| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LYPLA2 |
| Uniprot No | O95372 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-231aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMCGNTMSVPLLTDAATVSGAERETAAVIFL HGLGDTGHSWADALSTIRLPHVKYICPHAPRIPVTLNMKMVMPSWFDLMG LSPDAPEDEAGIKKAAENIKALIEHEMKNGIPANRIVLGGFSQGGALSLY TALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAILQCHGELDPMVP VRFGALTAEKLRSVVTPARVQFKTYPGVMHSSCPQEMAAVKEFLEKLLPP V |
| 预测分子量 | 27 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
nan
LYPLA2 (lysophospholipase 2), also known as acylprotein thioesterase 2. is a member of the serine hydrolase superfamily. This enzyme plays a critical role in lipid metabolism by catalyzing the hydrolysis of acylated residues from proteins or lysophospholipids, thereby regulating post-translational modifications and lipid signaling pathways. Structurally, it contains a conserved α/β-hydrolase fold and a catalytic triad (Ser-Asp-His) essential for its enzymatic activity. LYPLA2 is implicated in modulating cellular processes such as membrane trafficking, signal transduction, and energy homeostasis through its interaction with lipid substrates like palmitate or myristate.
Research has linked LYPLA2 dysfunction to metabolic disorders, including obesity and insulin resistance, as it influences lipid storage and adipocyte differentiation. Additionally, its role in depalmitoylating specific proteins (e.g., H-Ras, Gα subunits) highlights its regulatory potential in oncogenic signaling and neurological diseases. For instance, altered LYPLA2 activity has been observed in Alzheimer’s disease, where lipid dysregulation contributes to amyloid-beta pathology.
Recombinant LYPLA2 protein is typically produced using expression systems like *E. coli* or mammalian cells, enabling biochemical and structural studies. Purification methods often involve affinity chromatography followed by functional validation via fluorometric or mass spectrometry-based assays. Its recombinant form serves as a tool to investigate substrate specificity, inhibitor screening for therapeutic development, and deciphering mechanisms underlying lipid-associated diseases. Recent advances in cryo-EM and X-ray crystallography have further elucidated its dynamic substrate-binding pockets, fostering targeted drug design. Overall, recombinant LYPLA2 remains pivotal in bridging molecular insights with translational applications in metabolic and neurodegenerative research.
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