Recombinant Human Cerebellin-1 Protein, CF

(1 citations)   
  • Purity
    >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.
  • Activity
    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.
  • Source
    Chinese Hamster Ovary cell line, CHO-derived Glu22-Leu193, with an N-terminal HA (YPYDVPDYA) tag
  • Accession #
  • N-terminal Sequence
    Analysis
    Tyr
  • Predicted Molecular Mass
    20 kDa (monomer)
  • SDS-PAGE
    30-35 kDa (monomer) & Oligomer, reducing conditions
6934-CB
 
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.
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).
  • References:
    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
Related Research Areas
Citations:

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.

1 Citations: Showing 1 - 1

  1. 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;9(1):e84823.
    Species: N/A
    Sample Type: Recombinant Protein
    Application: Surface Plasmon Resonance
Primary Antibodies
Description Application Cat# Citations Images  

HA Tag Antibody

WB MAB060 3  
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