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Recombinant Human Afamin His-tag Protein, CF

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2 μg/lane of Recombinant Human Afamin (Catalog # 8065-AF) was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 71 - 80 kDa and ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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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 ED50 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
  • Bioactivity
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

  • Afamin
  • AFM
  • ALB2
  • ALB2alpha-Alb
  • ALBA
  • ALBAalpha-albumin
  • ALF
  • Alpha-Alb
  • Alpha-albumin
  • MGC125338
  • MGC125339

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).
  1. Liu, H. et al. (2011) DNA Cell Biol. 30:137.
  2. Kratzer, I. et al. (2009) J Neurochem. 108(3):707.
  3. Kim, B.J. et al. (2012) Bone. 51:431.
  4. Naschberger, A. et al. (2017) Structure. 25:1907.
  5. Mihara, E. et al. (2016) Elife. 5:11621.
  6. Köninger, A. et al. (2018) Arch Gynecol Obstet. 298(5):1009.
  7. Aktas B. et al. (2013). Anticancer Res. 33:329.
  8. Tramontana A. et al. (2018) Clin. Chim. Acta. 476:160.
  9. Kollerits, B. et al. (2017) Diabetes Care. 40:1386.

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