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SAB3500987

Sigma-Aldrich

Anti-TOM70 antibody produced in rabbit

affinity isolated antibody

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

mouse, human, rat

concentration

1 mg/mL

technique(s)

ELISA: suitable
immunoblotting: suitable
immunofluorescence: suitable
immunohistochemistry: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... TOMM70A(9868)

Immunogen

Antibody was raised against a 15 amino acid synthetic peptide near the center of human TOM70.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Linkage

The action of this antibody can be blocked using blocking peptide SBP3500987.

Physical form

Supplied at 1 mg/mL in PBS with 0.02% sodim 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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Certificates of Analysis (COA)

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Stephan Kutik et al.
The Journal of cell biology, 179(4), 585-591 (2007-11-14)
Most mitochondrial proteins are synthesized in the cytosol and imported into one of the four mitochondrial compartments: outer membrane, intermembrane space, inner membrane, and matrix. Each compartment contains protein complexes that interact with precursor proteins and promote their transport. These
Jason C Young et al.
Cell, 112(1), 41-50 (2003-01-16)
The role of cytosolic factors in protein targeting to mitochondria is poorly understood. Here, we show that in mammals, the cytosolic chaperones Hsp90 and Hsp70 dock onto a specialized TPR domain in the import receptor Tom70 at the outer mitochondrial
Sven Geisler et al.
Journal of cell science, 127(Pt 15), 3280-3293 (2014-06-08)
Depolarized mitochondria are degraded by mitophagy in a process that depends on the Parkinson's disease gene products PINK1 and Parkin. This is accompanied by ubiquitylation of several mitochondrial substrates. The roles of E2 ubiquitin-conjugating enzymes (UBE2) in mitophagy are poorly

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