Rabbit SOD (Mn) Polyclonal Antibody | anti-Sod2 antibody

SOD (Mn) Antibody: RPE

Cat. Num. AAA806474

• Reactivity: Human, Rat, Mouse, Bovine, Canine, Chicken, Dosophila, Guinea pig, Pig, Hamster, Monkey, Rabbit, Sheep, Xenopus
• Applications: Western Blot, Immunoprecipitation, ELISA, Immunohistochemistry, Immunofluorescence
• Synonyms: SOD (Mn); Polyclonal Antibody; SOD (Mn) Antibody: RPE; Manganese SOD; IPO B; Mn SOD; SOD2; anti-Sod2 antibody

• Host: Rabbit
• Reactivity: Human, Rat, Mouse, Bovine, Canine, Chicken, Dosophila, Guinea pig, Pig, Hamster, Monkey, Rabbit, Sheep, Xenopus
• Clonality: Polyclonal
• Form/Format: Affinity (antigen) Purified
• Concentration: 1mg/mL (varies by lot)
• Sequence Length: 222

• Applicable Applications for anti-Sod2 antibody: Western Blot (WB), Immunoprecipitation (IP), ELISA (EIA), Immunohistochemistry (IHC), Immunofluorescence (IF)
• Application Notes: 0.5ug/ml was sufficient for detection of Mn SOD in 20ug of rat brain tissue extract
• Conjugate: RPE
• Storage Buffer: PBS pH7, 50% glycerol, 0.09% sodium azide
• Preparation and Storage: -20 degree C

Western Blot (WB)

(Western blot analysis of Rat Tissue lysates showing detection of SOD2 protein using Rabbit Anti-SOD2 Polyclonal Antibody (SPC-117). Load: 15 ugprotein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Rabbit Anti-SOD2 Polyclonal Antibody (SPC-117) at 1:1000 for 2 hours at RT. Secondary Antibody: Donkey Anti-Rabbit IgG: HRP for 1 hour at RT.)

Immunohistochemistry (IHC)

(Immunohistochemistry analysis using Rabbit Anti-SOD2 Polyclonal Antibody (SPC-117). Tissue: backskin. Species: Mouse. Fixation: Bouin's Fixative Solution. Primary Antibody: Rabbit Anti-SOD2 Polyclonal Antibody (SPC-117) 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.)

Related Product Information for anti-Sod2 antibody

Background Info: Detects a ~25kDa protein corresponding to the molecular mass of Mn superoxide dismutase (SOD) on SDS PAGE immunoblots.

Scientific Background: Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2" to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2,5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extra-cellular space (7). SOD3 can also be distinguished by its heparin-binding capacity (1).

Product Categories/Family for anti-Sod2 antibody

Oxidative Stress

References

1.Adachi T., et al. (1992). Clin. Chim. Acta. 212: 89-102. 2.Barrister J.V., et al. (1987). Crit. Rev. Biochem. 22:111- 180. 3.Furukawa Y., O'Halloran T. (2006). Antioxidants & Redo Signaling. Vol 8, No 5,6. 4.Gao B., et al. (2003). Am J Physiol Lung Cell Mol Physiol 284: L917-L925. 5.Hassan H.M. (1988). Free Radical Biol. Med. 5: 377-385. 6.Kurobe N., et al. (1990) Biomedical Research. 11: 187- 194 7.Wispe J.R., et al. (1989) BBA. 994: 30-36. 8.Xiao-Hong Liu., et al. (1993) Brain Research. 625: 29-37.
1. Allan, M. E. and Storey, K. B. (2012). Expression of NF-κB and downstream antioxidant genes in skeletal muscle of hibernating ground squirrels, Spermophilus tridecemlineatus. Cell Biochemistry and Function. 30 (2), 166-174. doi:10.1002/cbf.1832

2. Ishii, H., Kunihiro, S., Tanaka, M., Hatano, K. and Nishikata, T. (2012). Cytosolic subunits of ATP synthase are localized to the cortical endoplasmic reticulum-rich domain of the ascidian egg myoplasm. Development, growth & differentiation. 54 (8), 753-766. doi: 10.1111/dgd.12003
3. Wu, H., Hsiao, T., Chien, C., and Lai, M. (2009). Ischemic conditioning by short periods of reperfusion attenuates renal ischemia/reperfusion induced apoptosis and autophagy in the rat. J Biomed Sci. 16 (19). doi:10.1186/1423-0127-16-19

NCBI and Uniprot Product Information

• NCBI GI #: 8394331
• NCBI GeneID: 24787
• NCBI Accession #: NP_058747.1
• NCBI GenBank Nucleotide #: NM_017051.2
• UniProt Accession #: P07895
• Molecular Weight: 24,674 Da
• NCBI Official Full Name: superoxide dismutase
• NCBI Official Synonym Full Names: superoxide dismutase 2, mitochondrial
• NCBI Official Symbol: Sod2
• NCBI Protein Information: superoxide dismutase [Mn], mitochondrial; superoxide dismutase [Mn], mitochondrial; Superoxide dimutase 2, mitochondrial; mitochondrial superoxide dismutase 2
• UniProt Protein Name: Superoxide dismutase [Mn], mitochondrial
• Protein Family: Superoxide dismutase
• UniProt Gene Name: Sod2
• UniProt Entry Name: SODM_RAT

NCBI Description

manganese superoxide dismutase; intramitochondrial free radical scavenging enzyme [RGD, Feb 2006]

Uniprot Description

SOD2: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Genetic variation in SOD2 is associated with susceptibility to microvascular complications of diabetes type 6 (MVCD6). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new- onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Belongs to the iron/manganese superoxide dismutase family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Oxidoreductase; Mitochondrial; EC 1.15.1.1

Cellular Component: mitochondrion; cytoplasm; mitochondrial inner membrane; intracellular; myelin sheath

Molecular Function: identical protein binding; protein binding; DNA binding; manganese ion binding; superoxide dismutase activity; oxygen binding

Biological Process: positive regulation of nitric oxide biosynthetic process; heart development; response to lipopolysaccharide; protein homotetramerization; post-embryonic development; response to selenium ion; glutathione metabolic process; regulation of mitochondrial membrane potential; negative regulation of neuron apoptosis; response to electrical stimulus; response to drug; erythrophore differentiation; mitochondrion organization and biogenesis; release of cytochrome c from mitochondria; negative regulation of fat cell differentiation; regulation of transcription from RNA polymerase II promoter; response to manganese ion; iron ion homeostasis; response to reactive oxygen species; DNA damage response, signal transduction resulting in induction of apoptosis; response to zinc ion; age-dependent response to reactive oxygen species; negative regulation of fibroblast proliferation; hydrogen peroxide metabolic process; neuron development; response to oxidative stress; response to activity; superoxide release; negative regulation of apoptosis; oxygen homeostasis; removal of superoxide radicals; locomotory behavior; vasodilation; response to L-ascorbic acid; age-dependent response to oxidative stress; negative regulation of cell proliferation; apoptotic mitochondrial changes; response to radiation; sensory perception of sound; acetylcholine vasodilation involved in regulation of systemic arterial blood pressure; regulation of catalytic activity; regulation of blood pressure; response to gamma radiation; hemopoiesis; response to axon injury; protein homooligomerization; aging; response to nutrient levels; response to superoxide; superoxide metabolic process; liver development; response to silicon dioxide; response to hyperoxia; response to cadmium ion; response to hydrogen peroxide; detection of oxygen; response to hypoxia; response to cold; induction of apoptosis by oxidative stress; hydrogen peroxide biosynthetic process