Analytical Data
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Gene name
GAMT
- Application
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Alternative Names
GAMT;Guanidinoacetate N-methyltransferase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14353
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Expression Region
1-236aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSAPSATPIFAPGENCSPAWGAAPAAYDAA DTHLRILGKPVMERWETPYMHALAAAASSKGGRVLEVGFGMAIAASKVQE APIDEHWIIECNDGVFQRLRDWAPRQTHKVIPLKGLWEDVAPTLPDGHFD GILYDTYPLSEETWHTHQFNFIKNHAFRLLKPGGVLTYCNLTSWGELMKS KYSDITIMFEETQVPALLEAGFRRENIRTEVMALVPPADCRYYAFPQMIT PLVTKGLEHH HHHH
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Molecular Weight
30 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
GAMT (Guanosine monophosphate activation enzyme) is a critical enzyme involved in the biosynthesis of creatine, which plays a vital role in energy metabolism within muscle and brain tissues. The significance of GAMT is underscored by its involvement in the creatine biosynthesis pathway, where it catalyzes the conversion of guanidinoacetate and ATP into creatine and AMP. Deficiencies in GAMT can lead to severe neurological disorders, including GAMT deficiency, characterized by intellectual disability, seizures, and movement disorders due to compromised energy metabolism in the brain. Therefore, understanding GAMT's structure and function is crucial for development of therapeutic strategies. Recent advancements in recombinant protein technology have enabled the production of GAMT in heterologous systems, allowing for detailed functional studies and structural characterization. These efforts have facilitated the exploration of GAMT's enzymatic mechanisms, regulation, and potential as a drug target for metabolic diseases. Furthermore, recombinant GAMT could serve as a tool for therapeutic enzyme replacement in affected individuals, highlighting the enzyme's relevance in translational research and clinical applications. Understanding the biochemical properties and potential applications of GAMT can pave the way for innovations in treating energy metabolism disorders, ultimately contributing to improved health outcomes.
