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P0090

Sigma-Aldrich

Anti-PMP70−Atto 488 antibody produced in rabbit

1.5-3 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-70 kDa Peroxisonal membrane protein, Anti-ABCD3, Anti-PXMP1

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About This Item

MDL number:
MFCD01865555
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

Atto 488 conjugate

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

rat, mouse, human

packaging

antibody small pack of 25 μL

storage condition

protect from light

concentration

1.5-3 mg/mL

technique(s)

direct immunofluorescence: 10-20 μg/mL using human HeLa cells

UniProt accession no.

P28288

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ABCD3(5825)
mouse ... Abcd3(19299)
rat ... Abcd3(25270)

General description

70 kDa peroxisomal membrane protein (PMP70) belongs to the adrenoleukodystrophy (ALD) subfamily of the ATP-binding cassette (ABC) transporter superfamily. It is a half-size ABC integral membrane protein consisting of 6 transmembrane domains and one ATP-binding domain.
ATP-binding cassette sub-family D member 3 (ABCD3) is a peroxisomal membrane protein belonging to an ATP binding cassette family. The gene encoding it is localized on human chromosome 1p21-22 and rat chromosome 2q41.

Immunogen

synthetic peptide corresponding to amino acid residues 644-659 of rat PMP70 conjugated to KLH. The corresponding sequence is identical in mouse and differs by one amino acid in human.

Application

Atto 488 antibody produced in rabbit has been used in immunofluorescence.

Biochem/physiol Actions

70 kDa peroxisomal membrane protein (PMP70) forms a stable complex with the adrenoleukodystrophy protein, (ALDP), and several other peroxisomal proteins. ATP-binding/hydrolysis by PMP70 and ALDL and their phosphorylation are involved in the regulation of fatty acid transport into peroxisomes. Mutations in the PMP70 (PXMP1) gene may cause a subset of Zellweger syndrome-2, an autosomal recessive disorder that is manifested by a defective import mechanisms for peroxisomal matrix enzymes.
ATP-binding cassette sub-family D member 3 (ABCD3) is responsible for the transport of fatty acids into peroxisomes by an ATP-dependent mechanism. It also participates in the oxidation of dicarboxylic acids. Defects in the protein activity result in hepatosplenomegaly, a liver disease. Change in the expression of ABCD3 is associated with prostate tumor aggressiveness and a deficiency of the protein causes bile acid biosynthesis defect.

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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Breaking the Diffraction Barrier in Fluorescence Microscopy by Optical Shelving.
Bretschneider, S.; Eggeling, Chr.; Hell, S. W.
Physical Review Letters, 98(21) (2007)
Adenosine triphosphate binding cassette (ABC) transporters are expressed and regulated during terminal keratinocyte differentiation: a potential role for ABCA7 in epidermal lipid reorganization.
Kielar D
The Journal of Investigative Dermatology (2003)
RNAi-mediated silencing of ABCD3 gene expression in rat C6 glial cells: A model system to study PMP70 function
Rita Di
Neurochemistry International (2008)
Targeting elements in the amino-terminal part direct the human 70-kDa peroxisomal integral membrane protein (PMP70) to peroxisomes
Biermanns M and Gartner J
Biochemical and Biophysical Research Communications, 285(3), 649-655 (2001)
Kai Wen Teng et al.
eLife, 5 (2016-12-10)
Site-specific fluorescent labeling of proteins inside live mammalian cells has been achieved by employing Streptolysin O, a bacterial enzyme which forms temporary pores in the membrane and allows delivery of virtually any fluorescent probes, ranging from labeled IgG's to small
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