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Recombinant human RPL30 protein

Ribosomes, the organelles that catalyze protein synthesis, consists 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. RPL30 is a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L30E family of ribosomal proteins. It is located in the cytoplasm. This gene is co-transcribed with the u72 small nucleolar RNA gene, which is located in its fourth intron. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. Recombinant human RPL30 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

Product Specifications

Product Name Alternative

60S ribosomal protein L30, L30

Expression System

E.coli

Antigen Species

Human

Tag

His-Tag

Applications

SDS-PAGE

Concentration

0.25 mg/mL (determined by Bradford assay)

Purity

> 90% by SDS-PAGE

Molecular Weight

15.2 kDa (138aa) confirmed by MALDI-TOF

Additionnal Information

RPL30, 60S ribosomal protein L30, L30, ATGP2273-10 µg, ATGP2273-20 µg, ATGP2273-50 µg, ATGP2273-100 µg, ATGP2273-250 µg, ATGP2273-500 µg, ATGP2273-1 mg, ATGP2273-10, ATGP2273-20, ATGP2273-50, ATGP2273-100, ATGP2273-250, ATGP2273-500, ATGP2273-1

References & Citations

Feo S, Davies B, Fried M. et al. (Jun 1992) . Genomics 13 (1) : 201-207.

Storage Conditions

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Formulation

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 0.2M NaCl, 40% glycerol, 2mM DTT

Scientific Category

Epigenomics (Transcription & Translation)

NCBI Accession Number

NP_000980

Uniprot Accession Number

P62888

Species

Human

AA Sequence

MGSSHHHHHH SSGLVPRGSH MGSMVAAKKT KKSLESINSR LQLVMKSGKY VLGYKQTLKM IRQGKAKLVI LANNCPALRK SEIEYYAMLA KTGVHHYSGN NIELGTACGK YYRVCTLAII DPGDSDIIRS MPEQTGEK
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