||Journal of immunology (Baltimore, Md. : 1950) (164:4120)||2000|
An analysis of critical factors for quantitative immunoblotting.
MA3-019 was used in western blot to examine an immunoblot-analysis workflow for accuracy and precision
|Janes KA||Science signaling (8:null)||2015|
|Not Applicable||Not Cited||
Oxidoreductase activity is necessary for N-glycosylation of cysteine-proximal acceptor sites in glycoproteins.
MA3-019 was used in western blot to determine how N-glycosylation of cysteine-proximal acceptor sites in glycoproteins requires oxidoreductase activity
|Cherepanova NA,Shrimal S,Gilmore R||The Journal of cell biology (206:525)||2014|
Effects of oxidative stress on the solubility of HRD1, a ubiquitin ligase implicated in Alzheimer's disease.
MA3-019 was used in western blot to study the effects of oxidative stress on the solubility of the Alzheimer's disease-associated E3 ubiquitin ligase HRD1
|Saito R,Kaneko M,Kitamura Y,Takata K,Kawada K,Okuma Y,Nomura Y||PloS one (9:null)||2014|
Transport of estradiol-17ß-glucuronide, estrone-3-sulfate and taurocholate across the endoplasmic reticulum membrane: evidence for different transport systems.
MA3-019 was used in western blot to study the involvement of different systems in the ER transport of estradiol-17beta-glucuronide, estrone-3-sulfate and taurocholate
|Wlcek K,Hofstetter L,Stieger B||Biochemical pharmacology (88:106)||2014|
Unraveling the human dendritic cell phagosome proteome by organellar enrichment ranking.
MA3-019 was used in western blot to study the protein composition of phagosomes from human dendritic cell phagosome
|Buschow SI,Lasonder E,Szklarczyk R,Oud MM,de Vries IJ,Figdor CG||Journal of proteomics (75:1547)||2012|
mRNA escape from stress granule sequestration is dictated by localization to the endoplasmic reticulum.
MA3-019 was used in western blot to investigate the process of mRNA translation during stress response
|Unsworth H,Raguz S,Edwards HJ,Higgins CF,Yagüe E||FASEB journal : official publication of the Federation of American Societies for Experimental Biology (24:3370)||2010|
Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation.
MA3-019 was used in western blot to study role of protein degradation on endoplasmic reticulum stress and Alzheimer plaque deposits
|Kaneko M,Koike H,Saito R,Kitamura Y,Okuma Y,Nomura Y||The Journal of neuroscience : the official journal of the Society for Neuroscience (30:3924)||2010|
Endoplasmic reticulum (ER) chaperone regulation and survival of cells compensating for deficiency in the ER stress response kinase, PERK.
MA3-019 was used in western blot to study the relationship between endoplasmic reticulum chaperone regulation and the endoplasmic reticulum stress response kinase PERK.
|Yamaguchi Y,Larkin D,Lara-Lemus R,Ramos-Castañeda J,Liu M,Arvan P||The Journal of biological chemistry (283:17020)||2008|
Comparative proteomics profiling of a phospholamban mutant mouse model of dilated cardiomyopathy reveals progressive intracellular stress responses.
MA3-019 was used in western blot to perform the global proteomics surveys of cardiac ventricle of a phospholamban mutant mouse
|Gramolini AO,Kislinger T,Alikhani-Koopaei R,Fong V,Thompson NJ,Isserlin R,Sharma P,Oudit GY,Trivieri MG,Fagan A,Kannan A,Higgins DG,Huedig H,Hess G,Arab S,Seidman JG,Seidman CE,Frey B,Perry M,Backx PH,Liu PP,MacLennan DH,Emili A||Molecular and cellular proteomics : MCP (7:519)||2008|
A cellular UDP-glucose deficiency causes overexpression of glucose/oxygen-regulated proteins independent of the endoplasmic reticulum stress elements.
MA3-019 was used in western blot to determine the effect of cellular UDP-Glc level on stress protein expression.
|Flores-Diaz M,Higuita JC,Florin I,Okada T,Pollesello P,Bergman T,Thelestam M,Mori K,Alape-Giron A||The Journal of biological chemistry (279:21724)||2004|
Dimerization of P-selectin in platelets and endothelial cells.
MA3-019 was used in western blot to investigate P-selectin dimerization in human umbilical vein endothelial cells and resting platelets and the unique properties of the dimers.
|Barkalow FJ,Barkalow KL,Mayadas TN||Blood (96:3070)||2000|
mRNA redistribution during permanent focal cerebral ischemia.
MA3-019 was used in immunohistochemistry to study mRNA granule formation following experimental permanent focal cerebral ischemia
|Lewis MK,Jamison JT,Dunbar JC,DeGracia DJ||Translational stroke research (4:604)||2013|
Regulation of ER molecular chaperone prevents bone loss in a murine model for osteoporosis.
MA3-019 was used in immunohistochemistry to investigate the effect of endoplasmic reticulum stress on bone balance in a mouse osteoporosis model
|Hino S,Kondo S,Yoshinaga K,Saito A,Murakami T,Kanemoto S,Sekiya H,Chihara K,Aikawa Y,Hara H,Kudo T,Sekimoto T,Funamoto T,Chosa E,Imaizumi K||Journal of bone and mineral metabolism (28:131)||2010|
Activated somatostatin type 2 receptors traffic in vivo in central neurons from dendrites to the trans Golgi before recycling.
MA3-019 was used in immunohistochemistry to investigate the trafficking and recycling of activated somatostatin type 2 receptors in vivo in central neurons
|Csaba Z,Lelouvier B,Viollet C,El Ghouzzi V,Toyama K,Videau C,Bernard V,Dournaud P||Traffic (Copenhagen, Denmark) (8:820)||2007|
Restricted distribution of mRNAs encoding a sarcoplasmic reticulum or transverse tubule protein in skeletal myofibers.
MA3-019 was used in immunohistochemistry to investigate the distribution of CSQ and DHPR proteins and corresponding mRNAs during myogenic development
|Nissinen M,Kaisto T,Salmela P,Peltonen J,Metsikkö K||The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society (53:217)||2005|
Selective intracellular retention of extracellular matrix proteins and chaperones associated with pseudoachondroplasia.
MA3-019 was used in immunohistochemistry to study the mechanism for the cytoplasmic accumulation of extracellular matrix proteins and chaperones associated in pseudoachondroplasia
|Vranka J,Mokashi A,Keene DR,Tufa S,Corson G,Sussman M,Horton WA,Maddox K,Sakai L,Bächinger HP||Matrix biology : journal of the International Society for Matrix Biology (20:439)||2001|
|Non-human primate||Not Cited||
Inhibiting rotavirus infection by membrane-impermeant thiol/disulfide exchange blockers and antibodies against protein disulfide isomerase.
MA3-019 was used in flow cytometry to study the ability of non-cell-penetrating thiol-disulphide exchange inhibitors to reduce rotavirus infectivity and the potential involvement of protein disulfide isomerase
|Calderon MN,Guerrero CA,Acosta O,Lopez S,Arias CF||Intervirology (55:451)||2012|
Protein disulfide isomerase (PDI) associates with NADPH oxidase and is required for phagocytosis of Leishmania chagasi promastigotes by macrophages.
MA3-019 was used in immunoprecipitation to investigate the role of protein disulfide isomerase (PDI) during phagocytosis of Leishmania chagasi promastigotes by macrophages
|Santos CX,Stolf BS,Takemoto PV,Amanso AM,Lopes LR,Souza EB,Goto H,Laurindo FR||Journal of leukocyte biology (86:989)||2009|
Intracellularly located misfolded glycoprotein hormone receptors associate with different chaperone proteins than their cognate wild-type receptors.
MA3-019 was used in immunoprecipitation to study the folding of the glycoprotein hormone receptors and their misfolded mutants .
|Mizrachi D,Segaloff DL||Molecular endocrinology (Baltimore, Md.) (18:1768)||2004|
Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1.
MA3-019 was used in blocking/activating experiment to investigate the role of enzymatically catalyzed disulfide exchange for platelet adhesion to collagen via integrin alpha2beta1
|Lahav J,Wijnen EM,Hess O,Hamaia SW,Griffiths D,Makris M,Knight CG,Essex DW,Farndale RW||Blood (102:2085)||2003|
Protein disulfide isomerase, a component of the estrogen receptor complex, is associated with Chlamydia trachomatis serovar E attached to human endometrial epithelial cells.
MA3-019 was used in blocking/activating experiment to investigate the role of protein disulfide isomerase in the infectivity of Chlamydia trachomatis serovar E
|Davis CH,Raulston JE,Wyrick PB||Infection and immunity (70:3413)||2002|