Code Description Price Qty
PPH32-50 PODS® Human CXCL1, 50 million $170.00
PPH32-250 PODS® Human CXCL1, 250 million $490.00
PPH32-1000 PODS® Human CXCL1, 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 Human CXCL1. Also known as GRO-alpha, CXCL1 is a member of the CXC subfamily of chemokines. It is a proinflammatory cytokine and a potent neutrophil attractant, playing a role in neutrophil migration and activation. CXCL1 is both structurally and functionally related to CXCL2 and CXCL3, all of which signal primarily via the IL-8 receptor type B. In vitro, CXCL1 is cleaved into three isoforms, CXCL1(4-73), CXCL1(5-73) and CXCL1(6-73), each of which shows higher chemotactic activity than the full-length protein. CXCL1 is known to be overexpressed constitutively in tumorigenic cells, with elevated levels seen in several tumour types. Human CXCL1 shares 64% and 67% aa sequence identity with mouse and rat CXCL1, respectively.

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.


This product is produced with no animal derived raw products. All processing and handling employs animal free equipment and animal free protocols.

AA Sequence

Immobilization tag shown in blue.


Alternative Names

Growth-regulated alpha protein, GRO-alpha, C-X-C motif chemokine 1, Melanoma growth stimulatory activity (MGSA), Neutrophil-activating protein 3 (NAP-3)

Research Use Only

This product is for Research Use Only.

Product Details

118 aa

Molecular Weight

13.05 kDa




Spodoptera frugiperda (Sf9) cell culture

Accession Number


Endotoxin Level

<0.06 EU/ml as measured by gel clot LAL assay


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.