Analytical Data
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Gene name
LIPI
- Application
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Alternative Names
LIPI；LPDL；Lipase member I
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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
Q6XZB0
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Expression Region
16-460aa
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AA Sequence
DNKRP CLEFSQLSVK DSFRDLFIPR IETILMMYTR NNLNCAEPLF EQNNSLNVNF NTQKKTVWLI HGYRPVGSIP LWLQNFVRIL LNEEDMNVIV VDWSRGATTF IYNRAVKNTR KVAVSLSVHI KNLLKHGASL DNFHFIGVSL GAHISGFVGK IFHGQLGRIT GLDPAGPRFS RKPPYSRLDY TDAKFVDVIH SDSNGLGIQE PLGHIDFYPN GGNKQPGCPK SIFSGIQFIK CNHQRAVHLF MASLETNCNF ISFPCRSYKD YKTSLCVDCD CFKEKSCPRL GYQAKLFKGV LKERMEGRPL RTTVFLDTSG TYPFCTYYFV LSIIVPDKTM MDGSFSFKLL NQLGMIEEPR LYEKNKPFYK LQEVKILAQF YNDFVNISSI GLTYFQSSNL QCSTCTYKIQ RLMLKSLTYP ERPPLCRYNI VLKDREEVFL NPNTCTPKNT
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Molecular Weight
52.9 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
LIPI (Lysosomal Integral Membrane Protein I) is a protein implicated in various cellular processes, including lipid metabolism and lysosomal function. Its role in cellular homeostasis has attracted substantial interest in recent years, particularly due to its association with several diseases, including neurodegenerative disorders, where lysosomal dysfunction is a contributing factor. Research has shown that LIPI is involved in the regulation of lipid storage and degradation, making it a critical component of cellular lipid homeostasis. Furthermore, its potential as a therapeutic target for conditions linked to lysosomal dysfunction has prompted a growing body of work focused on LIPI's structural and functional properties. The study of recombinant LIPI protein has become essential for elucidating its mechanisms of action, as recombinant forms enable detailed analyses of its biochemical properties, interactions with other cellular components, and regulatory pathways. This research not only improves our understanding of LIPI's physiological roles but also opens avenues for developing innovative therapeutic strategies to address diseases associated with lysosomal dysfunction, thereby highlighting the importance of LIPI in biomedical research.
