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R0780

Sigma-Aldrich

Anti-Ribosomal Protein L26 (C-terminal) antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-RPL26

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About This Item

MDL number:
UNSPSC Code:
12352203

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

17 kDa

species reactivity

rat, human, mouse

concentration

~1 mg/mL

technique(s)

immunoprecipitation (IP): 10-20 μg using HEK-293T cell lysates
western blot: 0.5-1 μg/mL using HEK-293T cell extracts

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... RPL26(6154)
mouse ... Rpl26(19941)
rat ... Rpl26l1(307636)

Immunogen

synthetic peptide corresponding to amino acids 129-145 of human ribosomal protein L26, conjugated to KLH via an N-terminal added cysteine residue. The sequence is conserved in human, rat, and mouse.

Target description

Ribosomal Protein L26 (C-terminal) encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L24P family of ribosomal proteins.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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


Certificates of Analysis (COA)

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Ning Dai et al.
Genes & development, 27(3), 301-312 (2013-02-08)
Lack of IGF2 in mice results in diminished embryonic growth due to diminished cell proliferation. Here we show that mouse embryonic fibroblasts lacking the RNA-binding protein IMP1 (IGF2 mRNA-binding protein 1) have defective splicing and translation of IGF2 mRNAs, markedly
Ulrike Schumann et al.
BMC biology, 18(1), 40-40 (2020-04-16)
5-Methylcytosine (m5C) is a prevalent base modification in tRNA and rRNA but it also occurs more broadly in the transcriptome, including in mRNA, where it serves incompletely understood molecular functions. In pursuit of potential links of m5C with mRNA translation

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