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MABF288

Sigma-Aldrich

Anti-Roquin-1/2, clone 3F12 Antibody

clone 3F12, from rat

Synonyma:

Roquin-1, Roquin, RING finger and C3H zinc finger protein 1, RING finger and CCCH-type zinc finger domain-containing protein 1, RING finger protein 198

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rat

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

3F12, monoclonal

species reactivity

human, mouse

technique(s)

immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... RC3H1(149041)

General description

Roquin-1 shares 46% identity with Roquin-2 and both serve the same function and belong to the Zinc finger family of RNA binding proteins. Roquin-1/2 are cytoplasmic RNA suppression proteins that specifically bind selective RNAs and promote the deadenylation of mature mRNAs and their degradation. Roquin-1/2s targets include HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more critical RNAs. In particular, because of their impact on ICSO and gamma interferon and T helper cell activation, Roquin-1/2 are being examined as mediators of the systemic inflammation response and controllers of adaptive and innate immune responses in autoimmune disease. Roquin 1/2 are widely expressed and localized in the cytoplasm and/or P bodies and cytosolic stress granules when under cellular stress.

Specificity

This antibody specifically detects both Roquin-1 & Roquin-2 (Vogel, K.U., et al. (2013). Immunity. 38:655-668).

Immunogen

Recombinant protein corresponding to human Roquin-1/2.

Application

This Anti-Roquin-1/2, clone 3F12 Antibody is validated for use in Western Blotting and Immunoprecipitation for the detection of Roquin-1/2.
Western Blotting Analysis: A representative lot detected Roquin-1/2 in both Roquin-1 & Roquin-2 in normal MEFs, only Roquin-2 and Roquin-1 deficient MEFs, and neither protein in Roquin-1/2 deficient MEFs. This antibody also detected Roquin-1 and Roquin-2 in Mouse Spleen, Lymph Node, Thymus, Brain & Lung tissue, CD4+ T cells and Thymocyte lysates (Vogel, K.U., et al. (2013). Immunity. 38:655-668).
Immunoprecipitation Analysis: A representative lot immunoprecipitated Roquin-1/2 in MEF cell lysate (Vogel, K.U., et al. (2013). Immunity. 38:655-668).

Target description

125 kDa calculated

Physical form

Format: Purified

Other Notes

Concentration: Please refer to lot specific datasheet.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Navštívit knihovnu dokumentů

Johannes Braun et al.
Nucleic acids research, 46(22), 12109-12125 (2018-10-09)
Post-transcriptional gene regulation controls the amount of protein produced from a specific mRNA by altering both its decay and translation rates. Such regulation is primarily achieved by the interaction of trans-acting factors with cis-regulatory elements in the untranslated regions (UTRs)
Gregory J Connell et al.
RNA (New York, N.Y.), 29(8), 1117-1125 (2023-05-10)
The interactions of iron regulatory proteins (IRPs) with mRNAs containing an iron-responsive element (IRE) maintain cellular iron homeostasis and coordinate it with metabolism and possibly cellular behavior. The mRNA encoding transferrin receptor-1 (TFRC, TfR1), which is a major means of
Jaewoo Choi et al.
Cell cycle (Georgetown, Tex.), 17(18), 2243-2255 (2018-09-14)
Protein phosphorylation regulates a variety of cellular signaling pathways and fundamental mechanisms in cells. In this paper, we demonstrate that the mRNA decay factor Roquin2 is phosphorylated at tyrosine residue in position 691 in vivo. This phosphorylation disrupts the interaction
Jaewoo Choi et al.
Nature cell biology, 20(5), 586-596 (2018-04-27)
Kelch-like protein 6 (KLHL6) is an uncharacterized gene mutated in diffuse large B-cell lymphoma (DLBCL). Here we report that KLHL6 assembles with cullin3 to form a functional cullin-RING ubiquitin ligase. Mutations in KLHL6 inhibit its ligase activity by disrupting the

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