Detects human N-Cadherin in direct ELISAs.
In direct ELISAs, approximately 25%
cross-reactivity with recombinant mouse N-Cadherin is observed and no
cross-reactivity with recombinant human (rh) E-Cadherin or
rhCadherin-4/R-Cadherin is observed.
Monoclonal Mouse IgM Clone # 691701
Protein A or G purified from hybridoma culture supernatant
Mouse myeloma cell line NS0-derived recombinant human N-Cadherin Ser26-Arg159 Accession # P19022
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Detection of N-Cadherin in HeLa Human Cell Line by Flow Cytometry.
HeLa human cervical epithelial carcinoma cell line was stained with Mouse Anti-Human N‑Cadherin Monoclonal Antibody (Catalog # MAB13882, filled histogram) or isotype control antibody mouse IgM (open histogram), followed by Phycoerythrin-conjugated Anti-Mouse IgM Secondary Antibody (Catalog # F0116).
Preparation and Storage
Sterile PBS to a final concentration of 0.5 mg/mL.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
N‑Cadherin (Neural Cadherin; also CD325 and Cadherin-2) is a 130‑135 kDa member of the "classical" (or type I) cadherin subfamily, cadherin superfamily of proteins. It is expressed on multiple cell types, including neurons, fibroblasts, Schwann cells, endothelial cells and hepatic stellate cells. N‑Cadherin mediates homotypic binding, either in cis (same cell) or trans (adjacent cell). proN‑Cadherin is expressed as an 881 amino acid (aa) type I transmembrane glycoprotein. It may be initially inserted into the ER, where the 15‑20 kDa prodomain (aa 26‑159) is cleaved by proprotein convertase, and the mature molecule is transported to the surface. Alternatively, on neurons, proN‑Cadherin may first appear on the surface, with cleavage occurring at the time of synaptogenesis. Cleavage appears necessary for homophilic interaction as presence of the prodomain is suggested to negatively regulate oligomer formation. Over the entire prodomain, the human N‑Cadherin proregion shares 87% aa identity with the mouse N‑Cadherin proregion.
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