Recombinant Human Afamin His-tag Protein, CF Summary
Product Specifications
Leu22-Asn599, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
8065-AF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Scientific Data
2 μg/lane of Recombinant Human Afamin (Catalog # 8065-AF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 71 - 80 kDa and 55 - 70 kDa, respectively.
Reconstitution Calculator
Background: Afamin
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.
Citation for Recombinant Human Afamin His-tag Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
-
Protective effect of afamin protein against oxidative stress related injury in human ovarian granulosa cells
Authors: Zhang, Q;Zheng, X;Zhang, X;Zheng, L;
Journal of ovarian research
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
FAQs
No product specific FAQs exist for this product, however you may
View all Proteins and Enzyme FAQsReviews for Recombinant Human Afamin His-tag Protein, CF
Average Rating: 5 (Based on 2 Reviews)
Have you used Recombinant Human Afamin His-tag Protein, CF?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image
Filter by:
Afamin promote lung organoid growth