SOD2/Mn-SOD Antibody - BSA Free

Immunohistochemistry: SOD2/Mn-SOD Antibody [NB100-1992] - The effects of a high calcium/phosphate diet, of 1,25(OH)2D3, and of antioxidant supplementation on oxidative stress, DNA damage, and protein expression of oncogenes and tumor suppressive genes in 1alpha(OH)ase -/- mice. Mice from each group were treated as described in Figure 1. Representative micrographs of skin sections stained immunohistochemically for SOD2 and gamma-H2AX. Scale bars represent 50 um. Image collected and cropped by CiteAb from the following publication (//onlinelibrary.wiley.com/doi/abs/10.1111/acel.12951), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: SOD2/Mn-SOD Antibody [NB100-1992] - Analysis using Rabbit Anti-SOD (Mn) Polyclonal Antibody. Tissue: HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-SOD (Mn) Polyclonal Antibody at 1:120 for 12 hours at 4 degrees C. Secondary Antibody: R-PE Goat Anti-Rabbit (yellow) at 1:200 for 120 min at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 120 min at RT. Localization: Mitochondrion matrix. Magnification: 100x. (A) DAPI (blue) nuclear stain. (B) Anti-SOD (Mn) Antibody. (C) Composite.

Western Blot: SOD2/Mn-SOD Antibody [NB100-1992] - Western blot analysis of Rat Tissue lysates showing detection of SOD2/Mn-SOD protein using Rabbit Anti-SOD2/Mn-SOD Polyclonal Antibody (NB100-1992). Load: 15 ugprotein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Rabbit Anti-SOD2/Mn-SOD Polyclonal Antibody (NB100-1992) at 1:1000 for 2 hours at RT. Secondary Antibody: Donkey Anti-Rabbit IgG: HRP for 1 hour at RT.

Immunocytochemistry/Immunofluorescence: SOD2/Mn-SOD Antibody [NB100-1992] - Analysis using Rabbit Anti-SOD (Mn) Polyclonal Antibody. Tissue: HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-SOD (Mn) Polyclonal Antibody at 1:120 for 12 hours at 4 degrees C. Secondary Antibody: APC Goat Anti-Rabbit (red) at 1:200 for 120 min at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 120 min at RT. Localization: Mitochondrion matrix. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-SOD (Mn) Antibody. (C) Composite.

Immunohistochemistry: SOD2/Mn-SOD Antibody [NB100-1992] - Immunohistochemistry analysis using Rabbit Anti-SOD2/Mn-SOD Polyclonal Antibody (NB100-1992). Tissue: backskin. Species: Mouse. Fixation: Bouin's Fixative Solution. Primary Antibody: Rabbit Anti-SOD2/Mn-SOD Polyclonal Antibody (NB100-1992) at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Rabbit (green) at 1:50 for 1 hour at RT. Localization: Mitochondrion matrix.

Immunohistochemistry: SOD2/Mn-SOD Antibody [NB100-1992] - SOD2 mRNA & protein expression. RT-PCR: (A) SOD2 mRNA expression is higher in adults, & highest in the adult parenchyma. (B) No exposure effects on SOD2 mRNA were observed in neonates. (C) Adult SOD2 mRNA was decreased in PFP48. Data are presented as mean+SEM (n=5-7 rats/group, in each compartment), * significantly different compared to neonates in the same compartment, † significantly different compared to airways in the same age, ‡ significantly different compared to FA in the same compartment. Western blotting: (D) Scan of representative SOD2 & actin blots. (E) Neonatal whole lung SOD2 protein expression was unchanged with exposure, & (F) adult whole lung SOD2 protein trended upwards at PFP2, but was statistically insignificant. (G-J) Immunohistochemical localization of SOD2 in lung (n=6 rats/group). SOD2 protein was more abundant in adults compared to neonates, but no exposure specific differences were observed. Scale bar is 50 μm. Image collected & cropped by CiteAb from the following publication (//particleandfibretoxicology.biomedcentral.com/articles/10.1186/1743-8977-10-34), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: SOD2/Mn-SOD Antibody [NB100-1992] - SOD2 mRNA & protein expression. RT-PCR: (A) SOD2 mRNA expression is higher in adults, & highest in the adult parenchyma. (B) No exposure effects on SOD2 mRNA were observed in neonates. (C) Adult SOD2 mRNA was decreased in PFP48. Data are presented as mean+SEM (n=5-7 rats/group, in each compartment), * significantly different compared to neonates in the same compartment, † significantly different compared to airways in the same age, ‡ significantly different compared to FA in the same compartment. Western blotting: (D) Scan of representative SOD2 & actin blots. (E) Neonatal whole lung SOD2 protein expression was unchanged with exposure, & (F) adult whole lung SOD2 protein trended upwards at PFP2, but was statistically insignificant. (G-J) Immunohistochemical localization of SOD2 in lung (n=6 rats/group). SOD2 protein was more abundant in adults compared to neonates, but no exposure specific differences were observed. Scale bar is 50 μm. Image collected & cropped by CiteAb from the following publication (//particleandfibretoxicology.biomedcentral.com/articles/10.1186/1743-8977-10-34), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: SOD2/Mn-SOD Antibody [NB100-1992] - SOD2 mRNA & protein expression. RT-PCR: (A) SOD2 mRNA expression is higher in adults, & highest in the adult parenchyma. (B) No exposure effects on SOD2 mRNA were observed in neonates. (C) Adult SOD2 mRNA was decreased in PFP48. Data are presented as mean+SEM (n=5-7 rats/group, in each compartment), * significantly different compared to neonates in the same compartment, † significantly different compared to airways in the same age, ‡ significantly different compared to FA in the same compartment. Western blotting: (D) Scan of representative SOD2 & actin blots. (E) Neonatal whole lung SOD2 protein expression was unchanged with exposure, & (F) adult whole lung SOD2 protein trended upwards at PFP2, but was statistically insignificant. (G-J) Immunohistochemical localization of SOD2 in lung (n=6 rats/group). SOD2 protein was more abundant in adults compared to neonates, but no exposure specific differences were observed. Scale bar is 50 μm. Image collected & cropped by CiteAb from the following publication (//particleandfibretoxicology.biomedcentral.com/articles/10.1186/1743-8977-10-34), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SOD2/Mn-SOD Antibody [NB100-1992] - CAV-1 preserves mitochondrial respiratory function through regulation of OXPHOS expression.(A) OXPHOS complex subunits were detected through western blotting with appropriate antibodies. CAV-1 treatment significantly restored hypercholesterolemia-associated increased ETC complex I–V proteins levels. (B) Percentage of the OXPHOS complex (I–V) band intensities is presented in the graph. (C) Representative immunoblot displaying levels of CAV-1, CyPA, mitochondrial biogenesis markers, & antioxidant enzymes in the NC, HC, & HCAV-1 groups. (D) Columns represent average values over three independent experiments. The density for the NC group was set at 1; * & † are significantly different for the NC & HC groups, respectively, at P < 0.05. beta -actin was used as a loading control. Values are means ± SD. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0154210), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SOD2/Mn-SOD Antibody [NB100-1992] - SOD2 mRNA & protein expression. RT-PCR: (A) SOD2 mRNA expression is higher in adults, & highest in the adult parenchyma. (B) No exposure effects on SOD2 mRNA were observed in neonates. (C) Adult SOD2 mRNA was decreased in PFP48. Data are presented as mean+SEM (n=5-7 rats/group, in each compartment), * significantly different compared to neonates in the same compartment, † significantly different compared to airways in the same age, ‡ significantly different compared to FA in the same compartment. Western blotting: (D) Scan of representative SOD2 & actin blots. (E) Neonatal whole lung SOD2 protein expression was unchanged with exposure, & (F) adult whole lung SOD2 protein trended upwards at PFP2, but was statistically insignificant. (G-J) Immunohistochemical localization of SOD2 in lung (n=6 rats/group). SOD2 protein was more abundant in adults compared to neonates, but no exposure specific differences were observed. Scale bar is 50 μm. Image collected & cropped by CiteAb from the following publication (//particleandfibretoxicology.biomedcentral.com/articles/10.1186/1743-8977-10-34), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: SOD2/Mn-SOD Antibody [NB100-1992] - SOD2 mRNA & protein expression. RT-PCR: (A) SOD2 mRNA expression is higher in adults, & highest in the adult parenchyma. (B) No exposure effects on SOD2 mRNA were observed in neonates. (C) Adult SOD2 mRNA was decreased in PFP48. Data are presented as mean+SEM (n=5-7 rats/group, in each compartment), * significantly different compared to neonates in the same compartment, † significantly different compared to airways in the same age, ‡ significantly different compared to FA in the same compartment. Western blotting: (D) Scan of representative SOD2 & actin blots. (E) Neonatal whole lung SOD2 protein expression was unchanged with exposure, & (F) adult whole lung SOD2 protein trended upwards at PFP2, but was statistically insignificant. (G-J) Immunohistochemical localization of SOD2 in lung (n=6 rats/group). SOD2 protein was more abundant in adults compared to neonates, but no exposure specific differences were observed. Scale bar is 50 μm. Image collected & cropped by CiteAb from the following publication (//particleandfibretoxicology.biomedcentral.com/articles/10.1186/1743-8977-10-34), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SOD2/Mn-SOD Antibody [NB100-1992] - SOD2 mRNA & protein expression. RT-PCR: (A) SOD2 mRNA expression is higher in adults, & highest in the adult parenchyma. (B) No exposure effects on SOD2 mRNA were observed in neonates. (C) Adult SOD2 mRNA was decreased in PFP48. Data are presented as mean+SEM (n=5-7 rats/group, in each compartment), * significantly different compared to neonates in the same compartment, † significantly different compared to airways in the same age, ‡ significantly different compared to FA in the same compartment. Western blotting: (D) Scan of representative SOD2 & actin blots. (E) Neonatal whole lung SOD2 protein expression was unchanged with exposure, & (F) adult whole lung SOD2 protein trended upwards at PFP2, but was statistically insignificant. (G-J) Immunohistochemical localization of SOD2 in lung (n=6 rats/group). SOD2 protein was more abundant in adults compared to neonates, but no exposure specific differences were observed. Scale bar is 50 μm. Image collected & cropped by CiteAb from the following publication (//particleandfibretoxicology.biomedcentral.com/articles/10.1186/1743-8977-10-34), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

• Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Ch, Dr, Gp, Gt, Ha, Pm, Rb, Sh, Sq, Xp
• Applications: WB, ELISA, ICC/IF, IHC, IP
• Clonality: Polyclonal
• Host: Rabbit
• Conjugate: Unconjugated
• Format: BSA Free
• Concentration: 1.0 mg/ml

SOD2/Mn-SOD Antibody - BSA Free Summary

• Immunogen: Recombinant Rat Mn SOD Protein
• Localization: Mitochondrial matrix
• Specificity: Detects 25 kDa protein, corresponding to the molecular mass of Mn superoxide dismutase (SOD) on SDS-PAGE immunoblots.
• Isotype: IgG
• Clonality: Polyclonal
• Host: Rabbit
• Gene: SOD2
• Purity: Immunogen affinity purified

Applications/Dilutions

• Dilutions:
  • ELISA 1:100-1:2000
  • Immunocytochemistry/ Immunofluorescence 1:120
  • Immunohistochemistry 1:100
  • Immunohistochemistry-Paraffin 1:10-1:500
  • Immunoprecipitation 1:10-1:500
  • Western Blot 1:5000

Reactivity Notes

Goat reactivity reported in scientific literature (PMID: 28797922). Reacts with Ciona intestinalis (Sea squirt).

Packaging, Storage & Formulations

• Storage: Store at -20C. Avoid freeze-thaw cycles.
• Buffer: PBS (pH 7.4), 50% Glycerol
• Preservative: 0.09% Sodium Azide
• Concentration: 1.0 mg/ml
• Purity: Immunogen affinity purified

Alternate Names for SOD2/Mn-SOD Antibody - BSA Free

• EC 1.15.1.1
• indophenoloxidase B
• IPOB
• IPO-B
• manganese-containing superoxide dismutase
• mangano-superoxide dismutase
• Mn SOD
• Mn superoxide dismutase
• MnSOD
• MVCD6
• SOD, Mitochodrial
• SOD2
• superoxide dismutase [Mn], mitochondrial
• superoxide dismutase 2, mitochondrial

Background

Superoxide dismutase (SOD) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide (1, 2, 3). There are three SOD isoenzymes in mammalian cells. They are: extracellular SOD (EC SOD), copper and zinc-containing SOD (CuZn SOD) and manganese-containing SOD (Mn SOD, SOD-2). The CuZn form contains Cu and Zn ions and exists as a 32 kDa dimer in the cytosol. Mn SOD is an 80 kDa tetramer that contains Mn ion and resides in the mitochondrial matrix. Mn SOD is a tumor necrosis factor (TNF)-inducible enzyme that protects cells from NFmediated apoptosis (4) via superoxide anion detoxification and the subsequent regulation of apoptosis through cytochrome c release and the modulation of the redox state of the mitochondria (6). Mn SOD has also been shown to be a tumor suppressor in human breast cancer (7). Overexpression of this enzyme protects neurons from NMDAand nitric oxide-induced neurotoxicity.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for SOD2/Mn-SOD Antibody (NB100-1992)(44)

Publications using NB100-1992

• Han B, Zhao H, Gong X et al. Upregulation of PGC-1 alpha Attenuates Oxygen-Glucose Deprivation-Induced Hippocampal Neuronal Injury Neural plasticity 2022-06-09 [PMID: 35719138] (ICC/IF, Mouse)
• Peng L, Jiang J, Chen HN Et al. Redox-sensitive cyclophilin A elicits chemoresistance through realigning cellular oxidative status in colorectal cancer Cell reports 2021-11-30 [PMID: 34852234] (WB, Human)
• Suresh V, Mohanty V, Avula K et al. Quantitative proteomics of hamster lung tissues infected with SARS-CoV-2 reveal host factors having implication in the disease pathogenesis and severity FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2021-07-01 [PMID: 34105201] (IF/IHC, Hamster)
• Zhang H, Ma Y, Wang M et al. Dietary supplementation of l-arginine and N-carbamylglutamate enhances duodenal barrier and mitochondrial functions and suppresses duodenal inflammation and mitophagy in suckling lambs suffering from intrauterine-growth-restriction Food Funct. 2020-04-27 [PMID: 32374309]
• Aral C, Demirkesen S, Bircan R, Yasar Sirin D Melatonin reverses the oxidative stress and mitochondrial dysfunction caused by LETM1 silencing Cell Biol. Int. 2019-11-27 [PMID: 31777134] (WB, Mouse)
• Sun H, Qiao W, Cui M et al. The Polycomb Protein Bmi1 Plays a Crucial Role in the Prevention of 1,25(OH)2 D Deficiency-induced Bone Loss J Bone Miner Res. 2019-11-14 [PMID: 31725940] (IHC-P, WB, Mouse)
• Chen L, Yang R et al. 1,25-Dihydroxyvitamin D exerts an antiaging role by activation of Nrf2-antioxidant signaling and inactivation of p16/p53-senescence signaling. Aging Cell 2019-01-06 [PMID: 30907059] (IF/IHC, Mouse)
• Zhang H, Jin Y, Wang M et Al. N-Carbamylglutamate and l-arginine supplementation improve hepatic antioxidant status in intrauterine growth-retarded suckling lambs RSC Adv. 2020-03-18 [PMID: 30869672]
• Xie MY, Yang Y, Liu P et al. 5-aza-2'-deoxycytidine in the regulation of antioxidant enzymes in retinal endothelial cells and rat diabetic retina. Int J Ophthalmol 2019-01-18 [PMID: 30662833] (WB, Rat)
• Du Y, Gu X, Meng H et al. Muscone improves cardiac function in mice after myocardial infarction by alleviating cardiac macrophage-mediated chronic inflammation through inhibition of NF-kB and NLRP3 inflammasome. Am J Transl Res 2018-12-15 [PMID: 30662666] (WB, Mouse)
• Geng Q, Gao H, Yang R et al. Pyrroloquinoline Quinone Prevents Estrogen Deficiency-Induced Osteoporosis by Inhibiting Oxidative Stress and Osteocyte Senescence Int. J. Biol. Sci. 2019-01-01 [PMID: 30662347] (WB, Mouse)
• Guo YX, Zhang GM, Yao XL et al. Effects of nitric oxide on steroidogenesis and apoptosis in goat luteinized granulosa cells Theriogenology 2018-12-03 [PMID: 30530158] (WB, Goat)
• Chowdhury A, Aich A, Jain G et al. Defective Mitochondrial Cardiolipin Remodeling Dampens HIF-1a Expression in Hypoxia. Cell Rep. 2018-10-16 [PMID: 30332638] (Mouse)
• Fauzia E, Barbhuyan Tk, Shrivastava Ak et al. Chick Embryo: A Preclinical Model for Understanding Ischemia-Reperfusion Mechanism. Front Pharmacol. 2018-09-21 [PMID: 30298003] (WB, Chicken)
• Kurobe N, Kato K. Biomed. Rsch. 12:97-103. 1991-01-01
• Cai J, Chen Y, She Y et al. Aerobic exercise improves astrocyte mitochondrial quality and transfer to neurons in a mouse model of Alzheimer's disease. Brain pathology (Zurich, Switzerland) 2024-10-26 [PMID: 39462160]
• Qi XY, Yuan JD, Liu ZY et al. Sirtuin 3-mediated deacetylation of superoxide dismutase 2 ameliorates sodium fluoride-induced mitochondrial dysfunction in porcine oocytes The Science of the total environment 2024-01-15 [PMID: 37944611]
• Gu X, Zhao L, Ye J et al. 1,25(OH)2D3 ameliorates doxorubicin?induced cardiomyopathy by inhibiting the NLRP3 inflammasome and oxidative stress Experimental and Therapeutic Medicine 2023-07-11 [PMID: 37559932] (WB, Mouse)
  
  Details:
  1:1000 dilution
• Braun JL, Messner HN, Cleverdon REG et al. Heterozygous SOD2 deletion selectively impairs SERCA function in the soleus of female mice Physiological Reports 2022-05-17 [PMID: 35581738]
• Chen H, Zhou J, Chen H et al. Bmi-1-RING1B prevents GATA4-dependent senescence-associated pathological cardiac hypertrophy by promoting autophagic degradation of GATA4 Clinical and translational medicine 2022-04-01 [PMID: 35390228] (WB, Mouse)
• Dai Z, Li D, Du X et al. Drosophila Caliban preserves intestinal homeostasis and lifespan through regulating mitochondrial dynamics and redox state in enterocytes PLOS Genetics 2020-10-15 [PMID: 33057338]
• Yu C, Chen S, Wang X et al. Exposure to maternal diabetes induces endothelial dysfunction and hypertension in adult male rat offspring Microvasc. Res. 2020-09-18 [PMID: 32956647] (WB, Rat)
• Zhang Q, Li J, Li Y et al. Bmi deficiency causes oxidative stress and intervertebral disc degeneration which can be alleviated by antioxidant treatment J. Cell. Mol. Med. 2020-06-24 [PMID: 32583517] (WB, Mouse)
• Hesse R, Hurtado ML, Jackson RJ, Eaton SL et Al. Comparative profiling of the synaptic proteome from Alzheimer's disease patients with focus on the APOE genotype Acta Neuropathol Commun 2019-12-22 [PMID: 31862015]
• Guo Y, Nie H, Zhang G, Sun L. Effects of nutrient restriction and arginine treatment on oxidative stress in the ovarian tissue of ewes during the luteal phase. Theriogenology. 2018-02-01 [PMID: 29501008] (Sheep)
• Chen YH, Lin WW, Liu CS, Su SL. H2O2 induces caveolin-1 degradation and impaired mitochondrial function in E11 podocytes Mol Med Rep 2017-09-18 [PMID: 28944844] (WB, Human)
• Yao X, Zhang G, Guo Y et al. Vitamin D receptor expression and potential role of vitamin D on cell proliferation and steroidogenesis in goat ovarian granulosa cells Theriogenology 2017-08-03 [PMID: 28797922] (WB, Goat)
• Chen YH, Lin WW, Liu CS et al. Caveolin-1 Expression Ameliorates Nephrotic Damage in a Rabbit Model of Cholesterol-Induced Hypercholesterolemia. PLoS ONE. 2016-04-29 [PMID: 27124120] (IHC-P, WB, Rabbit)
• Zhang Y, Chen Y, Gucek M, Xu H. The mitochondrial outer membrane protein MDI promotes local protein synthesis and mtDNA replication. EMBO J. 2016-04-06 [PMID: 27053724] (WB, Drosophila)
• Chung C, Puthanveetil P, Ory DS, Lieberman AP Genetic and pharmacological evidence implicates cathepsins in Niemann-Pick C cerebellar degeneration Hum Mol Genet. 2016-03-31 [PMID: 26908626] (IHC-P, Mouse)
• Freitas I, Boncompagni E, Tarantola E et al. In Situ Evaluation of Oxidative Stress in Rat Fatty Liver Induced by a Methionine- and Choline-Deficient Diet. Oxid Med Cell Longev 2016-01-06 [PMID: 26881047] (WB)
• Messner H An in vivo, ex vivo, and in vitro exploration of the use of chronic hypoxia/physioxia and ROS/RNS-mediated alteration of physiological function in mitochondrial disease Thesis 2020-01-01 (WB, Human)
• Chen YH, Lin WW, Liu CS et al. Caveolin-1 provides palliation for adverse hepatic reactions in hypercholesterolemic rabbits. PLoS ONE 2014-01-29 [PMID: 24475013] (WB, IHC-P, Rabbit)
• Chan JK, Charrier JG, Kodani SD et al. Combustion-derived flame generated ultrafine soot generates reactive oxygen species and activates Nrf2 antioxidants differently in neonatal and adult rat lungs. Part Fibre Toxicol 2013-08-01 [PMID: 23902943] (WB, Rat)
• Hagopian K, Tomilov AA, Tomilova N et al. Shc proteins influence the activities of enzymes involved in fatty acid oxidation and ketogenesis Metabolism 2012-06-07 [PMID: 22683097] (WB, Mouse)
• Honda F, Kano H, Kanegane H, Nonoyama S, Kim ES, Lee SK, Takagi M, Mizutani S, Morio T. The kinase Btk negatively regulates the production of reactive oxygen species and stimulation-induced apoptosis in human neutrophils. Nat Immunol doi: 10 1038/ni 2234. 2012-02-26 [PMID: 22366891]
• Dumont M, Wille E, Stack C et al. Reduction of oxidative stress, amyloid deposition, memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer's disease. FASEB J :fj.09-132928. 2009-01-01 [PMID: 19346295]
• Furukawa Y, O’Halloran T. Antioxidants & Redo Signaling. 8( 5): 6. 2006-01-01 [PMID: 16771675]
• Gao B et al. Am J Physiol Lung. Cell Mol Physiol 284: L917-L925. 2003-01-01 [PMID: 12736188]
• Xiao-Hong Liu et al. Brain Res. 625: 29-37. 1993-01-01 [PMID: 7694776]
• Bannister JV, Bannister WH, Rotilio G. Aspects of the structure, function, and applications of superoxide dismutase. CRC Crit Rev Biochem;22(2):111-80. 1987-01-01 [PMID: 3315461]
• Hassan HM. Free Radical Biol. Med. 5: 377-385. 1988-01-01 [PMID: 2855738]
• Wispe JR, Clark JC, Burhans MS et al. Synthesis and processing of the precursor for human mangano-superoxide dismutase. BBA. 994: 30-36. 1989-01-01 [PMID: 2462451]
• Adachi T, Ohta H, Yamada H et al. Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody. Clin. Chim. Acta. 212: 89-102. 1992-01-01 [PMID: 1477980]

FAQs for SOD2/Mn-SOD Antibody (NB100-1992). (Showing 1 - 2 of 2 FAQs).

1. I want to measure SOD and Catalase on different erythroid subpopulation by using flow cytometry.I want to know whether these SOD and Catalase molecules are directly conjugated with fluorescence molecules or I have to do indirect staining.I have to use Ter 119 and CD71 molecule along with catalase or SO antibody.Can you please provide me detail protocol for using these antibodis or send me some references, if anyone used these antibodies by utilizing multicolour flow cytometry.
   • For our testing of NB100-1992, we used conjugated secondary antibodies. We have not yet tried to directly conjugate this primary, although this is certainly possible and would be expected to give the same results. We do not routinely test our antibodies in FACS, and in most cases, this application is validated by a trusted collaborator. For NB100-1992, viability for FACS was reported by a customer, and we do not have a detailed protocol for this application and product.
2. What is your recommended working dilution for IHC?
   • In regards to the IHC dilution, we would recommend starting at about 1:10-1:2000. Obviously this will depend on your samples and how highly expressed the protein is in them. You may need to optimize, but this is a good starting point.

Bioinformatics

• Gene Symbol: SOD2
• Entrez:
  • 6648(Human)
  • 20656(Mouse)
  • 24787(Rat)
• Uniprot:
  • P07895(Rat)