RPL15 AntibodyСпецификацияОбъем | 100 мкл | Синонимы | 60S ribosomal protein L15, EC45, RL15, | Клональность | Polyclonal Antibody | Организм | Human | uniprot | P61313 | Иммуноген | Synthesized peptide derived from internal of human RPL15. | Источник | Rabbit | Видовая специфичность | Human, Mouse, Rat | Применение | ELISA, WB,WB:1:500-1:3000 | Примечание | Ribosomes, the organelles that catalyze protein synthesis, 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 gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L15E family of ribosomal proteins. It is located in the cytoplasm. This gene shares sequence similarity with the yeast ribosomal protein YL10 gene. Although this gene has been referred to as RPL10, its official symbol is RPL15. This gene has been shown to be overexpressed in some esophageal tumors compared to normal matched tissues. Alternate splicing results in multiple transcript variants. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.<br/><br/>Herzog H., Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.<br/>Wang Q., Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.<br/>Yoshihama M., Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. | Клональность1 | Polyclonal | Изотип | IgG | Коньюгат | Non-conjugated | Буффер | Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. | Форма | liquid | Хранение | Upon receipt, store at -20°C or -80°C. Avoid repeated freeze. | Метод очистки | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. | Области исследований | Others | Ссылка на страницу на сайте производителя | ссылка | Western blot analysis of extracts from K562 cells and LOVO cells, using RPL15 antibody.
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