Analytical Data
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Gene name
LPXN
- Application
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Alternative Names
LPXN；LDLP；Leupaxin
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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
O60711
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Expression Region
1-386aa
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AA Sequence
MEELDALLEE LERSTLQDSD EYSNPAPLPL DQHSRKETNL DETSEILSIQ DNTSPLPAQL VYTTNIQELN VYSEAQEPKE SPPPSKTSAA AQLDELMAHL TEMQAKVAVR ADAGKKHLPD KQDHKASLDS MLGGLEQELQ DLGIATVPKG HCASCQKPIA GKVIHALGQS WHPEHFVCTH CKEEIGSSPF FERSGLAYCP NDYHQLFSPR CAYCAAPILD KVLTAMNQTW HPEHFFCSHC GEVFGAEGFH EKDKKPYCRK DFLAMFSPKC GGCNRPVLEN YLSAMDTVWH PECFVCGDCF TSFSTGSFFE LDGRPFCELH YHHRRGTLCH GCGQPITGRC ISAMGYKFHP EHFVCAFCLT QLSKGIFREQ NDKTYCQPCF NKLFPL
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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
LPXN, or Lipid Phosphate Phosphatase, is a crucial protein involved in various cellular processes, including cytoskeletal dynamics, cell migration, and signal transduction. Recent studies have highlighted its significant role in regulating cell adhesion and motility, which are essential for numerous physiological and pathological processes, including developmental biology, wound healing, and cancer metastasis. The recombinant expression of LPXN provides a valuable tool for elucidating its functional mechanisms and interaction partners. By studying LPXN in a controlled environment, researchers hope to uncover its specific roles in cellular signaling pathways and how its dysregulation may contribute to diseases like cancer and inflammatory disorders. The exploration of LPXN through recombinant protein techniques not only enhances our understanding of its biological functions but also opens avenues for therapeutic interventions targeting LPXN-related pathways. As a result, LPXN continues to garner attention in molecular biology and biomedical research, paving the way for potential advancements in treatment strategies.
