Description
Human proBNP Glycosylated Recombinant
| Catalog number: | B2016410 |
| Lot number: | Batch Dependent |
| Expiration Date: | Batch dependent |
| Amount: | 50 ug |
| Molecular Weight or Concentration: | between 20 and 25 kDa |
| Supplied as: | Powder |
| Applications: | a molecular tool for various biochemical applications |
| Storage: | -20 C |
| Keywords: | Recombinant human proBNP, glycosylated |
| Grade: | Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity>18 M-cm) and are filtered through 0.22 um. |
References
- Semenov AG, Tamm NN, Apple FS, Schulz KM, Love SA, Ler R, Feygina EE, Katrukha AG. Searching for a BNP standard: Glycosylated proBNP as a common calibrator enables improved comparability of commercial BNP immunoassays Clin Biochem. 2017 Mar;50(4-5):181-185.
- Crimmins DL, Kao JL. A glycosylated form of the human cardiac hormone pro B-type natriuretic peptide is an intrinsically unstructured monomeric protein Arch Biochem Biophys. 2008 Jul 1;475(1):36-41.
- Semenov AG, Tamm NN, Seferian KR, Postnikov AB, Karpova NS, Serebryanaya DV, Koshkina EV, Krasnoselsky MI, Katrukha AG. Processing of pro-B-type natriuretic peptide: furin and corin as candidate convertases Clin Chem. 2010 Jul;56(7):1166-76.
- Saenger AK, Rodriguez-Fraga O, Ler R, Ordonez-Llanos J, Jaffe AS, Goetze JP, Apple FS. Specificity of B-Type Natriuretic Peptide Assays: Cross-Reactivity with Different BNP, NT-proBNP, and proBNP Peptides Clin Chem. 2017 Jan;63(1):351-358.
- Ala-Kopsala M, Moilanen AM, Rys J, Ruskoaho H, Vuolteenaho O. Characterization of molecular forms of N-terminal B-type natriuretic peptide in vitro Clin Chem. 2010 Dec;56(12):1822-9.
- Hammerer-Lercher A, Halfinger B, Sarg B, Mair J, Puschendorf B, Griesmacher A, Guzman NA, Lindner HH. Analysis of circulating forms of proBNP and NT-proBNP in patients with severe heart failure Clin Chem. 2008 May;54(5):858-65.
- Semenov AG, Postnikov AB, Tamm NN, Seferian KR, Karpova NS, Bloshchitsyna MN, Koshkina EV, Krasnoselsky MI, Serebryanaya DV, Katrukha AG. Processing of pro-brain natriuretic peptide is suppressed by O-glycosylation in the region close to the cleavage site Clin Chem. 2009 Mar;55(3):489-98.
- Lee Y, Kim H, Chung J. An antibody reactive to the Gly63-Lys68 epitope of NT-proBNP exhibits O-glycosylation-independent binding Exp Mol Med. 2014 Sep 19;46(9):e114.
- Peng J, Jiang J, Wang W, Qi X, Sun XL, Wu Q. Glycosylation and processing of pro-B-type natriuretic peptide in cardiomyocytes Biochem Biophys Res Commun. 2011 Aug 5;411(3):593-8.
