PODS® Human Ephrin-A3
PODS® TechnologyPODS® 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 DescriptionThe product contains the polyhedrin protein co-crystalized with Human Ephrin-A3. Ephrin-A3 is a member of Ephrin-A famil, and it is also known as EHK1-L, EFL-2, and LERK-3. Ephrin-A ligands are structurally related to the extracellular domains of the transmembrane Ephrin-B ligands. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. Ephrin‑A3 expression can be up‑ or down‑regulated by hypoxia in the hippocampus or vascular endothelial cells, respectively. Ephrin-A3 interaction with EphA receptors induces neurite growth cone collapse and the repulsion of migrating axons, which is important for the accurate migration of axons during CNS development.
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-FreeThis product is produced with no animal derived raw products. All processing and handling employs animal free equipment and animal free protocols.
AA SequenceMADVAGTSNR DFRGREQRLF NSEQYNYNNS KNSRPSTSLY KKAGFNRHAV YWNSSNQHLR REGYTVQVNV NDYLDIYCPH YNSSGVGPGA GPGPGGGAEQ YVLYMVSRNG YRTCNASQGF KRWECNRPHA PHSPIKFSEK FQRYSAFSLG YEFHAGHEYY YISTPTHNLH WKCLRMKVFV CCASTSHSGE KPVPTLPQFT MGPNVKINVL EDFEGENPQV PKLEKSISGT SPKREHLPLA VGIAFFLMTF LAS
Alternative NamesEphrinA3, EFL2, EFL-2, EFNA3, Ehk1-L, EPH-related receptor tyrosine kinase ligand 3, EPLG3EHK1 ligand, LERK-3, LERK3, ligand of eph-related kinase 3
Research Use OnlyThis product is for Research Use Only.
|Molecular Weight||28.7 kDa|
|Source||Spodoptera frugiperda (Sf9) cell culture|
|Endotoxin Level||<0.06 EU/ml as measured by gel clot LAL assay|
|Formulation||PODS® were lyophilized from a volatile solution|
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.|
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.