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Key Documents

AV48473

Sigma-Aldrich

Anti-MTR antibody produced in rabbit

affinity isolated antibody

Synonyme(s) :

Mtr Antibody, Mtr Antibody - Anti-MTR antibody produced in rabbit, Anti-5-Methyltetrahydrofolate-homocysteine methyltransferase, Anti-FLJ45386

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

140 kDa

Espèces réactives

rat, guinea pig, mouse, horse, human, rabbit, bovine

Concentration

0.5 mg - 1 mg/mL

Technique(s)

western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... MTR(4548)

Description générale

MTR codes for 5-methyltetrahydrofolate-homocysteine methyltransferase that catalyzes the last step in methionine synthesis. Genetic alterations in MTR have been associated with methylcobalamin deficiency, breast cancer risk and prostate cancer susceptibility.
Rabbit Anti-MTR antibody recognizes chicken, human, mouse, rat, and bovine MTR.

Immunogène

Synthetic peptide directed towards the C terminal region of human MTR

Application

Rabbit Anti-MTR antibody is suitable for western blot applications at a concentration of 1μg/ml.

Actions biochimiques/physiologiques

MTR is the enzyme 5-methyltetrahydrofolate-homocysteine methyltransferase. This enzyme, also known as cobalamin-dependent methionine synthase, catalyzes the final step in methionine biosynthesis. Mutations in MTR have been identified as the underlying cause of methylcobalamin deficiency complementation group G. MTR encodes the enzyme 5-methyltetrahydrofolate-homocysteine methyltransferase. This enzyme, also known as cobalamin-dependent methionine synthase, catalyzes the final step in methionine biosynthesis. Mutations in MTR have been identified as the underlying cause of methylcobalamin deficiency complementation group G. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. The extent of this transcript is supported by transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Séquence

Synthetic peptide located within the following region: GSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTGIRL

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Andrés López-Cortés et al.
The American journal of the medical sciences, 346(6), 447-454 (2013-03-06)
The methylenetetrahydrofolate reductase (MTHFR), methionine synthase (MTR) and MTR reductase (MTRR) enzymes act in the folate metabolism, which is essential in methylation and synthesis of nucleic acids. The single nucleotide polymorphisms, MTHFR C677T, A1298C, MTR A2756G and MTRR A66G, cause
Rita de Cássia Carvalho Barbosa et al.
Anticancer research, 32(11), 4805-4811 (2012-11-17)
Polymorphisms in genes encoding enzymes of folate metabolism are a focus of breast cancer risk studies due of the role of these enzymes in DNA methylation, synthesis, and repair. MTHFR, encoding for 5,10-methylenetetrahydrofolate reductase, is one of the most studied

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