Transferrin in Mouse Thymus.
Transferrin was detected in perfusion fixed frozen sections of mouse thymus using Goat Anti-Mouse Transferrin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3987) at 5 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to the plasma membranes of lymphocytes. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
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.
Transferrin (also serotransferrin and siderophilin) is a secreted, monomeric 78-82 kDa glycoprotein member of the transferrin family of molecules. It is synthesized by hepatocytes and serves as a transport vehicle for ferric iron, as well as cobalt and manganese ions. When bound to iron, transferrin is referred to as holo-transferrin (Greek: holo - meaning whole or together). When it is absent iron, it is called apotransferrin (Greek: apo - meaning away or apart). Apotransferrin encounters and binds two ferric iron atoms at the basolateral surface of duodenal epithelium. Here, as holo-transferrin, it circulates and distributes iron to virtually all tissues by binding to transferrin receptor 1. Once bound, holo-transferrin is internalized, iron is released, and the resulting apotransferrin is recylced. Mature mouse apotransferrin is 678 amino acids (aa) in length. It is bilobar in shape, with 330 aa N- and C-terminal lobes that each bind one ferric atom. In the absence of iron, each lobe is "open"; when iron is present, the lobes close, forming a compact structure. Mature mouse apotransferrin is 72% and 88% aa identical to human and rat apotransferrin, respectively.
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