Recombinant Human Neuroglycan C/CSPG5 Protein, CF
Recombinant Human Neuroglycan C/CSPG5 Protein, CF Summary
Product Specifications
0.6-1.2 μg/mL.
Val31-Gln420, with a C-terminal 6-His tag
Analysis
41.9 kDa
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
5685-NG
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 500 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: Neuroglycan C/CSPG5
Neuroglycan C (NGC; also CSPG5 and CALEB) is a 120 - 150 kDa type I transmembrane glycoprotein and member of the neuregulin family of proteins (1 ‑ 2). Depending on its expression profile, NGC may be a glycoprotein of 120 kDa, or a chondroitin sulfate (CS) proteoglycan of 150 kDa (2 - 3). Human NGC is synthesized as a 566 amino acid (aa) precursor that contains a 30 aa signal sequence, a 393 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 122 aa cytoplasmic region. The ECD contains one CS attachment domain (aa 34 - 272), with CS attachment at Ser117, one EGF-like domain (aa 371 - 413), two potential sites for N-linked glycosylation, and twelve potential sites for O-linked glycosylation (4). Splicing variants produce three isoforms for human NGC. Isoform 1 is the long form. Isoform 2 has a deletion of aa 487 ‑ 513, while isoform 3 has an alternative start site at Met139 and the same deletion. Phosphorylation likely occurs at Ser249, and proteolysis generates a 75 kDa soluble fragment (5). Over aa 31 - 420, human NGC shares 84% aa identity with mouse NGC. NGC is expressed in nervous tissue and is found on retinal ganglion cells, cerebellar Purkinje cells and hippocampal neurons (6). NGC may function as a growth and differentiation factor involved in neuritogenesis. One study shows that the recombinant ectodomain of NGC core protein enhances neurite outgrowth from rat neocortical neurons in culture via phosphatidylinositol 3-kinase and protein kinase C signaling pathways (7). Another study states that NGC is a novel component of midkine receptors, a heparin-binding growth factor that promotes cell attachment and process extension in oligodendroglial precursor-like cells (3). NGC also acts as a growth factor by directly binding ERbB3 tyrosine kinase and transactivating ErbB2 (1).
- Kinugasa, Y. et al. (2004) Biochem. Biophys. Res. Commun 321:1045.
- Yasuda, Y. et al. (1998) Neurosci. Res. 32:313.
- Ichihara-Tanaka, K. et al. (2006) J. Biol. Chem. 281:30857.
- Aono, S. et al. (2004) J. Biol. Chem. 279:46536.
- Shuo, T. et al. (2007) J. Neurochem. 102:1561.
- Aono, S. et al. (2006) J. Neurosci. Res.83:110.
- Nakanishi, K. et al. (2006) J. Biol. Chem. 281:24970.
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