Recombinant Human CDH16 (C-6His)

Artikelnummer: EBT-EPT249
Artikelname: Recombinant Human CDH16 (C-6His)
Artikelnummer: EBT-EPT249
Hersteller Artikelnummer: EPT249
Alternativnummer: EBT-EPT249-10
Hersteller: ELK Biotechnology
Kategorie: Proteine/Peptide
Alternative Synonym: CDH16, Cadherin-16, Kidney-specific cadherin, Ksp-cadherin
Recombinant Human Cadherin-16 is produced by our Mammalian expression system and the target gene encoding Pro18-Ala786 is expressed with a 6His tag at the C-terminus.
Molekulargewicht: Molecular weight: 84.4 KDa. Apparent molecular weight: 90-115 KDa, reducing conditions
UniProt: O75309
Reinheit: Greater than 75% as determined by reducing SDS-PAGE.
Anwendungsbeschreibung: Redissolve: Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100µg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.. Endotoxin: Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. Background: Cadherin-16(CDH16) is a single-pass type I membrane protein which contains six cadherin domains. Mature cadherin proteins consist of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small highly conserved C-terminal cytoplasmic domain. Cadherins are calcium-dependent cell adhesion proteins and may contribute to the sorting of heterogeneous cell types. They preferentially interact with themselves in a homophilic manner in connecting cells. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. CDH16 is exclusively expressed in kidney, where the protein functions as the principal mediator of homotypic cellular recognition. It plays a role in the morphogenic direction of tissue development. CDH16 is composed of an extracellular domain containing 6 cadherin domains, a transmembrane region and a truncated cytoplasmic domain. However, it lacks the prosequence and tripeptide HAV adhesion recognition sequence typical of most classical cadherins.