Analytical Data
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Gene name
LATH
- Application
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Alternative Names
LATH；BASE；LATH；Putative BPIFA4P Protein
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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
Q86YQ2
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Expression Region
21-179aa
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AA Sequence
QEVLAGVSSQ LLNDLTQGLL RADFLPSLQT TGLQKPLSSA FDGVSGLLDI FGPPLTNEIN TVSIQVKNPQ LLHVSIESTP QRKEATVQVP FTSELIVQLL TMKPFTANMQ SDIKVQIRLE KNVGGRYELA FGNCRLLPEA IWIQTGVQLA PAQNLLWQT
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Molecular Weight
19.4 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
LATH, or Lysophosphatidic Acid Acyltransferase, is an enzyme that plays a crucial role in lipid metabolism, specifically in the biosynthesis of glycerolipids. Recent research has highlighted its significance in various physiological and pathological processes, including cell signaling, inflammation, and cancer progression. The functional characterization of LATH has gained attention due to its involvement in the production of lysophosphatidic acid (LPA), a bioactive lipid that influences cell proliferation, migration, and survival. Additionally, aberrant levels of LPA have been associated with several diseases, making LATH a potential therapeutic target. To better understand its function, researchers have focused on the recombinant expression of LATH, allowing for detailed biochemical analysis and structural studies. This approach facilitates the investigation of its mechanistic role in lipid metabolism and interaction with other signaling pathways. The insights gained from these studies may pave the way for the development of novel lipid-targeted therapies for conditions linked to dysregulated LPA signaling. Overall, the research into LATH and its recombinant protein forms holds promise for advancing our understanding of complex lipid networks in health and disease.
