Recombinant Human Fibrillin-1/FBN1 Fc Chimera Protein, CF Summary
|Human Fibrillin-1 |
Accession # P35555
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|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.
When Recombinant Human MFAP4 (Catalog # 10230-MF) is coated at 0.5 µg/mL, 100 µL/well, Recombinant Human Fibrillin-1/FBN1 Fc Chimera (Catalog # 10224-FI) binds with an ED50 of 0.1-0.6 µg/mL.
1 μg/lane of Recombinant Human Fibrillin-1/FBN1 Fc Chimera (Catalog # 10224-FI) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 97-108 kDa and 190-220 kDa, respectively.
Fibrillins are glycoproteins forming the backbone of microfibrils in elastic and non-elastic tissues. They interact with other components of the extracellular matrix (ECM) and play essential roles in tissue development, homeostasis and repair. Fibrillin-1 is a calcium-binding protein that assembles to form the structural component of the 10-12 nm microfibrils of the ECM. The human Fibrillin-1 has multiple domains, primarily consisting of epidermal growth factor (EGF)-like and other modules (1, 2). The calcium-binding modules in some of the EGF domains provide structural stability and the characteristic rod-like shape of the protein (3-8). Mature human Fibrillin-1 shares 97% amino acid (aa) sequence identity with mature mouse Fibrillin-1. Human Fibrillin-1 is synthesized as an approximately 350-kDa precursor molecule, which is then proteolytically processed by furin into its biologically active form (9-10). Fibrillin microfibers are further engaged in a number of cell matrix interactions such as with integrins, bone morphogenetic proteins (BMPs) and the large latent complex of transforming growth factor-beta (11). Fibrillin-1 mutations are associated with a range of heritable connective disorders, including Marfan syndrome and acromelic dysplasias (11-12).
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