Detects human Afamin in direct ELISAs and Western blots. In direct ELISAs, approximately 40% cross-reactivity with recombinant mouse Afamin is observed, and less than 1% cross-reactivity with recombinant human (rh) AFB and rhAFP is observed.
Polyclonal Sheep IgG
Human embryonic kidney cell line HEK293-derived recombinant human Afamin Leu22-Asn599 Accession # P43652
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Human Afamin by Western Blot. Western blot shows human plasma. PVDF membrane was probed with 0.25 µg/mL of Sheep Anti-Human Afamin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF8065) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Afamin at approximately 87 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & 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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
AFM (Afamin; also alpha -Albumin) is a secreted monomeric glycoprotein member of the Alb/albumin family of molecules. Although its MW in SDS-Page ranges from 84-88 kDa, MALDI-TOF analysis yields a likely more correct value of 70-75 kDa. It is expressed by hepatocytes, CNS endothelial cells and osteoclasts, and circulates in the blood at low μg/mL concentrations. AFM is known to bind and transport vitamin E, particularly under conditions where lipoprotein is limited. This is likely to be important in follicular fluid and CSF. It also serves as an osteoclast-derived chemoattractant for preosteoblasts, providing a rational for the observation that bone formation often follows bone resorption. Mature human AFM is 578 amino acids (aa) in length (aa 22-599). It contains three consecutive albumin domains (aa 36-206, 211-403 and 404-599) that contain a characteristic 5 or 6 intrachain disulfide bonds. Full-length human AFM shares 67% aa sequence identity with mouse AFM.
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