Analytical Data
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Gene name
LPCAT3
- Application
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Alternative Names
LPCAT3；MBOAT5；OACT5；Lysophospholipid acyltransferase 5
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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
Q6P1A2
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Expression Region
1-487aa
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AA Sequence
MASSAEGDEGTVVALAGVLQSGFQELSLNKLATSLGASEQALRLIISIFLGYPFALFYRHYLFYKETYLIHLFHTFTGLSIAYFNFGNQLYHSLLCIVLQFLILRLMGRTITAVLTTFCFQMAYLLAGYYYTATGNYDIKWTMPHCVLTLKLIGLAVDYFDGGKDQNSLSSEQQKYAIRGVPSLLEVAGFSYFYGAFLVGPQFSMNHYMKLVQGELIDIPGKIPNSIIPALKRLSLGLFYLVGYTLLSPHITEDYLLTEDYDNHPFWFRCMYMLIWGKFVLYKYVTCWLVTEGVCILTGLGFNGFEEKGKAKWDACANMKVWLFETNPRFTGTIASFNINTNAWVARYIFKRLKFLGNKELSQGLSLLFLALWHGLHSGYLVCFQMEFLIVIVERQAARLIQESPTLSKLAAITVLQPFYYLVQQTIHWLFMGYSMTAFCLFTWDKWLKVYKSIYFLGHIFFLSLLFILPYIHKAMVPRKEKLKKME
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Molecular Weight
56 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
LPCAT3, or Lysophosphatidylcholine acyltransferase 3, is an important enzyme involved in the biosynthesis of phospholipids, specifically in the acylation of lysophosphatidylcholine to form phosphatidylcholine. This metabolic process is crucial for maintaining cellular membrane integrity, lipid metabolism, and signaling pathways. Recent studies have implicated LPCAT3 in various physiological and pathological conditions, including inflammation, obesity, and metabolic disorders. Given its role in lipid metabolism, LPCAT3 has garnered attention as a potential therapeutic target for managing these conditions. The recombinant production of LPCAT3 allows researchers to investigate its enzymatic properties, substrate specificity, and regulatory mechanisms in detail. By utilizing techniques such as molecular cloning and protein expression, scientists can generate large quantities of purified LPCAT3 for biochemical assays and structural studies. Understanding the function and regulation of LPCAT3 can shed light on its contribution to cellular homeostasis and disease progression, ultimately paving the way for the development of novel pharmacological strategies that are aimed at modulating LPCAT3 activity for therapeutic benefit.
