Recombinant Rat Guanidinoacetate N-methyltransferase(Gamt) CSB-EP009227RA
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Gamt; Guanidinoacetate N-methyltransferase; EC 2.1.1.2
Species: (Organism)
Rattus norvegicus (Rat)
Gene Names:
Gamt
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
MSSSAASPLFAPGEDCGPAWRAAPAAYDTSDTHLQILGKPVMERWETPYMHSLAAAAASRGGRVLEVGFGMAIAASRVQQAPIKEHWIIECNDGVFQRLQNWALKQPHKVVPLKGLWEEEAPTLPDGHFDGILYDTYPLSEETWHTHQFNFIKTHAFRLLKPGGILTYCNLTSWGELMKSKYTDITAMFEETQVPALLEAGFQRENICTEVMALVPPADCRYYAFPQMITPLVTKH
Expression Region:
1-236aa
Subcellular Location:
Tissue Specificity:
Expressed in hepatic primordium in the embryo as soon as 12.5 days. In the adult, high levels of expression are found in liver and pancreas. Ubiquitously expressed in neuronal and glial cells in the brain.
Protein Length:
Full Length
Pathway:
Mol. Weight:
30.4 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Others
Function:
Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development.
Involvement in disease:
Relevance:
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Class I-like SAM-binding methyltransferase superfamily, RMT2 methyltransferase family
Reference:
crystal structures of guanidinoacetate methyltransferase ternary complexes.Komoto J., Yamada T., Takata Y., Konishi K., Ogawa H., Gomi T., Fujioka M., Takusagawa F.Biochemistry 43:14385-14394(2004)
