Detects human Cadherin-13 in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant human (rh) E-Cadherin, rhN-Cadherin, rhP-Cadherin, rhVE-Cadherin, rhCadherin-8, -11, -12 or -17 is observed.
Monoclonal Rat IgG2A Clone # 392411
Protein A or G purified from hybridoma culture supernatant
Mouse myeloma cell line NS0-derived recombinant human Cadherin-13 Glu23-Ala692 Accession # P55290
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.
Recombinant Human Cadherin‑13 under non-reducing conditions only (Catalog # 3264-CA)
0.25 µg/106 cells
NCI‑H460 human large cell lung carcinoma cell line
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Cadherin‑13 in Mouse Brain. Cadherin‑13 was detected in immersion fixed frozen sections of mouse brain (cerebellum) using Rat Anti-Human Cadherin‑13 Monoclonal Antibody (Catalog # MAB3264) at 25 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Rat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS017) and counterstained with hematoxylin (blue). Specific staining was localized to Purkinje cells. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
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.
Cadherin-13, also known as T-cadherin and H-cadherin, is a 105 kDa member of the cadherin family of transmembrane glycoproteins that mediate calcium-dependent intercellular adhesion (1). However, Cadherin-13 is an atypical member, lacking transmembrane and cytosolic domains and containing a GPI moiety that anchors Cadherin-13 to the plasma membrane (1‑2). Human Cadherin-13 is synthesized as a 713 amino acid (aa) precursor that contains a 22 aa signal sequence, a 116 aa propeptide, a 555 aa mature chain, and a second propeptide of 20 aa that is removed in the mature form to reveal the GPI anchor. The mature form contains five cadherin domains and eight potential sites for N-linked glycosylation. Mature human Cadherin-13 shares 96% aa identity with mature mouse Cadherin-13. Cadherin-13 is expressed in various tissues. It is highly expressed in the heart, and in the CNS, Cadherin-13 is expressed in the cerebral cortex, medulla, hippocampus, amygdala, thalamus, and substantia nigra (2). There are higher levels of Cadherin-13 in the adult brain than in developing brain (2). Cadherin-13 is also expressed in skin in the basal layer of the epidermis, lung, liver, kidney, and blood vessels (2). The structural characteristics of Cadherin-13 predict that it is unlikely to function as a true adhesion molecule in vivo (2). It is suggested that it may act rather as a signaling receptor participating in recognition of the environment and regulation of cell motility, proliferation, and phenotype (2). Cellular expression levels of Cadherin-13 in various tissues often correlate, negatively or positively, with the proliferative potential of the cells (2). Cadherin-13 may also act as a suppressor of tumor cell growth (2). This potential role for Cadherin-13 was emphasized by localization of Cadherin-13 gene to chromosome 16q24, a region exhibiting loss of heterozygosity in many solid tumors (2). Allelic loss of chromosome bands 16q24.1-q24.2 and reduced expression of Cadherin-13, as well as hypermethylation of the remaining allele have been detected in a considerable number of human cancers (2).
Tanihara, H. et al. (1994) Cell Adhes. Commun. 2:15.
Philippova, M. et al. (2009) Cell. Signal. 21:1035.
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