PODS™ Mouse Ephrin-B2

Code Description Price Qty
PPM301-50 PODS™ Mouse Ephrin-B2, 50 million £95.00
PPM301-250 PODS™ Mouse Ephrin-B2, 250 million £295.00
PPM301-1000 PODS™ Mouse Ephrin-B2, 1 billion £995.00
PODS™ co-crystals
PODS™ co-crystals

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 Mouse Ephrin-B2. Ephrin-B2 is a member of Ephrin-B family. Mouse Ephrin-B2 shares 97% identity with human Ephrin-B2. Ephrin-B proteins are involved in cell migration, tissue morphogenesis and cancer progression.

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.

AA Sequence

MADVAGTSNR DFRGREQRLF NSEQYNYNNS KNSRPSTSLY KKAGLMVIIV LEPIYWNSSN SKFLPGQGLV LYPQIGDKLD IICPKVDSKT VGQYEYYKVY MVDKDQADRC TIKKENTPLL NCARPDQDVK FTIKFQEFSP NLWGLEFQKN KDYYIISTSN GSLEGLDNQE GGVCQTRAMK ILMKVGQDAS SAGSARNHGP TRRPELEAGT NGRSSTTSPF VKPNPGSSTD GNSAGHSGNN LLGSE

Alternative Names

EphrinB2, EphB2, ephrin, Htk-L, ELF-2, LERK-5, NLERK-1
Product Details
Length 245 aa
Molecular Weight 27 kDa
Structure Monomer
Source Spodoptera frugiperda (Sf9) cell culture
Accession Number NP_034241.2
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 water. 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.