Products

R3672-2 - OSBPL8 (C) Antibody, Rabbit Polyclonal

Catalog No. R3672-2
Product Name OSBPL8 (C) Antibody, Rabbit Polyclonal
Price $279
  
 

Quantity: 100 ul                                                                                      Application: WB

Predicted I Observed M.W.: 101 I 120 kDa                                              Uniprot ID: Q9BZF1


Background:

Oxysterol-binding protein-related protein 8 (OSBPL8) is a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Like most members, OSBPL8 contains an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain. OSBPL8 is involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. 

Other Names:

Oxysterol-binding protein-related protein 8, ORP-8, OSBP-related protein 8, KIAA1451, ORP8, OSBP10, MST120, MSTP120

Source and Purity:

Rabbit polyclonal antibodies were produced by immunizing animals with a GST-fusion protein containing the C-terminal region of human OSBPL8. Antibodies were purified by affinity purification using immunogen. 

Storage Buffer and Condition:

Supplied in 1 x PBS (pH 7.4), 100 ug/ml BSA, 40% Glycerol, 0.01% NaN3. Store at -20 °C. Stable for 6 months from date of receipt.

Species Specificity:

Human, Mouse

Tested Applications: 

WB: 1:500-1:2,000 (detect endogenous protein*)

*: The apparent protein size on WB may be different from the calculated M.W. due to modifications.

Product Data:

OSBPL8 Antibody Western (Abiocode) 

Fig 1. A) Western blot of total cell extracts from mouse brain, using
anti-OSBPL8 (C) (R3672-2) at RT for 2 h. B) Same as in A except
that protein extracts from human 293T cells transfected with a vector
(Vec) or Flag-OSBPL8 were used.