Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml .
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Ribosomes that exist freely in the cytosol or those attached to the ER are intrinsically the same in their translational properties. ER-bound ribosomes are responsible for the production of secretory proteins and integral ER, Golgi, lysosomal, and plasma membrane spanning proteins. Such proteins contain signal sequences that direct their synthesis to the ER membrane. As the nascent polypeptide emerges from the ribosome, a signal recognition particle (SRP) binds to the signal sequence and serves to couple the ribosome to the protein-translocating machinery in the ER membrane. Although the SRP is a 325 kDa ribonucleoprotein, its 54 kDa subunit (SRP54) mediates interaction with, and targeting of, the nascent protein to the ER. Via its C-terminal M-domain, SRP54 associates with the nascent protein and inhibits its elongation. This complex binds to the SRP receptor on the ER, the ribosome is delivered to the translocation machinery, SRP is released, and elongation resumes. Targeting and insertion are tightly coupled to a GTPase cycle that involves SRP54 and SRP receptor. Although the mechanisms are unclear, release of SRP from the ER-bound complex requires GTP hydrolysis.
Development References (2)
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Rapiejko PJ, Gilmore R. Empty site forms of the SRP54 and SR alpha GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum. Cell. 1997; 89(5):703-713. (Biology). View Reference
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Traianedes K, Findlay DM, Martin TJ, Gillespie MT. Modulation of the signal recognition particle 54-kDa subunit (SRP54) in rat preosteoblasts by the extracellular matrix. J Biol Chem. 1995; 270(36):20891-20894. (Biology). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.