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Recombinant Human GPBB Protein

Placeholder Recombinant Human Myeloperoxidase Protein
Placeholder Recombinant Human MyBPC3 Protein
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DataSheet   

The recombinant human GPBB protein is derived from in vitro expression of human GPBB gene in E. coli and purified using his-tag affinity column and can be used in multiple applications such as cell culture, ELISA and western blot.

Alternative names for GPBB: Glycogen phosphorylase isoenzyme BB

This product is for Laboratory Research Use Only not for diagnostic and therapeutic purposes or any other purposes.

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Description

Genorise Recombinant Human GPBB Protein Summary

Alternative names for GPBB: Glycogen phosphorylase isoenzyme BB

Product Specifications

Purity > 97%, by SDSPAGE under reducing conditions and visualized by silver stain.
Endotoxin Level < 0.1 EU per 1 μg of the protein by the LAL method.
Activity na
Source E. coli derived human GPBB.
Accession # NP_002853.2
N-Terminal Sequence Analysis Lys
Amino Acid Sequence Lys545-Asp843
Predicted Molecular Mass 33 kDa
SDS-PAGE 33 kDa, reducing conditions

 

Background: 

Glycogen phosphorylase isoenzyme BB (abbreviation: GPBB) is an isoenzyme of glycogen phosphorylase.[1] This isoform of the enzyme exists in cardiac (heart) and brain tissue. The enzyme is one of the “new cardiac markers” which are discussed to improve early diagnosis in acute coronary syndrome.[2-4] A rapid rise in blood levels can be seen in myocardial infarction and unstable angina. GPBB based on its metabolic function is an enzyme for early laboratory detection of ischaemia and infarction.[5] In the aerobic heart muscle GPBB together with glycogen is tightly associated with the vesicles of the sarcoplasmic reticulum. Release of GPBB, the main isoform in the human myocardium, essentially depends on the degradation of glycogen, which is catalyzed by GP. Ischaemia is known to favour the conversion of bound GP in the b form into GP a, thereby accelerating glycogen breakdown, which is the ultimate prerequisite for getting GP into a soluble form being able to move freely in the cytosol. The efflux of GPBB into the extracellular fluid follows if ischaemia-induced structural alterations in the cell membrane become manifest. The clinical application of GPBB as a marker of ischaemic myocardial injury is a very promising tool for extending our knowledge of the severity of myocardial ischaemic events in the various coronary syndromes. GPBB along with cardiac Troponin I elevated after chemotherapy for acute leukemia and thus may serve a potential for detection of acute cardiotoxicity.[6] GPBB concentration measurement may be a useful tool for monitoring myocardial ischemia during a transjugular intrahepatic portosystemic shunts procedure.[7]

References

1.     Newgard CB, et al. (1988) J. Biol. Chem. 263 (8), 3850-3857 (1988)

  1. Apple FS, et al. (2005) Clin. Chem. 51 (5): 810–24.
  2. Peetz D, et al. (2005). Clin. Chem. Lab. Med. 43 (12): 1351–8.
  3. Lillpopp L, et al.(2012) Am. J. Cardiol. 110 (9), 1225-1230.
  4. Krause EG1, (1996) Mol Cell Biochem. 160-161:289-95.
  5. Horacek JM1, et al. (2010) Exp Oncol. 32(2):97-9.
  6. Vasatova M1, et al. (2015) Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub. 159(3):437-41.

 

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