PODS® Human CXCL12b

Code Description Price Qty
PPH159-50 PODS® Human CXCL12b, 50 million $160.00
PPH159-250 PODS® Human CXCL12b, 250 million $495.00
PPH159-1000 PODS® Human CXCL12b, 1 billion $1,650.00
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 CXCL12b. CXCL12, C-X-C motif chemokine 12 (CXCL12), is also known as Stromal cell-derived factor 1 β (SDF1 β). CXCL12 acts as a chemoattractant active on monocytes and T-lymphocytes but not neutrophils. The binding of CXCL12 to CXC receptor 4 (CXCR4) induces intracellular signalling through several divergent pathways which are implicated in chemotaxis, increase in intracellular calcium, cell survival and/or proliferation, and gene transcription. CXCL12 has diverse cellular functions including embryogenesis, tissue homeostasis, immune surveillance, inflammation, and tumour growth and metastasis. During embryogenesis, it is required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation.

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 KKAGFMNAKV VVVLVLVLTA LCLSDGKPVS LSYRCPCRFF ESHVARANVK HLKILNTPNC ALQIVARLKN NNRQVCIDPK LKWIQEYLEK ALNKRFKM

Alternative Names

SDF1/Stromal cell-derived factor 1

Research Use Only

This product is for Research Use Only.

Product Details
Length

138 aa

Molecular Weight

15.86 kDa

Structure

Dimer

Source

Spodoptera frugiperda (Sf9) cell culture

Accession Number

P48061

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.