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Key Documents

SAB4200206

Sigma-Aldrich

Anti-TRIM2 antibody produced in rabbit

enhanced validation

~1.5 mg/mL

Sinonimo/i:

Anti-RING finger protein 86, Anti-RNF86, Anti-Tripartite motif-containing protein 2

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

PM

antigen ~85 kDa

Reattività contro le specie

human, rat

Convalida avanzata

recombinant expression
Learn more about Antibody Enhanced Validation

Concentrazione

~1.5 mg/mL

tecniche

western blot: 1.5-3.0 μg/mL using rat spinal cord extracts (S1 fraction) and HEK-293T cell lysates over expressing human TRIM2.

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... TRIM2(23321)
mouse ... Trim2(80890)
rat ... Trim2(361970)

Descrizione generale

Tripartite motif containing 2 (TRIM2) is an E3 ubiquitin ligase, encoded by the gene mapped to human chromosome 4q31.3. The encoded protein belongs to the TRIM– NCL-1, HT2A and Lin-41 (NHL) protein family. This 81kDa protein is characterized with an N-terminal really interesting new gene (RING) finger domain and a B-box domain, a middle coiled-coil domain and a C-terminal NHL domain.
Tripartite motif-containing protein 2 (TRIM2), also known as RNF86, Narf is highly expressed in the nervous system.

Applicazioni

Anti-TRIM2 antibody produced in rabbit has been used in western blot analysis.
Anti-TRIM2 antibody produced in rabbit in immunoblotting and western blotting.

Azioni biochim/fisiol

Tripartite motif containing 2 (TRIM2) ubiquitinates neurofilament light chain, B-cell lymphoma 2 (Bcl-2)-interacting mediator and motor protein myosin V. It has a role in polarization of neurons and outgrowth of axons. Loss of function of the protein has been linked to early-onset axonal neuropathy.
Tripartite motif-containing protein (TRIM) RING finger proteins play an important role in cancerogenesis and in defense against viral infection. Mutations in the RING finger protein Parkin is associated with Parkinson′s disease (PD), and translocation of the TRIM gene is linked to acute promyelocytic leukemia. TRIM2 plays an important role in regulating neurofilament (NF-L) metabolism.

Stato fisico

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

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Deficiency of the E3 ubiquitin ligase TRIM2 in early-onset axonal neuropathy
Ylikallio E
Human Molecular Genetics, 22, 2975-2983 (2013)
Deficiency of the E3 ubiquitin ligase TRIM2 in early-onset axonal neuropathy
Ylikallio E, et al.
Human Molecular Genetics, 22(15), 2975-2983 (2013)
Emil Ylikallio et al.
Human molecular genetics, 22(15), 2975-2983 (2013-04-09)
Inherited peripheral neuropathies are a heterogeneous group of disorders that can affect patients of all ages. Children with inherited neuropathy often develop severe disability, but the genetic causes of recessive early-onset axonal neuropathies are not fully known. We have taken
Molecular cloning and characterization of neural activity-related RING finger protein (NARF): a new member of the RBCC family is a candidate for the partner of myosin V
Ohkawa N, et al.
Journal of Neurochemistry, 78(1), 75-87 (2001)
TRIM2, a novel member of the antiviral family, limits New World arenavirus entry
Sarute N, et al.
PLoS Biology, 17(2), e3000137-e3000137 (2019)

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