Recombinant Human Cerebellin-1 Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Cerebellin-1 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Cerebellin-1 is coated at 5 μg/mL, biotinylated recombinant rat NRXN-1 beta binds with an apparent K_D < 0.5 nM. Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Recombinant Human Cerebellin-1, immobilized at 3-30 μg/mL, is able to significantly enhance neurite outgrowth.
• Source: Chinese Hamster Ovary cell line, CHO-derived human Cerebellin-1 protein
  Glu22-Leu193, with an N-terminal HA (YPYDVPDYA) tag
• Accession #: P23435
• N-terminal Sequence: Tyr
• Protein/Peptide Type: Recombinant Proteins
• Gene: CBLN1
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
  • Bioactivity2
• Theoretical MW: 20 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: 30-35 kDa (monomer) & Oligomer, reducing conditions

Packaging, Storage & Formulations

• Storage: 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 PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 250 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Cerebellin-1 Protein, CF

• CBLN1
• cerebellin 1 precursor
• Cerebellin1
• Cerebellin-1
• CLN1
• Precerebellin

Background

Cerebellin-1 (CBLN1) is a 35 kDa secreted glycoprotein in the Cerebellin family of TNF superfamily molecules (1). Cerebellins contain an N‑terminal collagenous domain and a C-terminal TNF/C1q-like domain. Mature human Cerebellin-1 shares 100% aa sequence identity with mouse and rat Cerebellin-1. It is expressed in the cerebellum, the parafascicular nucleus of the thalamus, and in the adrenal cortex and pancreatic islets (2 - 5). Cerebellin-1 forms noncovalent homotrimers that are disulfide-linked into hexamers (6). It can also form hetero-oligomers with Cerebellins-2, -3, and -4 and is required for the secretion of Cerebellin-3 (7 - 9). Cerebellin-1 is subject to proteolysis which can liberate 15-mer or 16-mer bioactive peptides from the C1q domain or remove the regions necessary for trimer or hexamer formation (6). Formation of the hexamer is required for Cerebellin-1’s ability to bind to synaptic structures (9, 10). It binds to postsynaptic densities through direct interactions with the glutamate receptor subunit GluRδ2 and to presynaptic membranes through direct interactions with alpha and beta Neurexins that contain the SS4 insert (11 - 14). The trans-synaptic trimolecular complex of GluRδ2, Cerebellin-1, and Neurexin promotes both presynaptic and postsynaptic development (11, 12). Cerebellin-1 itself is required for synaptic development, maintenance, and function (10, 12 - 15). It can also be internalized by Purkinje cells following secretion by cerebellar granule cells (2, 8, 15). The 16-mer and 15-mer peptides derived from Cerebellin-1 exert multiple endocrine effects including promoting corticosteroid secretion by cortical adrenal cells, inhibiting glucose‑stimulated insulin secretion from pancreatic islets, promoting Neuropeptide Y secretion by the hypothalamus, and decreasing plasma thyroid stimulating hormone (TSH) levels (4, 5, 16).

1. Yuzaki, M. (2011) Curr. Opin. Neurobiol. 21:215.
2. Wei, P. et al. (2009) Mol. Cell. Neurosci. 41:258.
3. Kusnoor, S.V. et al. (2010) J. Comp. Neurol. 518:2525.
4. Rucinski, M. et al. (2009) Int. J. Mol. Med. 23:363.
5. Strowski, M.Z. et al. (2009) Regul. Pept. 157:19.
6. Bao, D. et al. (2005) J. Neurochem. 95:618.
7. Iijima, T. et al. (2007) Eur. J. Neurosci. 25:1049.
8. Bao, D. et al. (2006) Mol. Cell. Biol. 26:9327.
9. Matsuda, K. et al. (2009) Eur. J. Neurosci. 29:707.
10. Ito-Ishida, A. et al. (2008) J. Neurosci. 28:5920.
11. Matsuda, K. et al. (2010) Science 328:363.
12. Matsuda, K. and M. Yuzaki (2011) Eur. J. Neurosci. 33:1447.
13. Uemura, T. et al. (2010) Cell 141:1068.
14. Joo, J.-Y. et al. (2011) Biochem. Biophys. Res. Commun. 406:627.
15. Hirai, H. et al. (2005) Nat. Neurosci. 8:1534.
16. Gardiner, J.V. et al. (2010) Diabetes Obes. Metab. 12:883.

Publications for Cerebellin-1/Precerebellin (6934-CB)(3)

Publications using 6934-CB

• P Han, Y She, Z Yang, M Zhuang, Q Wang, X Luo, C Yin, J Zhu, SR Jaffrey, SJ Ji Cbln1 regulates axon growth and guidance in multiple neural regions PloS Biology, 2022-11-17;20(11):e3001853. 2022-11-17 [PMID: 36395107] (IHC, Transgenic Mouse)
• PJ Gandhi, DY Gawande, GP Shelkar, SG Gakare, T Kiritoshi, G Ji, B Misra, R Pavuluri, J Liu, V Neugebauer, SM Dravid Dysfunction of Glutamate Delta-1 Receptor-Cerebellin 1 Trans-Synaptic Signaling in the Central Amygdala in Chronic Pain Cells, 2021-10-03;10(10):. 2021-10-03 [PMID: 34685624] (In Vivo, Mouse, Rat)
• Haddick P, Tom I, Luis E, Quinones G, Wranik B, Ramani S, Stephan J, Tessier-Lavigne M, Gonzalez L Defining the ligand specificity of the deleted in colorectal cancer (DCC) receptor. PLoS ONE, 2014-01-06;9(1):e84823. 2014-01-06 [PMID: 24400119] (Surface Plasmon Resonance)

Bioinformatics

• Gene Symbol: CBLN1
• Uniprot:
  • P23435()