PODS® Human BMP-3
PODS® Technology
PODS® proteins are made using an insect cell expression system in which the active protein is co-expressed alongside polyhedrin carrier protein. Polyhedrin forms microcrystals within insect cells which specifically capture the active protein to form a co-crystal complex. The active protein is captured in its nascent, natively folded form with limited scope for proteolytic degradation. Consequently, excellent levels of bioactivity are observed. The PODS® co-crystals provide a sustained release mechanism and can be used to functionalize surfaces. For further details, please refer to the PODS® Technology page.Product Description
The product contains the polyhedrin protein co-crystalized with Human BMP-3. BMP-3, also known as Bone Morphogenetic Protein 3 or osteogenin, is a member of the TGF superfamily of proteins. Akin to the other functionally and structurally related bone morphogenic proteins (BMPs), BMP-3 is involved in cartilage and bone formation. However, unlike most other BMPs, BMP-3 negatively regulates bone density by antagonizing the ability of osteogenic BMPs, such as BMP-2, to induce osteoprogenitor differentiation and ossification. It has been suggested that this inhibitory effect could be through an Activin signalling pathway rather than direct competition with osteogenic BMPs. The BMP-3 protein is a disulfide-linked homodimer and highly conserved across animal species; for example, the amino acid sequence of human and rat BMP-3 are 98% identical. BMP-3 is frequently expressed in adult and foetal cartilage.Usage Recommendation
PODS® co-crystals provide a depot of proteins which are steadily secreted. It has been estimated that the biological activity of 50 million PODS® co-crystals generates the same peak dose as 3.3 µg of standard recombinant protein. However, at 5 days following the start of seeding the PODS® co-crystals, there are more than 50% of these peak levels still present in the culture system. Ultimately, the amount of PODS® co-crystals that is optimal for a particular experiment should be determined empirically. Based on previous data, we suggest using 50 million PODS® co-crystals in place of 3.3 µg of standard growth factor as a starting point."
To control for cross-reactivity with cells or as a negative control, we recommend using PODS® growth factors alongside PODS® Empty crystals, as the latter do not contain or release cargo protein.
Animal-Free
This product is produced with no animal derived raw products. All processing and handling employs animal free equipment and animal free protocols.AA Sequence
MADVAGTSNRDFRGREQRLFNSEQYNYNNSKNSRPSTSLYKKAGFQWIEPRNCARRYLKVDFADIGWSEWIISPKSFDAYYCSGACQFPMPKSLKPSNHATIQSIVRAVGVVPGIPEPCCVPEKMSSLSILFFDENKNVVLKVYPNMTVESCACR*Alternative Names
BMP3, BMP3A, BMP-3A, Bone Morphogenetic Protein 3, Bone Morphogenetic Protein 3A, OsteogeninResearch Use Only
This product is for Research Use Only.| Product Details | |
|---|---|
| Length | 111 aa |
| Molecular Weight | 35.2 kDa |
| Structure | Dimer |
| Source | Spodoptera frugiperda (Sf9) cell culture |
| Accession Number | P12645 |
| Endotoxin Level | <0.06 EU/ml as measured by gel clot LAL assay |
| Formulation | PODS® were lyophilized from a volatile solution |
| Reconstitution |
PODS® co-crystals may be reconstituted at 200 million co-crystals/ml in sterile PBS. 20% glucose has a buoyant density closer to PODS® co-crystals and can be useful for aliquoting. PODS® co-crystals are highly stable when stored in aqueous solution (pH range 6 - 8). |
| Stability and Storage | Upon receipt, store at 4°C. PODS® co-crystals are stable for at least 1 year when dry and 6 months when resuspended. |
References
Fasséli Coulibaly, Elaine Chiu, Keiko Ikeda, Sascha Gutmann, Peter W. Haebel, Clemens Schulze-Briese, Hajime Mori, and Peter Metcalf. The molecular organization of cypovirus polyhedra. (2007) Nature. 446: 97-101.
Rey FA. Virology: Holed up in a natural crystal. (2007) Nature. 446: 35-37.
Mori H. Immobilization of Bioactive Growth Factors into Cubic Proteinous Microcrystals (Cypovirus Polyhedra) and Control of Cell Proliferation and Differentiation. (2010) NSTI-Nanotech. 3: 222-225.
Satoshi Abe, Hiroshi Ijiri, Hashiru Negishi, Hiroyuki Yamanaka, Katsuhito Sasaki, Kunio Hirata, Hajime Mori, and Takafumi Ueno. Design of Enzyme-Encapsulated Protein Containers by In-Vivo Crystal Engineering. (2015) Advanced Materials. 27(48): 7951-7956.
