Recombinant Human Lactate Dehydrogenase B/LDHB Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Human Lactate Dehydrogenase B/LDHB Protein, CF Summary

Details of Functionality
Measured by its ability to reduce pyruvate to lactate. The specific activity is >60,000 pmol/min/μg, as measured under the described conditions.
Source
E. coli-derived human Lactate Dehydrogenase B/LDHB protein
Ala2-Leu334, with N-terminal Met and 6-His tag
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Enzymes
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
37 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
36 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Tris, NaCl, TCEP and Glycerol.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Assay Procedure
  • Assay Buffer:  25 mM Tris, 100 mM NaCl, pH 7.5
  • Recombinant Human LDHB (rhLDHB) (Catalog # 9205-HB)
  • beta -Nicotinamide adenine dinucleotide, reduced disodium salt hydrate ( beta -NADH) (Sigma, Catalog # N8129), 20 mM stock in 0.1 M Sodium Borate, pH 9.0
  • 100 mM Sodium Pyruvate (Gibco, Catalog # 11360)
  • 96-well Clear Plate  (Catalog # DY990)
  • Plate Reader (Model: SpectraMax Plus by Molecular Devices) or equivalent
  1. Dilute rhLDHB to 0.4 ng/µL in Assay Buffer.
  2. Prepare a substrate mixture containing 1.6 mM beta -NADH and 4 mM sodium pyruvate in Assay Buffer.
  3. In a plate load 50 µL of 0.4 ng/µL rhLDHB, and start the reaction by adding 50 µL of substrate mixture. Include a Substrate Blank containing 50 µL Assay Buffer and 50 µL of substrate mixture. 
  4. Read plate at 340 nm (absorbance) in kinetic mode for 5 minutes.
  5. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (OD/min) x well volume (L) x 1012 pmol/mol x (-1)
ext. coeff** (M-1cm-1) x path corr.*** (cm) x amount of enzyme (µg)


     *Adjusted for Substrate Blank
     **Using the extinction coefficient 6220 M-1cm-1
     ***Using the path correction 0.320 cm
     Note: the output of many spectrophotometers is in mOD.

Per Well:
  • rhLDHB: 0.020 µg
  • beta -NADH: 0.8 mM
  • Sodium pyruvate: 2 mM

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Lactate Dehydrogenase B/LDHB Protein, CF

  • EC 1.1.1
  • EC 1.1.1.27
  • Epididymis Secretory Protein Li 281
  • HEL-S-281
  • Lactate Dehydrogenase B
  • LDH heart subunit
  • LDHB
  • LDH-B
  • LDHBD
  • LDH-H
  • L-lactate dehydrogenase B chain
  • Renal Carcinoma Antigen NY-REN-46
  • TRG-5

Background

A hallmark of most cancer cells is an altered metabolism involving a shift to aerobic glycolysis with lactate production coupled with a higher uptake of glucose as the main source of energy. Lactate dehydrogenase (LDH) is key to this shift by catalyzing the formation of lactate by reducing pyruvate with NADH, which also generates NAD(+) that is essential for the continuity of glycolysis (1). Inhibiting LDH activity has an anti-proliferative effect on cancer cells (2). It may reverse the resistance of tumor cells to conventional chemo- and radiotherapy. Recent research has renewed interest in LDH as an anticancer drug target (3). LDH enzymes have three homologous subunits LDHA, LDHB and LDHC. The combination of these three results to multiple isozymes, including LDH-M and LDH-H. Mutations in LDHB cause lactate dehydrogenase B deficiency, a condition with no deleterious effects on health (4).
  1. Faloppi L. et al. (2016) Sci Rep. 6:24136.
  2. Ghosh, M. et al. (2016) Chem. Commun. 52:2401.
  3. Augoff, K. et al. (2015) Cancer Lett. 358:1.
  4. Maekawa M. et al. (1993). Hum. Genet. 91:423.
  5. Maekawa M. et al. (1990). Biochem. Biophys. Res. Commun. 168:677.

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