C-Peptide EIA - Cosmo Bio Co.,Ltd.

Antibodies

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C-Peptide EIA

Catalog No.: YII-YK010-EX
Size: 1KIT
Price: ¥76000
$1014
antigen/source: C-Peptide
catalog info: Catalog 2012-p110
Storage: 4C
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Immunogen: Rat
Reacts with: Rat
Measurement Range: 1.56 - 50 ng/mL
Purpose: This ELISA kit is used for quantitative determination of rat C-Peptide in its plasma, serum, urine and culture supernatant samples. The kit is characterized for sensitive quantification, high specificity and no influences with other components in samples. Rat C-Peptide standard is highly purified synthetic product (purity: higher than 98%).
component: Antibody: X
Plate: X
Coating: X
Control: -
Standard: X
Labeling: X
Substrate: X
Others: X
1. Antibody coated plate 1 plate (96 wells)
2. C-Peptide standard 1 vial
3. Labeled antigen 1 vial
4. C-Peptide antibody 1 bottle (12 mL)
5. SA-HRP solution 1 bottle (12 mL)
6. Substrate buffer 1 bottle (24 mL)
7. OPD tablet 2 tablets
8. Stopping solution 1 bottle (12 mL)
9. Buffer solution 1 bottle (30 mL)
10. Washing solution 1 bottle (50 mL)
11. Adhesive foil 3 sheets

Other:

 Supplementary 
Competitive
 Applicable sample 
Culture Supernatant, Plasma, Serum, Urine
[Other]
This enzyme immunoassay (EIA) kit is a stable and convenient assay system for rat C-peptide in its plasma, serum, urine and culture supernatant.
The processing of proinsulin, which occurs within the B cell, yields insulin and C-peptide and insulin and C-peptide are secreted in equimolar quantities into blood circulation. Therefore, the measurement of C-peptide in blood reflects the concentration of insulin and also provides valuable information to evaluate the pancreatic B cell function.
The EIA kit is using synthetic rat C-Peptide I as standard and biotinylated rat C-Peptide I as labeled antigen. The kit contains specific polyclonal antibody (C-peptide antibody) recognized to the amino acid sequence in the C-terminal side region which are common between rat C-Peptide I and II.


Reference:

•  Granado M, Garcia-Caceres C, Frago LM, Argente J, Chowen JA. Endocrinology. 2010 May;151(5):2008-18.
>Maezawa Y, Yokote K, Sonezaki K, Fujimoto M, Kobayashi K, Kawamura H, Tokuyama T, Takemoto M, Ueda S, Kuwaki T, Mori S, Wahren J, Saito Y. Diabetes Metab Res Rev. 2006 Jul-Aug;22(4):313-22.
•  Markussen, J. and Sundby, F. (1972): Eur. J. Biochem., 25: 153.
•  Massey, D. E. and Smyth, D. G. (1975): J. Biol. Chem. 250: 6288.
5. Miyachi, Y. Vaitukais, J. L. Nieschlag, E. and Lipsett, M. B. (1972): J. Clin. Endocr.,34: 23.
•  Smyth, D. G., Markussen, J. and Sundby, F. (1974): Nature (Lond), 248:151.
•  Tager, H. S., Emdin, S.O., Clark, J. L. and Steiner, D. F. (1973): J. 248: 3476
•  Tager, H. S. and Steiner, D. F. (1972): J. Biol. Chem., 247, 7936
•  Yanaihara, N., Sakagami,M., Sakura, N., Iizuka, Y., Nishida, T., Hashimoto, T. and Yanaihara, C. (1977) In: Deabetes. p116 Ed J.S.Bajaj. Excerpta Media, Amsterdam.
10. Yanaihara, N., Nishida, T., Sakagami, M., and Yanaihara, C. (1977): In: Peptide Chemistry 1976, p85 Ed T.Nakajima. Protein Research Foundation, Osaka.
11. Yanaihara, N., Yanaihara, C., Sakagami, Sakura, N., Hashimoto, T. and Nishida, T. (1978): Diabetes, 27, (Suppl 1 ) 149
•  Yanaihara, C., Ozaki, J., Nishida, T , Iizuka, Y., Sato H., Yanaihara, N.,and Kaneko, T. (1979): p87.Eds. S. Baba, T. Kaneko, N. Yanaihara, Excerpta Medica, Amsterdam-Oxford.
13. Luo, W. Q., Kanno, T., Winarto, A, Iwanaga, T., Li., J., Futai, Y. Yanaihara, C., and Yanaihara, N. (1998) : Biomed, Res., 19, 127
 
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