Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. When Recombinant Human Cadherin-9 Fc Chimera is
immobilized at 1 μg/mL, 100 μL/well,
Recombinant
Human Cadherin‑6/KCAD Fc Chimera (Catalog # 2715-CA)
binds with an ED50 of 0.6-3.6 μg/mL.
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Source | Human embryonic kidney cell, HEK293-derived human Cadherin-9 protein
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Accession # | |||||||
N-terminal Sequence | Gly54 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Dilutions |
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Theoretical MW | 89.1 kDa. 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. |
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SDS-PAGE | 92-106 kDa, under reducing conditions |
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Publications |
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Storage |
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 250 μg/mL in PBS. |
Cadherin-9 (CDH9) is a member of the larger Cadherin superfamily of cell surface glycoproteins originally identified as proteins mediating cell-cell adhesion (1). In humans, there are more than 100 cadherin members divided into distinct families and numerous sub-families (1-3). Cadherins share a general structural architecture with an extracellular domain (ECD) containing 2 or more extracellular Ca2+ binding cadherin repeat (EC) domains, a single-pass transmembrane section, and a short cytoplasmic tail (1-3). Cadherins function by forming homophilic binding interactions through these EC domains to generate both trans and cis dimers (1-3). Human CDH9 is categorized as a classical cadherin, containing 5 EC domains, and the ECD shares 94% amino acid sequence identity with the ECD of both mouse and rat CDH9, respectively. Cadherins are found in diverse cell types and have been implicated as essential for the morphogenesis and homeostasis of multiple tissues and organs (1-3). Human CDH9 functions primarily in the central nervous system and is expressed in DG and CA3 neurons. Loss of CDH9 expression leads to defects in synapse formation and differentiation of specific neural circuits. (4). Additionally, disruption to CDH9 and CDH10 genes has been linked to autism spectrum disorders (5, 6). CDH9 expression has been identified in human kidney, and it has been used as a cell surface marker for fibroblasts (7). Recently, CDH9 has been reported as a potential suppressor of cancer metastasis (8).
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