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146839 Rabbit Anti-PRR5L (Proline-rich Protein 5-like, Protein Observed with Rictor-2, Protor-2, PROTOR2)

Specifications
References
Clone Type
Polyclonal
Host
Rabbit
Source
Human
Isotype
IgG
Grade
Affinity Purified
Applications
E IC IF WB
Crossreactivity
Hu Mo
Shipping Temp
Blue Ice
Storage Temp
-20°C

Proline-rich protein 5-like (PRR5L), also known as Protor-2, is structurally similar to PRR5 and also binds to the mTOR complex 2 (mTORC2). PRR5L is not required for mTORC2 integrity or kinase activity, but dissociates from mTORC2 upon knockdown of tuberous sclerosis complex 1 (TSC1) and TSC2. Knockdown of PRR5L reduced apoptosis in mTORC2 deficient cells as well as cells where mTOR was active, suggesting that mTORC2-dissociated PRR5L may promote apoptosis, and thus play a role in the balance between cell growth and cell death.

Applications
Suitable for use in ELISA, Western Blot, Immunofluorescence and Immunocytochemistry. Other applications not tested.
Recommended Dilution
Western Blot: 1ug/ml Immunocytochemistry: 10ug/ml Immunofluorescence: 20ug/ml Optimal dilutions to be determined by the researcher.
Positive Control
3T3 (NIH) Cell Lysate
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Synthetic peptide corresponding to 17aa from near the center of human PRR5L.
Form
Supplied as a liquid in PBS, 0.02% sodium azide.
Purity
Purified by immunoaffinity chromatography.
Specificity
Recognizes human PRR5L. Species Crossreactivity: mouse.
References
1. Thedieck K, Polak P, Kim ML, et al. 2007. PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis. PLoS One 2007; 2:e1217. 2. Pearce LR, Huang X, Boudeau J, et al. Identification of Protor as a novel Rictor-binding component of mTOR complex-2. Biochem. J. 2007; 405:513-22.
USBio References
No references available
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