Recombinant Human BMP-4 (E. coli-expressed) Protein, CF
Recombinant Human BMP-4 (E. coli-expressed) Protein, CF Summary
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 Acetonitrile and TFA.|
|Reconstitution||Reconstitute at 100 μg/mL in 4 mM HCl.|
|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.
Recombinant Human BMP-4 (E. coli-expressed) (Catalog # 314-BPE) induces alkaline phosphatase production in ATDC5 mouse chondrogenic cell line. The ED50 for this effect is 6-48 ng/mL.
2 μg/lane of Recombinant Human BMP-4(E. coli-expressed) (Catalog # 314-BPE) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing major bands at 9 kDa and 21 kDa, respectively.
Bone morphogenetic protein 4 (BMP-4) is a TGF-beta superfamily ligand that is widely expressed from early embryogenesis through adulthood. It plays an important role in mesenchyme formation, epidermal determination, suppression of neural induction, the development of multiple organs, and tissue repair (1-5). It is an integral part of many stem cell differentiation pathways, including lung tissue, (6), adipogenesis (7) and osteogenesis (8, 9). The human BMP-4 precursor contains a 273 amino acid (aa) propeptide and a 116 amino acid (aa) mature protein (10). Processing of the propeptide by furin or proprotein convertase 6 enables the formation of the mature disulfide-linked homodimeric BMP-4 and facilitates its secretion. Similar intracellular processes may lead to the formation and recreation of BMP4/BMP7 disulfide-linked heterodimer (11-13). Mature human and mouse BMP-4 share 98% aa sequence identity. Human BMP-4 shares 85% aa sequence identity with human BMP-2 and less than 50% with other human BMPs. In Xenopus, BMP-4 dimers provide ventralizing signals for existing mesoderm (14). BMP-4 signals through tetrameric complexes composed of type I (primarily Activin RIA or BMPR-IA) and type II (primarily Activin RIIA or BMPR-II) receptors (15, 16). The bioavailability of BMP-4 is regulated by its interaction with multiple proteins and glycosaminoglycans (17-19).
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