Analytical Data
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Gene name
LIPH
- Application
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Alternative Names
LIPH；LPDLR；MPAPLA1；PLA1B；Lipase member H
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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
Q8WWY8
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Expression Region
19-451aa
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AA Sequence
EE TCPSFTRLSF HSAVVGTGLN VRLMLYTRKN LTCAQTINSS AFGNLNVTKK TTFIVHGFRP TGSPPVWMDD LVKGLLSVED MNVVVVDWNR GATTLIYTHA SSKTRKVAMV LKEFIDQMLA EGASLDDIYM IGVSLGAHIS GFVGEMYDGW LGRITGLDPA GPLFNGKPHQ DRLDPSDAQF VDVIHSDTDA LGYKEPLGNI DFYPNGGLDQ PGCPKTILGG FQYFKCDHQR SVYLYLSSLR ESCTITAYPC DSYQDYRNGK CVSCGTSQKE SCPLLGYYAD NWKDHLRGKD PPMTKAFFDT AEESPFCMYH YFVDIITWNK NVRRGDITIK LRDKAGNTTE SKINHEPTTF QKYHQVSLLA RFNQDLDKVA AISLMFSTGS LIGPRYKLRI LRMKLRSLAH PERPQLCRYD LVLMENVETV FQPILCPELQ L
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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
LIPH, or lysosomal integral membrane protein 2, is a key player in lipid metabolism and plays a crucial role in the lysosomal function of cells. Its primary function is associated with the hydrolysis of lysophosphatidic acid (LPA), a lipid signaling molecule involved in various physiological processes, including cell proliferation, migration, and survival. Dysregulation of LIPH has been implicated in several pathological conditions, including cancer, neurodegenerative diseases, and metabolic disorders. The study of recombinant LIPH protein has gained significance as researchers aim to elucidate its structure-function relationships and regulatory mechanisms. Understanding the exact role of LIPH in cellular metabolism and signaling pathways could provide insights into therapeutic targets for diseases linked to lipid dysregulation. Furthermore, the production of recombinant LIPH allows for detailed biochemical analysis and potential application in drug discovery, making it a valuable tool in both basic and applied research. By exploring the mechanisms through which LIPH contributes to cellular homeostasis and its dysregulation in disease states, researchers are hopeful to develop innovative strategies for intervention and treatment. Thus, LIPH serves as a promising focus for ongoing studies aimed at enhancing our understanding of lipid biology and its implications in health and disease.
