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AB229458

Anti-RPL22 antibody

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(6 Publications)

Rabbit Polyclonal RPL22 antibody. Suitable for WB, IHC-P and reacts with Human, Rat samples. Cited in 6 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human RPL22.

View Alternative Names

Large ribosomal subunit protein eL22, 60S ribosomal protein L22, EBER-associated protein, Epstein-Barr virus small RNA-associated protein, Heparin-binding protein HBp15, EAP, RPL22

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-RPL22 antibody (AB229458)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-RPL22 antibody (AB229458)

Paraffin-embedded rat brain tissue stained for RPL22 using ab229458 at 1/500 dilution in immunohistochemical analysis.

Western blot - Anti-RPL22 antibody (AB229458)
  • WB

Supplier Data

Western blot - Anti-RPL22 antibody (AB229458)

15% SDS-PAGE gel.

All lanes:

Western blot - Anti-RPL22 antibody (ab229458) at 1/500 dilution

All lanes:

HepG2 (human liver hepatocellular carcinoma cell line) whole cell extract at 30 µg

Predicted band size: 15 kDa

true

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human, Rat

Applications

IHC-P, WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Human RPL22.

P35268

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.025% Proclin 300 Constituents: PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°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.

RPL22 also known as Ribosomal Protein L22 is a component of the 60S subunit of ribosomes playing an important role in protein synthesis. It has an approximate molecular weight of 16 kDa. Expression of RPL22 occurs in various tissues but it shows high levels in the brain liver and spleen. The protein's structural role within the ribosome allows it to contribute to the assembly and stability necessary for ribosomal function.
Biological function summary

RPL22 contributes to ribosomal biogenesis by being part of a larger ribonucleoprotein complex. It participates in the assembly of the 60S subunit of ribosomes which is essential for translation. The proper function of RPL22 ensures accurate and efficient polypeptide elongation during protein synthesis. Being a part of the ribosomal machinery RPL22 impacts cell proliferation and growth as ribosomes are critical for producing proteins needed for cell development and function.

Pathways

RPL22 plays a role in the translation machinery impacting the protein synthesis pathway. It interacts with other ribosomal proteins such as RPL5 and RPL10 which together facilitate the translation of mRNA into protein. Additionally RPL22 has relevance in the mTOR signaling pathway an important regulator of cell growth and proliferation where it affects processes by influencing ribosomal output and protein translation directly.

RPL22 links to conditions such as cancer and Diamond-Blackfan anemia. Its aberrant expression or mutations can affect ribosome function contributing to tumorigenesis due to uncontrolled protein synthesis and cell proliferation. In particular studies show that leukemia and solid tumors may involve altered RPL22 activity. In Diamond-Blackfan anemia disrupted ribosomal biogenesis due to mutations in RPL22 associates with bone marrow failure. The protein's interactions with other ribosomal proteins like RPS19 help illustrate its potential involvement in these diseases.

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 : 32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed : 23636399, PubMed : 32669547).
See full target information RPL22

Publications (6)

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

Journal of the American Chemical Society 146:12410-12422 PubMed38669207

2024

Programmable RNA Loading of Extracellular Vesicles with Toehold-Release Purification.

Applications

Unspecified application

Species

Unspecified reactive species

Mette Galsgaard Malle,Ping Song,Philipp M G Löffler,Nazmie Kalisi,Yan Yan,Julián Valero,Stefan Vogel,Jørgen Kjems

Neural development 19:1 PubMed38167468

2024

Loss of G9a does not phenocopy the requirement for Prdm12 in the development of the nociceptive neuron lineage.

Applications

Unspecified application

Species

Unspecified reactive species

Panagiotis Tsimpos,Simon Desiderio,Pauline Cabochette,Philippe Poelvoorde,Sadia Kricha,Luc Vanhamme,Coralie Poulard,Eric J Bellefroid

Nature cell biology 24:1541-1557 PubMed36192632

2022

Alternative RNA splicing modulates ribosomal composition and determines the spatial phenotype of glioblastoma cells.

Applications

Unspecified application

Species

Unspecified reactive species

Tatyana D Larionova,Soniya Bastola,Tatiana E Aksinina,Ksenia S Anufrieva,Jia Wang,Victoria O Shender,Dmitriy E Andreev,Tatiana F Kovalenko,Georgij P Arapidi,Polina V Shnaider,Anastasia N Kazakova,Yaroslav A Latyshev,Victor V Tatarskiy,Alexander A Shtil,Pascale Moreau,Francis Giraud,Chaoxi Li,Yichan Wang,Maria P Rubtsova,Olga A Dontsova,Michael Condro,Benjamin M Ellingson,Mikhail I Shakhparonov,Harley I Kornblum,Ichiro Nakano,Marat S Pavlyukov

Bioengineered 13:6650-6664 PubMed35230214

2022

L22 ribosomal protein is involved in dynamin-related protein 1-mediated gastric carcinoma progression.

Applications

Unspecified application

Species

Unspecified reactive species

Jianghong Cheng,Zizhuo Sha,Ruisan Zhang,Jinghao Ge,Peng Chen,Xuefeng Kuang,Jiazhi Chang,Kai Ren,Xianyang Luo,Shuai Chen,Xingchun Gou

Biomedicines 9: PubMed34572398

2021

Cyclic Hypoxia Conditioning Alters the Content of Myoblast-Derived Extracellular Vesicles and Enhances Their Cell-Protective Functions.

Applications

Unspecified application

Species

Unspecified reactive species

Yan Yan,Tingting Gu,Stine Duelund Kaas Christensen,Junyi Su,Thomas Ravn Lassen,Marie Vognstoft Hjortbak,IJu Lo,Susanne Trillingsgaard Venø,Andrea Erzsebet Tóth,Ping Song,Morten Schallburg Nielsen,Hans Erik Bøtker,Blagoy Blagoev,Kim Ryun Drasbek,Jørgen Kjems

Frontiers in immunology 12:699900 PubMed34220863

2021

RPL22 Overexpression Promotes Psoriasis-Like Lesion by Inducing Keratinocytes Abnormal Biological Behavior.

Applications

Unspecified application

Species

Unspecified reactive species

Jinrong Zeng,Yue Zhang,Hanyi Zhang,Yuezhong Zhang,Lihua Gao,Xiaoliang Tong,Yajie Xie,Qian Hu,Chunli Chen,Shu Ding,Jianyun Lu
View all publications

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