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Merck

S2147

Sigma-Aldrich

Monoclonal Anti-Superoxide Dismutase (SOD) antibody produced in mouse

clone SD-G6, ascites fluid

别名:

Anti-ALS, Anti-ALS1, Anti-HEL-S-44, Anti-IPOA, Anti-SOD, Anti-STAHP, Anti-hSod1, Anti-homodimer

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About This Item

MDL號碼:
分類程式碼代碼:
12352203
NACRES:
NA.41

生物源

mouse

共軛

unconjugated

抗體表格

ascites fluid

抗體產品種類

primary antibodies

無性繁殖

SD-G6, monoclonal

包含

15 mM sodium azide

物種活性

canine, human, rat

技術

indirect ELISA: 1:300

同型

IgG1

UniProt登錄號

運輸包裝

dry ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... SOD1(6647)
rat ... Sod1(24786)

一般說明

Monoclonal Anti-Superoxide Dismutase (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Superoxide Dismutase (SOD) is a family of metalloenzymes widely distributed in both plants and animals. In mammalian tissues, three types of superoxide dismutase [Cu-Zn-SOD, Mn-SOD, extracellular (EC)-SOD] occur. Human manganese superoxide dismutase (MnSOD), isolated from liver is composed of 22 kDa subunits each containing one Mn atom, while SOD from bovine erythrocyte has a molecular weight of 32.5 kDa. Superoxide Dismutase occurs in high concentrations in brain, liver, heart, erythrocytes and kidney.
Superoxide Dismutase (SOD) or CuZn-SOD (SOD1), a cytoplasmic and mitochondrial intermembrane space protein is located on human chromosome 21q22. It belongs to superoxide dismutase multigene family.

特異性

The antibody recognizes natural and recombinant human-Cu-Zn-SOD, human placental SOD, and human erythrocyte SOD using direct capture or competitive ELISA. Cross-reactivity has been observed with human liver and salivary gland, rat salivary gland, pheochromocytoma cell line (PC12), and dog salivary gland. No reactivity was observed with SOD from bovine erythrocytes, kidney, and liver; dog erythrocytes; Bacillus stearothermophilus; E. coli, or horseradish.

免疫原

recombinant human copper-zinc superoxide dismutase (Cu-Zn-SOD).

應用

Anti-Superoxide Dismutase (SOD) antibody has been used in immunohistochemistry and Cu-Zn SOD detection via ELISA.

生化/生理作用

Superoxide Dismutase (SOD) appear to protect cells against reactive free radicals by scavenging the superoxide radicals produced by ionization radiation or through other mechanisms. SOD have been proposed as clinically useful for a wide variety of applications including prevention of oncogenesis, tumor promotion, tumor invasiveness, radiation damage, reduction of the cytotoxic and cardiotoxic effects of anticancer drugs, as a measure against the aging process and as anti-inflammatory agents.
Superoxide Dismutase (SOD) or CuZn-SOD (SOD1) mutations results in amyotrophic lateral sclerosis It acts as a mediator of the HMF (hypomagnetic field) effect.

免責聲明

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Marcel Maier et al.
Science translational medicine, 10(470) (2018-12-07)
Mutations in the gene encoding superoxide dismutase 1 (SOD1) lead to misfolding and aggregation of SOD1 and cause familial amyotrophic lateral sclerosis (FALS). However, the implications of wild-type SOD1 misfolding in sporadic forms of ALS (SALS) remain unclear. By screening
Superoxide Dismutases: Role in Redox Signaling, Vascular Function, and Diseases
Fukai T, et al.
Antioxidants & Redox Signaling, 15(6), 1583-1583 (2011)
Targeted expression of human CuZn superoxide dismutase gene in mouse central nervous system
Li Y, et al.
Journal of Neuroscience Methods, 89(1), 49-55 (1999)
Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
Johnston JA, et al.
Proceedings of the National Academy of Sciences of the USA, 97(23), 12571-12576 (2000)
The Functional Role of MnSOD as a Biomarker of Human Diseases and Therapeutic Potential of a New Isoform of a Human Recombinant MnSOD
Borrelli A, et al.
BioMed Research International, 2014 (2014)

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