PODS® Mouse Activin A

Code Description Price Qty
PPM29-50 PODS® Mouse Activin A, 50 million $170.00
PPM29-250 PODS® Mouse Activin A, 250 million $490.00
PPM29-1000 PODS® Mouse Activin A, 1 billion $1,630.00
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 Activin A. Activin A is a member of the Transforming Growth Factor beta (TGF-β) family of proteins with a wide range of biological activities. Activins are produced in many tissue types including the skin, gonads, lungs, and pituitary gland. Activins interact with receptor type I and type II serine/threonine protein kinases, to activate SMAD signaling and regulate diverse cellular functions, such as cell proliferation, differentiation, wound healing, apoptosis, and metabolism. Activin A is a homodimer comprised of two activin beta A chains. Mouse Activin A shares 100% amino acid sequence identity with human, rat, porcine, bovine, and feline Activin A proteins.

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

MADVAGTSNR DFRGREQRLF NSEQYNYNNS KNSRPSTSLY KKAGFMGNIC AKKQFFVSFK DIGWNDWIIA PSGYHANYCE GECPSHIAGT SGSSLSFHST VINHYRMRGH SPFANLKSCC VPTKLRPMSM LYYDDGQNII KKDIQNMIVE ECGCS

Alternative Names

Inhibin beta-1, FRP, FSH-releasing protein, EDF, erythroid differentiation factor, FRP, follicle stimulating hormone releasing protein, Activin-A

Research Use Only

This product is for Research Use Only.
Product Details
Length 155 aa
Molecular Weight 35 kDa
Structure Dimer
Source Spodoptera frugiperda (Sf9) cell culture
Accession Number P08476
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.