Rat Cadherin-15 / CDH15 Protein (Fc Tag)

CDH15

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Catalog Number	P80281-R02H
Organism Species	Rat
Host	Human Cells
Synonyms	CDH15
Molecular Weight	The recombinant rat CDH15 /Fc comprises 822 amino acids and has a predicted molecular mass of 90.6 kDa. The apparent molecular mass of the protein is approximately 118 kDa in SDS-PAGE under reducing conditions.
predicted N	Val 22
SDS-PAGE
Purity	> 92 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the rat CDH15 (Q75NI5) (Met1-Gly602) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
Bio-activity
Research Area	Cell Biology |Cell Cycle |Cell Differentiation
Formulation	Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	Cadherin-15, also known as CDH15, is a member of the cadherin superfamily. Cadherins consist of an extracellular domain containing 5 cadherin domains, a transmembrane region, and a conserved cytoplasmic domain. Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Cadherin-15 contains 5 cadherin domains. It is expressed in some normal epithelial tissues and in some carcinoma cell lines. Defects in CDH3 are the cause of ectodermal dysplasia with ectrodactyly and macular dystrophy (EEM), also known as EEM syndrome, Albrectsen-Svendsen syndrome or Ohdo-Hirayama-Terawaki syndrome. Ectodermal dysplasia defines a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. EEM is an autosomal recessive condition characterized by features of ectodermal dysplasia such as sparse eyebrows and scalp hair, and selective tooth agenesis associated with macular dystrophy and ectrodactyly.
Reference	Shibata T, et al. (1997) Identification of human cadherin-14, a novel neurally specific type II cadherin, by protein interaction cloning. J Biol Chem. 272(8):5236-40. Bornemann A, et al. (1994) Immunocytochemistry of M-cadherin in mature and regenerating rat muscle. Anat Rec. 239(2):119-25. Donalies M, et al. (1991) Expression of M-cadherin, a member of the cadherin multigene family, correlates with differentiation of skeletal muscle cells. Proc Natl Acad Sci. 88(18):8024-8.