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AB60068

Anti-FTSJ2抗体[2372C6a]

Anti-FTSJ2 antibody [2372C6a]

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(3 Publications)

Mouse Monoclonal FTSJ2 antibody. Suitable for WB and reacts with Recombinant full length protein - Human samples. Cited in 3 publications. Immunogen corresponding to Recombinant Fragment Protein within Human MRM2.

查看别名

FJH1, FTSJ2, MRM2, 16S rRNA (uridine(1369)-2'-O)-methyltransferase, 16S rRNA [Um1369] 2'-O-methyltransferase, Protein ftsJ homolog 2

1 Images
Western blot - Anti-FTSJ2 antibody [2372C6a] (AB60068)
  • WB

Unknown

Western blot - Anti-FTSJ2 antibody [2372C6a] (AB60068)

Western blot analysis of immunized recombinant protein, using ab60068.

All lanes:

Western blot - Anti-FTSJ2 antibody [2372C6a] (ab60068)

Predicted band size: 27 kDa

Observed band size: 33 kDa

false

关键信息

宿主种属

Mouse

克隆

Monoclonal

克隆号

2372C6a

亚型

IgG1

不含载体蛋白

No

应用

WB

applications

免疫原

Recombinant Fragment Protein within Human MRM2. The exact immunogen used to generate this antibody is proprietary information.

Q9UI43

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反应性数据

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Recombinant full length protein - Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" } } }
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性能和储存信息

形式
Liquid
纯化工艺
Affinity purification Protein G
纯化说明
Purified using protein G column chromatography, from culture supernatant of hybridoma cultured in a medium containing bovine IgG-depleted (approximately 95%) fetal bovine serum.
存储溶液
pH: 7.4 Preservative: 0.05% Sodium azide Constituents: PBS, 1% BSA, 0.812% Sodium chloride, 0.1312% Sodium phosphate, 0.03% Tripotassium orthophosphate, 0.0225% Potassium chloride
运输条件
Blue Ice
推荐的短期储存条件
+4°C
推荐的长期储存条件
-20°C
分装信息
Upon delivery aliquot
储存信息
Avoid freeze / thaw cycle
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补充信息

This supplementary information is collated from multiple sources and compiled automatically.

FTSJ2 also known as hPrmA or methyltransferase-like protein 1 is an enzyme with a mass of approximately 83 kDa. It functions as a human 2'-O-methyltransferase and takes part in ribosomal RNA modification by methylating the ribose moiety in RNA molecules. You can find FTSJ2 widely expressed in various human tissues with notable expression in the liver and brain. The enzyme localizes mainly in the nucleolus a site central to ribosomal RNA biosynthesis and modification activities.
Biological function summary

The enzymatic activities of FTSJ2 contribute to ribosome assembly and stability by modifying specific rRNA components. These modifications are essential for the accurate assembly of ribosomal subunits and the proper function of the translation machinery within the cell. FTSJ2 does not function in isolation; it often operates as part of multiprotein complexes which assist in guiding and regulating its methyltransferase activity.

Pathways

Methylation activity by FTSJ2 plays a critical role in the RNA processing pathway and cellular translation machinery. It directly affects the biogenesis of rRNA ensuring the efficient assembly of ribosomal units required for protein synthesis. FTSJ2 interacts with other proteins such as NOP10 and NOP56 which are potentials linking it to the broader ribonucleoprotein complex within cells.

Alterations in FTSJ2 activity and expression have connections to several human conditions notably cancer and neurological disorders. Aberrations in the rRNA modification process could lead to disruptions in protein synthesis and uncontrolled cell proliferation which are often observed in cancerous cells. In the context of neurological disorders FTSJ2's function links to proteins like FBL which play key roles in neural cell RNA processing. Changes in their function could potentially contribute to neurodegenerative conditions.
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产品实验方案

For this product, it's our understanding that no specific protocols are required. You can visit:
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靶点信息

S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA (PubMed : 25009282, PubMed : 25074936, PubMed : 35177605). This activity may require prior 2'-O-methylguanosine modification at position 1370 (Gm1370) by MRM3 (PubMed : 35177605). Essential for late-stage assembly of mtLSU required for efficient translation of mitochondrial DNA encoded proteins; methyltransferase activity is not required for this function (PubMed : 35177605). Essential for mitochondrial respiratory function (PubMed : 35177605).
See full target information MRM2
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文献 (3)

Recent publications for all applications. Explore the full list and refine your search

Human molecular genetics 26:4257-4266 PubMed28973171

2017

Defective mitochondrial rRNA methyltransferase MRM2 causes MELAS-like clinical syndrome.

Applications

Unspecified application

Species

Unspecified reactive species

Caterina Garone,Aaron R D'Souza,Cristina Dallabona,Tiziana Lodi,Pedro Rebelo-Guiomar,Joanna Rorbach,Maria Alice Donati,Elena Procopio,Martino Montomoli,Renzo Guerrini,Massimo Zeviani,Sarah E Calvo,Vamsi K Mootha,Salvatore DiMauro,Ileana Ferrero,Michal Minczuk

The Journal of biological chemistry 289:24936-42 PubMed25074936

2014

Assignment of 2'-O-methyltransferases to modification sites on the mammalian mitochondrial large subunit 16 S ribosomal RNA (rRNA).

Applications

Unspecified application

Species

Human

Ken-Wing Lee,Daniel F Bogenhagen

The Journal of biological chemistry 288:31386-99 PubMed24036117

2013

Mitochondrial ribosomal RNA (rRNA) methyltransferase family members are positioned to modify nascent rRNA in foci near the mitochondrial DNA nucleoid.

Applications

WB

Species

Unspecified reactive species

Ken-Wing Lee,Cynthia Okot-Kotber,Joseph F LaComb,Daniel F Bogenhagen
View all publications
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