Human Recombinant MAT1A protein, GST-TEV Tag (V2LY-0526-LY5473)

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host
Baculovirus-Insect Cells
Protein Species
Human
Tag
GST-TEV Tag
Protein Construction
This product is Human Recombinant MAT1A protein, GST-TEV Tag consist of Amino Acid: 1-395 and predicts a molecular mass of 65 kDa.
Molecule Mass
65 kDa
Sequence
Amino Acid: 1-395
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
Batch dependent.
Endotoxin
Please contact us for more information.
Format
Liquid
Buffer
Tris, NaCl, Glutathione, EDTA, DTT, PMSF, Glycerol
Preservative
None
Storage
Store product at -70°C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
More Infomation

Target

Full Name
methionine adenosyltransferase I, alpha
Function
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Biological Process
Methionine catabolic process Source: UniProtKB
One-carbon metabolic process Source: UniProtKB-KW
Protein homotetramerization Source: UniProtKB
S-adenosylmethionine biosynthetic process Source: ComplexPortal
Cellular Location
Cytosol
Other locations
methionine adenosyltransferase complex
Involvement in disease
Methionine adenosyltransferase deficiency (MATD):
An inborn error of metabolism resulting in isolated hypermethioninemia. Most patients have no clinical abnormalities, although some neurologic symptoms may be present in rare cases with severe loss of methionine adenosyltransferase activity.
PTM
S-nitrosylation of Cys-120 inactivates the enzyme.
An intrachain disulfide bond can be formed. The protein structure shows that the relevant Cys residues are in a position that would permit formation of a disulfide bond.
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For research use only. Not intended for any clinical use.

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