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SAB4200206

Sigma-Aldrich

Anti-TRIM2 antibody produced in rabbit

enhanced validation

~1.5 mg/mL

Synonym(s):

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

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~85 kDa

species reactivity

human, rat

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

concentration

~1.5 mg/mL

technique(s)

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

UniProt accession no.

Q9C040

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Application

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

Biochem/physiol Actions

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.

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

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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RING finger 1 mutations in Parkin produce altered localization of the protein
Cookson MR, et al.
Human Molecular Genetics, 12(22), 2957-2965 (2003)
TRIM2, a novel member of the antiviral family, limits New World arenavirus entry
Sarute N, et al.
PLoS Biology, 17(2), e3000137-e3000137 (2019)
Exome sequencing reveals homozygous TRIM2 mutation in a patient with early onset CMT and bilateral vocal cord paralysis.
Pehlivan D
Human Genetics, 34, 671-673 (2015)
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
Deficiency of the E3 ubiquitin ligase TRIM2 in early-onset axonal neuropathy
Ylikallio E, et al.
Human Molecular Genetics, 22(15), 2975-2983 (2013)
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