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GSH (Shorten Name),
Product Name:

General GSH/ Glutathione ELISA Kit

 
Cat.#:

E9182Ge

Brand:
EIAab®
Regulatory Status:
Detection Method:
ELISA
Assay Type:
Competitive
Detection Range:
1.25-80ng/mL
Sensitivity:
0.625ng/mL
Specificity:
Natural and recombinant general Glutathione
Sample Type:
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Sample Data:
Assay Procedure:
Research Area:
-
Product Overview:
E9182Ge is a ready-to-use microwell, strip plate ELISA (enzyme-linked immunosorbent assay) Kit for analyzing the presence of the A Disintegrin and Metalloprotease 30 (Glutathione) ELISA Kit target analytes in biological samples. The concentration gradients of the kit standards or positive controls render a theoretical kit detection range in biological research samples containing Glutathione. The ELISA analytical biochemical technique of the E9182Ge kit is based on Glutathione antibody-Glutathione antigen interactions (immunosorbency) and an HRP colorimetric detection system to detect Glutathione antigen targets in samples. The ELISA Kit is designed to detect native, recombinant, Glutathione. Appropriate sample types may include undiluted human body fluids and/or tissue homogenates, secretions. Quality control assays assessing reproducibility identified the intra-assay CV (%) and inter-assay CV(%).
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General GSH ELISA Kit
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Product Datasheets
Datasheet:
Instruction:
MSDS:


Linearity
The linearity of the kit was assayed by testing samples spiked with appropriate concentration of Glutathione and their serial dilutions. The results were demonstrated by the percentage of calculated concentration to the expected.

Sample

1:2

1:4

1:8

1:16

serum(n=5)

93-105%

107-117%

107-116%

80-89%

EDTA plasma(n=5)

114-123%

103-113%

101-111%

86-98%

heparin plasma(n=5)

97-110%

 

113-122%

88-97%

103-116%

 

General Annotation


Sub Unit:
N/A


Function:
Glutathione (GSH) is a tripeptide with a gamma peptide linkage between the amine group of cysteine (which is attached by normal peptide linkage to a glycine) and the carboxyl group of the glutamate side-chain. It is an antioxidant, preventing damage to important cellular components caused by reactive oxygen species such as free radicals and peroxides. Thiol groups are reducing agents, existing at a concentration of approximately 5 mM in animal cells. Glutathione reduces disulfide bonds formed within cytoplasmic proteins to cysteines by serving as an electron donor. In the process, glutathione is converted to its oxidized form, glutathione disulfide (GSSG), also called L-(–)-glutathione. Once oxidized, glutathione can be reduced back by glutathione reductase, using NADPH as an electron donor. The ratio of reduced glutathione to oxidized glutathione within cells is often used as a measure of cellular toxicity.


Location:
N/A


Sample Data
Sample Data
Sample Data
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