Analytical Data
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Gene name
OSBPL9
- Application
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Alternative Names
ORP9; OSBP4
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96SU4
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Expression Region
Gln498~His736
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Molecular Weight
66kDa
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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
OSBPL9, or Oxysterol Binding Protein-Like 9, is a member of the OSBP family of proteins that play pivotal roles in lipid metabolism and cellular signaling. The interest in OSBPL9 arises from its involvement in various physiological processes, including cholesterol transport, lipid raft formation, and cellular responses to oxysterols—oxidized derivatives of cholesterol that influence cellular processes such as inflammation and cell proliferation. Recent studies have indicated that OSBPL9 may be implicated in several pathological conditions, including cancer and metabolic disorders, suggesting that understanding its structure and function could pave the way for novel therapeutic strategies. Furthermore, the protein’s ability to interact with membranes and binding partners underscores its potential significance in cellular compartmentalization and signaling pathways. Given the increasing prevalence of diseases linked to dysregulated lipid homeostasis, the characterization and exploration of OSBPL9 via recombinant protein studies may provide valuable insights into its biological roles and therapeutic applications. By elucidating its molecular mechanisms and interactions, researchers aim to clarify how OSBPL9 contributes to health and disease, which is essential for developing targeted interventions in lipid-related disorders. Thus, OSBPL9 has emerged as a compelling subject for further investigation within the field of cell biology and biochemistry.
