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AB157111

Anti-RPL26 antibody

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(1 Publication)

Goat Polyclonal RPL26 antibody. Suitable for WB and reacts with Human, Mouse samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human RPL26 aa 50 to C-terminus.

View Alternative Names

Large ribosomal subunit protein uL24, 60S ribosomal protein L26, RPL26

1 Images
Western blot - Anti-RPL26 antibody (AB157111)
  • WB

Unknown

Western blot - Anti-RPL26 antibody (AB157111)

All lanes:

Western blot - Anti-RPL26 antibody (ab157111) at 0.4 µg/mL

Lane 1:

293T whole cell lysate at 50 µg

Lane 2:

293T whole cell lysate at 15 µg

Lane 3:

HeLa whole cell lysate at 50 µg

Lane 4:

Jurkat whole cell lysate at 50 µg

Lane 5:

NIH/3T3 whole cell lysate at 50 µg

Predicted band size: 17 kDa

true

Exposure time: 3min

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human, Mouse

Applications

WB

applications

Immunogen

Synthetic Peptide within Human RPL26 aa 50 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

P61254

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 - 8 Preservative: 0.09% Sodium azide Constituents: 99% Tris citrate/phosphate
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

RPL26 also known as Ribosomal Protein L26 is a component of the 60S subunit of the ribosome. It has a mass of approximately 17 kDa. This protein primarily expresses in tissues with high levels of protein synthesis including muscle liver and brain. As part of the ribosome RPL26 plays an essential role in the synthesis of proteins by facilitating the assembly of amino acids into polypeptide chains.
Biological function summary

RPL26 contributes to the complex process of translation by ensuring the stability and proper function of the ribosome. As a structural part of the large ribosomal subunit it helps maintain the integrity of the ribosomal architecture necessary for effective translation. This protein also indirectly affects mRNA processing and mRNA stability both of which influence the efficiency of protein synthesis.

Pathways

RPL26 participates in translation and ribosome biogenesis pathways. It interacts closely with other ribosomal proteins and rRNA to form the functional ribosome. Within these pathways RPL26 is linked with proteins like RPL5 and RPL11 which also contribute to the assembly and stability of the ribosome. Efficient protein synthesis by this pathway is fundamental for cellular growth and proliferation.

RPL26 is associated with conditions like Diamond-Blackfan anemia and cancer. Diamond-Blackfan anemia is a ribosomopathy resulting from mutations in ribosomal proteins including RPL26 disrupting normal erythropoiesis. The depletion or malfunction of RPL26 can also influence cancer progression by altering the translational capacity of cancer cells affecting proteins like p53 that control cell cycle and apoptosis.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Component of the large ribosomal subunit (PubMed : 23636399, PubMed : 26100019, PubMed : 32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed : 23636399, PubMed : 26100019, PubMed : 32669547).
See full target information RPL26

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Histochemistry and cell biology 149:75-96 PubMed28983690

2017

Subcellular localization and characterization of estrogenic pathway regulators and mediators in Atlantic salmon spermatozoal cells.

Applications

Unspecified application

Species

Unspecified reactive species

Kristian R von Schalburg,Brent E Gowen,Jong S Leong,Eric B Rondeau,William S Davidson,Ben F Koop
View all publications

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