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Merck
CN

AV46301

Sigma-Aldrich

Anti-MRPS12 antibody produced in rabbit

affinity isolated antibody

Synonym(s):

Anti-MPR-S12, Anti-MT-RPS12, Anti-Mitochondrial ribosomal protein S12, Anti-RPMS12, Anti-RPS12, Anti-RPSM12

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41
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biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

12 kDa

species reactivity

human

concentration

0.5 mg - 1 mg/mL

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... MRPS12(6183)

General description

Mitochondrial ribosomal protein S12 (MRPS12), which is similar to bacterial ribosomal protein S12, is a eucaryote nucleus-encoded mitoribosomal component of mitochondrial translational apparatus that is translated on mitochondrial ribosomes.

Immunogen

Synthetic peptide directed towards the N terminal region of human MRPS12

Application

Anti-MRPS12 polyclonal antibody is used to tag mitochondrial ribosomal protein S12 for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of mitochondrial ribosomal protein S12 in mitochondrial ribosome structure and protein synthesis.

Biochem/physiol Actions

Anti-MRPS12 polyclonal antibody reacts with canine, human, rat, and bovine mitochondrial ribosomal protein S12 proteins.
Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS12 is the 28S subunit protein that belongs to the ribosomal protein S12P family. The protein is a key component of the ribosomal small subunit and controls the decoding fidelity and susceptibility to aminoglycoside antibiotics.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 S12P family. The encoded protein is a key component of the ribosomal small subunit and controls the decoding fidelity and susceptibility to aminoglycoside antibiotics. The gene for mitochondrial seryl-tRNA synthetase is located upstream and adjacent to this gene, and both genes are possible candidates for the autosomal dominant deafness gene (DFNA4). Splice variants that differ in the 5′ UTR have been found for this gene; all three variants encode the same protein.

Physical form

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Other Notes

Synthetic peptide located within the following region: LVPRLWATCSMATLNQMHRLGPPKRPPRKLGPTEGRPQLKGVVLCTFTRK

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Sonia Emperador et al.
Frontiers in genetics, 5, 469-469 (2015-02-03)
Several homoplasmic pathologic mutations in mitochondrial DNA, such as those causing Leber hereditary optic neuropathy or non-syndromic hearing loss, show incomplete penetrance. Therefore, other elements must modify their pathogenicity. Discovery of these modifying factors is not an easy task because

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