Analytical Data
-
Gene name
OSBP
- Application
-
Alternative Names
OSBP;OSBP1;Oxysterol-binding Protein 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P22059
-
Expression Region
324-407aa
-
AA Sequence
GATVLPANTPGNVGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLG HKRTGSNISGASSDISLDEQYKHQLEETKKEKRT
-
Molecular Weight
35 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
OSBP (Oxysterol-Binding Protein) is a pivotal player in cellular lipid metabolism and signaling, functioning as a lipid sensor that interacts with oxysterols, a class of bioactive lipids derived from cholesterol. Research into OSBP has gained momentum due to its critical role in regulating the transport of lipids between cellular organelles, specifically the endoplasmic reticulum and the Golgi apparatus, thereby influencing various cellular processes including membrane biogenesis, cell proliferation, and apoptosis. OSBP also serves as an important mediator in the response to cellular stress and has been implicated in several pathological conditions, such as cardiovascular diseases and cancer, highlighting its potential as a therapeutic target. The study of OSBP recombinant proteins has provided valuable insights into its molecular mechanisms and interactions with other proteins and lipids. By elucidating the structural and functional aspects of OSBP, researchers aim to uncover the complexities of lipid metabolism and develop novel strategies for intervention in diseases associated with dysregulated lipid homeostasis. The development of recombinant OSBP proteins facilitates a better understanding of their biochemical properties, enabling the exploration of their role in cellular signaling pathways and overall lipid management within the cell. As such, the research on OSBP and its recombinant proteins is vital for advancing our understanding of lipid biology and its implications in health and disease.











