|Application ||WB, E|
|Other Accession||P19943, P99027, P42899, NP_000995|
|Predicted||Bovine, Mouse, Rabbit|
|Calculated MW||11665 Da|
|Antigen Region||13-41 aa|
|Other Names||60S acidic ribosomal protein P2, Renal carcinoma antigen NY-REN-44, RPLP2, D11S2243E, RPP2|
|Target/Specificity||This RPLP2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 13-41 amino acids from the N-terminal region of human RPLP2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||RPLP2 Antibody (N-Term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Plays an important role in the elongation step of protein synthesis.|
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Provided below are standard protocols that you may find useful for product applications.
RPLP2 consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This protein encodes a ribosomal phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the E. coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P1. The P2 protein can interact with P0 and P1 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
Martinez-Azorin,F. FEBS Lett. 582 (20), 3029-3032 (2008) Martinez-Azorin,F. Biochem. J. 413 (3), 527-534 (2008) Sugiyama,N. Mol. Cell Proteomics 6 (6), 1103-1109 (2007)
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