Recombinant Human Afamin His-tag Protein, CF Summary
Details of Functionality |
Measured by its ability to bind Biotinylated Recombinant Mouse Wnt-3a
(Catalog #
BT1324)
in a functional ELISA. The ED 50 for this effect is 0.8-6.4 µg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human Afamin protein Leu22-Asn599, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Leu22 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
67 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
71-80 kDa
|
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Afamin His-tag Protein, CF
Background
AFM (Afamin; also known as Alpha
-Albumin) is a secreted monomeric glycoprotein of the Alb/Albumin family of
molecules. It is expressed by hepatocytes (1), CNS endothelial cells (2)
and osteoclasts (3), and circulates in the blood at low μg/mL concentrations.
AFM is known to bind and transport vitamin E family molecules, playing an
important role for transporting at the blood-brain-barrier (2). It
also plays a role in maintaining solubility for transporting Wnt proteins (4, 5).
AFM also serves as an osteoclast-derived chemoattractant for preosteoblasts,
providing a rational for the observation that bone formation often follows bone
resorption (3). Mature human AFM is 578
amino acids (aa) in length (aa 22-599). It contains three consecutive albumin
domains (aa 36-206, aa 211-403 and aa 404-599) that contain a characteristic 5
or 6 intrachain disulfide bonds. Full-length human AFM shares 66% aa sequence
identity with mouse AFM and 67% aa sequence identity with rat AFM. The
importance of Afamin in transport of molecules has led to a suggested
diagnostic role in various diseases, including pre-eclampsia (6), ovarian
cancer (7), and both gestational and type-2 diabetes (8, 9).
- Liu, H. et al. (2011) DNA Cell Biol. 30:137.
- Kratzer, I. et al. (2009) J Neurochem. 108(3):707.
- Kim, B.J. et al. (2012) Bone. 51:431.
- Naschberger, A. et al. (2017) Structure. 25:1907.
- Mihara, E. et al. (2016) Elife. 5:11621.
- Köninger, A. et al. (2018) Arch Gynecol Obstet. 298(5):1009.
- Aktas B. et al. (2013). Anticancer Res. 33:329.
- Tramontana A. et al. (2018) Clin. Chim. Acta. 476:160.
- Kollerits, B. et al. (2017) Diabetes Care. 40:1386.
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