Recombinant Human Cerebellin-1 Protein, CF

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Recombinant Human Cerebellin-1 Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
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 KD < 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.
Chinese Hamster Ovary cell line, CHO-derived human Cerebellin-1 protein
Glu22-Leu193, with an N-terminal HA (YPYDVPDYA) tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
20 kDa (monomer)
30-35 kDa (monomer) & Oligomer, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 250 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.
  • 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.
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Background: Cerebellin-1

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.
Entrez Gene IDs
869 (Human); 12404 (Mouse); 498922 (Rat)
Alternate Names
CBLN1; cerebellin 1 precursor; Cerebellin1; Cerebellin-1; CLN1; Precerebellin

Citations for Recombinant Human Cerebellin-1 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. Cbln1 regulates axon growth and guidance in multiple neural regions
    Authors: P Han, Y She, Z Yang, M Zhuang, Q Wang, X Luo, C Yin, J Zhu, SR Jaffrey, SJ Ji
    PloS Biology, 2022-11-17;20(11):e3001853.
    Species: Transgenic Mouse
    Sample Types: Whole Tissue
    Applications: IHC
  2. Dysfunction of Glutamate Delta-1 Receptor-Cerebellin 1 Trans-Synaptic Signaling in the Central Amygdala in Chronic Pain
    Authors: PJ Gandhi, DY Gawande, GP Shelkar, SG Gakare, T Kiritoshi, G Ji, B Misra, R Pavuluri, J Liu, V Neugebauer, SM Dravid
    Cells, 2021-10-03;10(10):.
    Species: Mouse, Rat
    Sample Types: In Vivo
    Applications: In Vivo
  3. Defining the ligand specificity of the deleted in colorectal cancer (DCC) receptor.
    Authors: Haddick P, Tom I, Luis E, Quinones G, Wranik B, Ramani S, Stephan J, Tessier-Lavigne M, Gonzalez L
    PLoS ONE, 2014-01-06;9(1):e84823.
    Applications: Surface Plasmon Resonance


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