Rabbit Polyclonal RPLP0 antibody. Suitable for WB, IHC-P and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human RPLP0 aa 50 to C-terminus.
IgG
Rabbit
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 79.99% PBS, 20% Glycerol (glycerin, glycerine)
Liquid
Polyclonal
WB | IHC-P | |
---|---|---|
Human | Tested | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/500.00000 - 1/3000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
Select an associated product type
Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
60S acidic ribosomal protein P0, 60S ribosomal protein L10E, Large ribosomal subunit protein uL10, RPLP0
Rabbit Polyclonal RPLP0 antibody. Suitable for WB, IHC-P and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human RPLP0 aa 50 to C-terminus.
60S acidic ribosomal protein P0, 60S ribosomal protein L10E, Large ribosomal subunit protein uL10, RPLP0
IgG
Rabbit
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 79.99% PBS, 20% Glycerol (glycerin, glycerine)
Liquid
Polyclonal
Affinity purification Immunogen
Blue Ice
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
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This supplementary information is collated from multiple sources and compiled automatically.
RPLP0 also known as 60S acidic ribosomal protein P0 is an integral component of the ribosomal machinery. It acts as a scaffold within the large 60S subunit of the ribosome which plays a fundamental role in protein synthesis. The protein has an approximate mass of 34.4 kDa. RPLP0 is ubiquitously expressed across various tissues indicating its essential role in cellular biology. Its expression is well-documented in highly proliferative tissues and organs reflecting the ribosome's central role in maintaining cellular growth and division.
RPLP0 participates actively in ribosome structure and function. It forms part of the ribosomal stalk together with the P1 and P2 proteins facilitating interactions with GTPase translation factors during protein synthesis. This ribosomal complex is important for elongation phase of protein translation where it actively assists in the accurate and efficient elongation of polypeptide chains. By participating in the ribosome's structural framework RPLP0 drives the translation process influencing protein output in cells. This makes it essential for overall protein homeostasis.
RPLP0 is deeply embedded within the processes of translation and ribosome biogenesis. It associates with the major pathway of ribosome assembly wherein new ribosomes are synthesized and configured. It functions alongside other ribosomal proteins like RPLP1 and RPLP2 which work together to maintain efficient protein synthesis. The interaction among these proteins within the translation pathway highlights the integrated nature of RPLP0 in facilitating cellular protein production.
RPLP0 has notable implications in cancer and Diamond-Blackfan anemia (DBA). Aberrations in ribosomal proteins including RPLP0 have been linked to oncogenesis where disrupted protein synthesis contributes to uncontrolled cellular proliferation. Additionally alterations in RPLP0 have associations with DBA a ribosomopathy characterized by defective red blood cell production. Within these disease contexts RPLP0's interaction with other ribosomal proteins like RPL11 can influence disease progression and cellular anomalies seen in such conditions.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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Immunohistochemical analysis of paraffin-embedded Human colon carcinoma tissue labeling RPLP0 with ab154970 at 1/500 dilution.
12% SDS PAGE
All lanes: Western blot - Anti-RPLP0 antibody (ab154970) at 1/1000 dilution
Lane 1: 293T whole cell lysate at 30 µg
Lane 2: A431 whole cell lysate at 30 µg
Predicted band size: 34 kDa
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