Adenosylhomocysteinase (Protein name
), SAHH_RAT from NCBI database.
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General Annotation
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Antigen Annotation
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3D
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Predicted Eptitope
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Vaild Sequence
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Related Databases
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Gene name:
Ahcy;
Protein name:
Adenosylhomocysteinase(AdoHcyase);
Alternative:
S-adenosyl-L-homocysteine hydrolase;
Organism:
Rat (Rattus norvegicus).
General Annotation
Sub Unit:
Homotetramer.
Function:
Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
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s
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Precision
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Intra-assay Precision (Precision within an assay):Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.
Intra-Assay CV: ≤8.2%
Inter-assay Precision (Precision between assays):Three samples of known concentration were tested in five separate assays to assess inter-assay precision.
Inter-Assay CV: ≤11.7%
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Recovery
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Recovery was determined by spiking various levels of SAHH into serum and plasma .
Sample Type
Average(%)
Recovery Range(%)
Serum
108
105-113
Plasma
106
102-108
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Linearity
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The linearity of the kit was assayed by testing samples spiked with appropriate concentration of SAHH and their serial dilutions. The results were demonstrated by the percentage of calculated concentration to the expected.
Sample
1:2
1:4
1:8
1:16
serum(n=5)
106-112%
102-112%
104-110%
103-114%
EDTA plasma(n=5)
103-114%
104-114%
100-115%
105-111%
heparin plasma(n=5)
102-103%
103-112%
101-114%
106-109%
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];PARTIAL PROTEIN SEQUENCE
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Cited for: PROTEIN SEQUENCE OF 143-151 AND 268-285;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD;COFACTOR;SUBUNIT
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Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT GLU-245
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Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS);MUTAGENESIS OF ASP-131; LYS-186; ASP-190 AND ASN-191