Analytical Data
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Gene name
AGMAT
- Application
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Alternative Names
AGMAT;GDAH;Guanidino acid hydrolase. mitochondrial
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Species
E.coli
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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
B7LFJ6
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Expression Region
1-306aa
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AA Sequence
MSTLGHQYDNSLVSNAFGFLRLPMNFQPYDSDADWVITGVPFDMATSGRA GGRHGPAAIRQVSTNLAWEHNRFPWNFDMRERLNVVDCGDLVYAFGDARE MSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDA HTDTYANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIRTEFDIDNGFTVLD ACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGL TSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYIQ AAKKGE
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Molecular Weight
50 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
AGMAT (agmatine) is a biogenic amine derived from the amino acid arginine, primarily studied for its roles in various physiological processes. It functions as a neurotransmitter and has been implicated in neuroprotection, modulating nitric oxide synthesis, and exhibiting potential therapeutic effects in conditions like neuropathic pain and depression. The recombinant expression of AGMAT-related proteins has gained attention in the field of biotechnology, as it allows for the study of AGMAT’s biochemical pathways and its interactions with cellular systems. Researchers are particularly interested in employing recombinant techniques to produce AGMAT and its analogs for drug development, as well as to unravel the mechanisms of its action in the central nervous system. These investigations are crucial for understanding AGMAT's role in cellular signaling and may lead to novel therapeutic strategies that harness its beneficial effects while addressing neurological disorders. By optimizing AGMAT biosynthesis through recombinant technologies, the research aims to provide insights into its multifaceted functions and therapeutic potential, bridging the gap between basic science and clinical applications.











