Recombinant Human Adenosylhomocysteinease/AHCY Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 6466-AH

R&D Systems, part of Bio-Techne
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6466-AH-010
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Key Product Details

Source

E. coli

Accession #

P23526

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Adenosylhomocysteinase/AHCY Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human Adenosylhomocysteinase/AHCY protein
Ser2-Tyr432, with an N-terminal Met and 6-His tag

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

49 kDa

SDS-PAGE

43 kDa, reducing conditions

Activity

Measured by the hydrolysis of S-adenosyl-L-homocysteine.
The specific activity is >350 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

6466-AH
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Background: Adenosylhomocysteinase/AHCY

Human S‑Adenosylhomocysteinase (AHCY) is a cytoplasmic tetramer with a tightly bound NAD co‑factor for each subunit (1, 2). It is the only known enzyme to catalyze the breakdown of S‑adenosylhomocysteine (AdoHcy) to homocysteine and adenosine. AdoHcy hydrolysis is a reversible reaction with an equilibrium favoring AdoHcy formation, but hydrolysis prevails under physiological conditions due to the rapid removal of adenosine and homocysteine. Thus, AHCY’s activity in mammals is directly related to homocysteine level, an independent risk factor for vascular disease (3). It also functions as a regulator of biological transmethylation by controlling the concentration of AdoHcy, a potent competitive inhibitor of all S-adenosyl-L-methionine methyltransferases (1). A mutation in the human AHCY results in AHCY deficiency with increase of plasma creatine kinase, methionine, S‑adenosylmethionine and AdoHcy, delay of myelination, myopathy and psychomotor retardation (4, 5).

References

  1. Turner, M. A. et al. (2000) Cell Biochem. Biophys. 33:101.
  2. Takata, Y. et al. (2002) J. Biol. Chem. 277:22670.
  3. Gellekink, H. et al. (2004) Eur. J. Hum. Genet. 12:942.
  4. Baric, I. et al. (2004) Proc. Natl. Acad. Sci. USA. 101:4234.
  5. Fumic, K. et al. (2007) Eur. J.Hum. Genet. 15:347. 

Alternate Names

AdoHcyase, AHCY, SAHH

Entrez Gene IDs

191 (Human)

Gene Symbol

AHCY

UniProt

P23526 (Human)

Additional Adenosylhomocysteinase/AHCY Products

Product Documents for Recombinant Human Adenosylhomocysteinease/AHCY Protein, CF

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Product Specific Notices for Recombinant Human Adenosylhomocysteinease/AHCY Protein, CF

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