Measured by its ability to induce myeloperoxidase release from cytochalasin B-treated human neutrophils. Schröder, J.M. et al. (1987) J. Immunol. 139:3474. The ED50 for this effect is 0.1‑0.3 µg/mL. Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with human CXCR2. The ED50 for this effect is 0.2‑1 ng/mL.
Source
E. coli-derived rat CXCL1/GRO alpha/KC/CINC-1 protein Ala25-Lys96
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Bioactivity2
Theoretical MW
7.8 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using 515-CN in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rat CXCL1/CINC-1 Protein
CINC1
CINC-1
CXCL1
FSP
GRO alpha
GRO1
GROa
KC
MGSA
MGSA-a
MGSA-alpha
NAP-3
SCYB1
Background
CXCL1, also known as KC, GRO alpha , and CINC-1, is an approximately 8 kDa proinflammatory chemokine that plays a key role in neutrophil migration and activation (1). Mature rat CXCL1 shares 67% and 92% aa sequence identity with human and mouse CXCL1, respectively (2, 3). It is produced by many cell types in inflammatory sites and during chronic inflammatory diseases (1). CXCL1 can associate into bioactive dimers and primarily signals through CXCR2/IL-8 RB but can also bind with lower affinity to CXCR2/IL-8 RA (4-6). It induces neutrophil migration, extravasation, respiratory burst, and degranulation and also induces T cells to produce proinflammatory IL-17 (5, 7, 8). CXCL1 additionally binds to Syndecan-1 on epithelial cells which acts as a sink for CXCL1 activity until Syndecan-1 cleavage by MMP-7 (9). CXCL1 is up-regulated in spinal cord astrocytes by inflammatory stimuli or tumor cell injection, and it exacerbates pain sensation by potentiating excitatory NMDA neurotransmission (10, 11). In the circulatory system, CXCL1 interacts with CXCR2 on endothelial cells to promote lymphatic tube formation and angiogenesis (12, 13). It promotes the hypertrophic differentiation of chondrocytes resulting in cartilage matrix deposition, calcification, and remodeling (14). It interacts with both CXCR1 and CXCR2 on adipose stromal cells and promotes their recruitment to prostate tumors in obese patients (15). It also binds CXCR2 on ovarian cancer cells, leading to cleavage of cell surface HB-EGF, transactivation of EGF R, and cell proliferation (16).
Strieter, R.M. et al. (2005) Cytokine Growth Factor Rev. 16:593.
Watanabe, K. et al. (1989) J. Biol. Chem. 264:19559.
Huang, S. et al. (1992) Biochem. Biophys. Res. Commun. 184:922.
Sawant, K.V. et al. (2015) J. Innate Immun. 7:647.
Geiser, T. et al. (1993) J. Biol. Chem. 268:15419.
Ahuja, S.K. and P.M. Murphy (1996) J. Biol. Chem. 271:20545.
Jin, L. et al. (2014) J. Immunol. 193:3549.
De Filippo, K. et al. (2013) Blood 121:4930.
Gill, S.E. et al. (2016) Am. J. Respir. Cell. Mol. Biol. PMID 26934670.
Cao, D.-L. et al. (2014) Exp. Neurol. 261:328.
Xu, J. et al. (2014) J. Neuroinflamm. 11:38.
Xu, J. et al. (2012) Int. J. Cancer 130:787.
Miyake, M. et al. (2013) Lab. Invest. 93:768.
Merz, D. et al. (2003) J. Immunol. 171:4406.
Zhang, T. et al. (2016) Nat. Commun. 7:11674.
Bolitho, C. et al. (2010) Endocr. Relat. Cancer 17:929.
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