Product Includes | Product # | Quantity | Mol. Wt | Isotype/Source |
---|---|---|---|---|
Aldolase A (D73H4) Rabbit mAb | 8060 | 20 µl | 40 kDa | Rabbit IgG |
Enolase-1 Antibody | 3810 | 20 µl | 47 kDa | Rabbit  |
Enolase-2 Antibody | 9536 | 20 µl | 47 kDa | Rabbit  |
PDHK1 (C47H1) Rabbit mAb | 3820 | 20 µl | 47 kDa | Rabbit IgG |
PFKFB2 (D7G5R) Rabbit mAb | 13045 | 20 µl | 55 kDa | Rabbit IgG |
PFKFB3 (D7H4Q) Rabbit mAb | 13123 | 20 µl | 60 kDa | Rabbit IgG |
PGAM1 (D3J9T) Rabbit mAb | 12098 | 20 µl | 28 kDa | Rabbit IgG |
Anti-rabbit IgG, HRP-linked Antibody | 7074 | 100 µl | Goat  |
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Description
The Glycolysis II Antibody Sampler Kit provides an economical means to investigate select enzymes involved in glycolysis. The kit contains enough primary antibody to perform two western blot experiments per primary antibody.
Storage
Background
Glycolysis is the metabolic process by which glucose is converted to pyruvate in a sequence of enzymatic steps. Phosphofructokinase (PFK) catalyzes the phosphorylation of fructose-6-phosphate in glycolysis (1). The bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase or PFKFB) catalyzes the synthesis and degradation of fructose 2,6-bisphosphate and regulates its steady-state level. Four different PFKFB isoforms (PFKFB1, PFKFB2, PFKFB3, and PFKFB4) have been identified (2). Aldolase (fructose bisphosphate aldolase) is a glycolytic enzyme that catalyzes the conversion of fructose 1, 6-bisphosphate to 3-phosphoglyceraldehyde (3). Phosphoglycerate mutase (PGAM1) catalyzes the conversion of 3-phosphoglycerate to 2-phosphoglycerate during glycolysis (4). Enolase is an important glycolytic enzyme involved in the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Mammalian enolase exists as three subunits: enolase-1 (α-enolase), enolase-2 (γ-enolase) and enolase-3 (β-enolase) that can form both homo- and heterodimers (5). Pyruvate dehydrogenase kinase (PDHK) phosphorylates PDH and inactivates it, whereas dephosphorylation of PDH is carried out by pyruvate dehydrogenase phosphatase to generate the active form (6).
- Mediavilla, D. et al. (2008) J Biochem 144, 235-44.
- Atsumi, T. et al. (2005) Diabetes 54, 3349-57.
- Castaldo, G. et al. (2000) Clin Chem 46, 901-6.
- Vander Heiden, M.G. et al. (2010) Science 329, 1492-9.
- Pancholi, V. (2001) Cell Mol Life Sci 58, 902-20.
- Wigfield, S.M. et al. (2008) Br J Cancer 98, 1975-84.
Background References
Trademarks and Patents
Limited Uses
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