Measured in a cell proliferation assay using SH‑SY5Y human neuroblastoma cells. The ED50 for this effect is 4-16 ng/mL. Measured by its binding ability in a functional ELISA. Immobilized Recombinant Human GFR alpha ‑3/GDNF R alpha ‑3 Fc Chimera (Catalog # 7269-FR) at 1 µg/mL (100 µL/well) can bind Recombinant Human Artemin with an apparent Kd <1 nM.
Source
E. coli-derived human Artemin protein Ala108-Gly220
>95%, 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
Binding Activity
Bioactivity
Theoretical MW
12 kDa (monomer). 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.
SDS-PAGE
12 kDa, reducing conditions
Publications
Read Publications using 2589-AR/CF 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 HCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCl.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Artemin Protein, CF
Artemin
ARTN
Enovin
EVN
EVNneurotrophic factor
NBN
Neublastin
Background
Human Artemin (ARTN; also known as enovin and neublastin) is a GDNF family ligand that is distantly related to the TGF-beta superfamily of molecules (1-4). As such, it is synthesized as a preproprotein, and contains a variable length pre-, or signal sequence, plus a 68 amino acid (aa) proregion and a 113 aa mature segment (5-7). Alternate splicing and start sites create signal sequences of 22, 30 and 39 aa, respectively. Their significance is unknown. Following synthesis and proteolytic processing, mature ARTN is secreted as a presumably glycosylated, 28 kDa disulfide-linked homodimer that contains three intrachain disulfide bonds and the typical TGF-beta signature cysteine-knot motif (5, 7). In the mature region, human ARTN is 89% and 88% aa identical to rat (8) and mouse ARTN (5, 7), respectively. Cells known to express ARTN include Schwann cells (2) and embryonic vascular smooth muscle cells (9). Human ARTN is active on rodent cells (5). The receptor for ARTN has been identified as the ligand binding subunit GFR alpha -3 plus the signal transducing subunit, RET (1, 5). The GFR alpha -1/RET receptor complex has also been suggested to be a ligand binding unit for ARTN (2, 5). Evidence, however, suggests that the GFR alpha -1/RET complex plays no functional role in ARTN activity (10, 11). ARTN is known to be a chemoattractant for sympathetic neuron axons innervating the developing cardiovascular system (9). It also promotes sensory neuron survival and likely plays a role in the development of the peripheral nervous system (5). Finally, it has been reported to reverse neuropathic pain due to nerve injury, and to help resolve morphological changes associated with nerve damage (12).
Airaksinen, M.S. and M. Saarma (2002) Nat. Rev. Neurosci. 3:383.
Saarma, M. (2000) Eur. J. Biochem. 267:6968.
Sariola, H. et al. (2003) J. Cell Sci. 116:3855.
Chang, H. et al. (2002) Endocr. Rev. 23:787.
Baloh, R.H. et al. (1998) Neuron 21:1291.
Masure, S. et al. (1999) Eur. J. Biochem. 266:892.
Rosenblad, C. et al. (2000) Mol. Cell. Neurosci. 15:199.
Stover, T. et al. (2000) Brain Res. Mol. Brain Res. 76:25.
Honma, Y. et al. (2002) Neuron 35:267.
Rakowicz, W.P. et al. (2002) J. Neurosci. 22:3953.
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