PODS® Human Activin B

Code Description Price Qty
PPH307-50 PODS® Human Activin B, 50 million £100.00
PPH307-250 PODS® Human Activin B, 250 million £305.00
PPH307-1000 PODS® Human Activin B, 1 billion £1,025.00
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 Human Activin B. Activin B is a member of the TGF-β superfamily, which are disulfide-linked dimeric proteins that were originally purified from gonadal fluids and had as primary role to stimulate the release of pituitary follicle stimulating hormones (FSH). Activin B has shown to have a wide range of biological activities including: mesoderm induction, neural cell differentiation, bone remodeling, hematopoiesis, reproductive physiology, and hormone secretion from the hypothalamic, pituitary and gonadal glands. Activins exert their biological activities through binding to the heterodimeric complex composed of two membrane spanning serine-threonine kinases designated as type I and type II. Two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B) have been identified. Activin B signals through the ActRII receptor (Activin Receptor type II).

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 KKAGFGLECD GRTNLCCRQQ FFIDFRLIGW NDWIIAPTGY YGNYCEGSCP AYLAGVPGSA SSFHTAVVNQ YRMRGLNPGT VNSCCIPTKL STMSMLYFDD EYNIVKRDVP NMIVEECGCA

Alternative Names

Inhibin beta-2, Activin-B, INHBB, Inhibin Beta B, Inhibin Beta-2

Research Use Only

PODS® Limited Use Label License. A license applies for this product, please see Product User Guide below for details.
Product Details
Length 160 aa
Molecular Weight 36 kDa
Structure Dimer
Source Spodoptera frugiperda (Sf9) cell culture
Accession Number Q53T31
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.