Analytical Data
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Gene name
LPGAT1
- Application
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Alternative Names
LPGAT1; FAM34A; KIAA0205; Acyl-CoA:lysophosphatidylglycerol acyltransferase 1; Acyl-CoA:monoacylglycerol acyltransferase LPGAT1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92604
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Expression Region
1-370aa
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AA Sequence
MAITLEEAPWLGWLLVKALMRFAFMVVNNLVAIPSYICYVIILQPLRVLDSKRFWYIEGIMYKWLLGMVASWGWYAGYTVMEWGEDIKAVSKDEAVMLVNHQATGDVCTLMMCLQDKGLVVAQMMWLMDHIFKYTNFGIVSLVHGDFFIRQGRSYRDQQLLLLKKHLENNYRSRDRKWIVLFPEGGFLRKRRETSQAFAKKNNLPFLTNVTLPRSGATKIILNALVAQQKNGSPAGGDAKELDSKSKGLQWIIDTTIAYPKAEPIDIQTWILGYRKPTVTHVHYRIFPIKDVPLETDDLTTWLYQRFVEKEDLLSHFYETGAFPPSKGHKEAVSREMTLSNLWIFLIQSFAFLSGYMWYNIIQYFYHCLF
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Molecular Weight
69.5 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
LPGAT1 (Lysophosphatidylglycerol acyltransferase 1) is an enzyme that plays a critical role in the biosynthesis of glycerolipids, which are essential components of cell membranes. This enzyme catalyzes the acylation of lysophosphatidylglycerol to form phosphatidylglycerol, a key lipid involved in various cellular functions, including membrane dynamics, signaling pathways, and energy metabolism. Research into LPGAT1 has gained momentum due to its potential implications in various biological processes and diseases, such as cardiovascular disorders, metabolic syndromes, and neurological conditions. The recombinant expression of LPGAT1 in heterologous systems provides a valuable tool for studying its biochemical characteristics and functional significance. Understanding the enzyme's structure, substrate specificity, and regulatory mechanisms can shed light on its role in lipid metabolism and its contribution to disease pathology. Furthermore, recombinant LPGAT1 can serve as a platform for developing therapeutic strategies aimed at modulating lipid profiles in disease states, highlighting the importance of ongoing research in this area. Overall, the exploration of LPGAT1 not only advances our knowledge of lipid biochemistry but also opens avenues for innovative treatments targeting related metabolic and degenerative diseases.
