Analytical Data
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Gene name
Carnmt1
- Application
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Alternative Names
Carnmt1；C9orf41；Carnosine 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
Q8N4J0
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Expression Region
1-409aa
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AA Sequence
MQRRRRPPPP TSRLPEGCGG GGGGSEEVEV QFSAGRWGSA AAVSAAAAAA TRSTEEEEER LEREHFWKII NAFRYYGTSM HERVNRTERQ FRSLPANQQK LLPQFLLHLD KIRKCIDHNQ EILLTIVNDC IHMFENKEYG EDGNGKIMPA STFDMDKLKS TLKQFVRDWS ETGKAERDAC YQPIIKEILK NFPKERWDPS KVNILVPGAG LGRLAWEIAM LGYACQGNEW SFFMLFSSNF VLNRCSEINK YKLYPWIHQF SNNRRSADQI RPIFFPDVDP HSLPPGSNFS MTAGDFQEIY SECNTWDCIA TCFFIDTAHN VIDYIDTIWK ILKPGGIWIN LGPLLYHFEN LANELSIELS YEDIKNVVLQ YGFKVEVEKE SVLSTYTVND LSMMKYYYEC VLFVVRKPQ
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Molecular Weight
47.1 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
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Protein Description
Carnmt1, also known as Carnitine O-acetyltransferase 1, is a pivotal enzyme involved in the metabolism of fatty acids and the carnitine shuttle, which plays a crucial role in energy production within the mitochondria. Research into Carnmt1 has gained momentum due to its significant implications in metabolic disorders and mitochondrial dysfunctions, conditions that have become increasingly prevalent in modern society. The enzyme facilitates the transfer of acetyl groups to carnitine, thereby promoting the transport of fatty acids across the mitochondrial membrane. Aberrations in Carnmt1 expression or activity have been linked to various metabolic diseases, including obesity, insulin resistance, and cardiovascular conditions. Understanding the precise mechanisms and regulation of Carnmt1 is essential for developing therapeutic strategies aimed at restoring metabolic health. Recent studies have focused on the recombinant expression of Carnmt1 to elucidate its structural and functional properties, which can provide insights into its enzymatic mechanisms and interactions with other metabolic pathways. Additionally, analyzing the reconstitution of Carnmt1 as a recombinant protein allows for the exploration of potential inhibitors or activators, thereby paving the way for novel treatments targeting metabolic dysfunctions. This area of research is vital in the context of increasing global health challenges related to obesity and metabolic syndrome, making it an important focus for future studies in biochemistry and pharmacology.
