Product Description

MRPS5 Polyclonal Antibody

Sizes: 50µl, 100µl

Catalogue Numbers: BS65204-50, BS65204-100

Product: Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Swiss-Prot: P82675

Host: Rabbit

Reactivity: Human

Applications: IHC-p, IF (paraffin section), ELISA

All Applications: Immunohistochemistry: 1/100 - 1/300. ELISA: 1/40000. Not yet tested in other applications.

Background: mitochondrial ribosomal protein S5(MRPS5) Homo sapiens Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that belongs to the ribosomal protein S5P family. Pseudogenes corresponding to this gene are found on chromosomes 4q, 5q, and 18q. [provided by RefSeq, Jul 2008],

Purification and Purity: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Storage and Stability: -20°C/1 year

Note: For research use only, not for use in diagnostic procedure.

Extra Notes: Immunohistochemistry analysis of paraffin-embedded human testis, using MRPS5 Antibody. The picture on the right is blocked with the synthesized peptide.

Specificity: MRP-S5 Polyclonal Antibody detects endogenous levels of MRP-S5 protein.

Alternative Name: MRPS5; 28S ribosomal protein S5; mitochondrial; MRP-S5; S5mt

Immunogen: The antiserum was produced against synthesized peptide derived from human MRPS5. AA range:367-416

Conjugate: Unconjugated

Modification: Unmodified