Human Hemopexin protein fragment (ab91693)
- Product nameHuman Hemopexin protein fragmentSee all Hemopexin proteins and peptides ...
- SourceE. coli
- Amino Acid Sequence
- SequenceFFQGDREWFWDLATGTMKERSWPAVGNCSSALRWLGRYYC FQGNQFLRFDPVRGE VPPRYPRDVRDYFMPCPGRGHGH RNGTGHGNSTHHGPEYMRCSPHLVLSALTSDN HGATYA FSGTHYWRLDTSRDGWHSWPIAHQWPQGPSAVDAAFSWEE KLYLVQGTQ VYVFLTKGGYTLVSGYPKRLEKEVGTPHG IILDSVDAAFICPGSSRLHIMAGRRL WWLDLKSGAQAT WTELPWPHEKVDGALCMEKSLGPNSCSANGPGLYLIHGPN LYC YSDVEKLNAAKALPQPQNVTSLLGCTH (Ami no acid sequence (Sequence determined by 5' Sequencing))
- Amino acids161 to 462
Our Abpromise guarantee covers the use of ab91693 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
- Additional NotesProtein Identity confirmed by Mass Spectrometry (MS/MS) (acquired on initial reference batch)
- Concentration information loading...
Preparation and Storage
- Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.5% Trehalose, 6M Urea, 100mM Sodium hydrogen phosphate, 10mM Sodium chloride, pH 4.5
- ReconstitutionReconstitute with 64 µl aqua dest.
- Beta 1B glycoprotein
- FunctionBinds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.
- Tissue specificityExpressed by the liver and secreted in plasma.
- Sequence similaritiesBelongs to the hemopexin family.
Contains 5 hemopexin-like domains.
modificationsN- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.
- Cellular localizationSecreted.
Human Hemopexin protein fragment images
The image shows an electrophoretic assay performed using an Agilent 5100 ALP. In some images coloured control bands can be seen at 15 kDa (green) and/or 240 kDa (purple). The protein-specific band is blue.
References for Human Hemopexin protein fragment (ab91693)
ab91693 has not yet been referenced specifically in any publications.