Recombinant Human ABCB6/PRP protein (ab127452)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% Purified via His tag
- Tags: His-DHFR tag N-Terminus
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant Human ABCB6/PRP protein -
Purity
> 95 % Purified via His tag.
Purity is >95% by SDS-PAGE. -
Expression system
Escherichia coli -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Predicted molecular weight
24 kDa -
Amino acids
598 to 818 -
Tags
His-DHFR tag N-Terminus
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab127452 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
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Form
Lyophilized -
Additional notes
This product was previously labelled as ABCB6
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at -20ºC.
Constituents: 0.32% Tris HCl, 0.58% Sodium chloride
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ReconstitutionReconstitute with water to desired concentration.
General Info
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Alternative names
- ABC
- ABC transporter umat
- ABC14
see all -
Function
Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis. -
Tissue specificity
Widely expressed. Highest expression in heart and skeletal muscles. -
Sequence similarities
Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily.
Contains 1 ABC transmembrane type-1 domain.
Contains 1 ABC transporter domain. -
Developmental stage
Highly expressed in fetal liver. -
Cellular localization
Mitochondrion outer membrane. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab127452 has not yet been referenced specifically in any publications.