ELISA Kit FOR Cadherin-1

B0017h

Description

Gene name:	CDH1(CDHE;UVO);
Protein name:Alternative: CD:	Cadherin-1; Uvomorulin;CAM 120/80;Epithelial cadherin(E-cadherin); CD324;
Organism:	Human (Homo sapiens).

Sub Unit:	Homodimer; disulfide-linked. Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and potentially alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs). Interacts with AJAP1, CTNND1 and DLGAP5 (By similarity). Interacts with TBC1D2. Interacts with LIMA1. Interacts with CAV1. Interacts with the TRPV4 and CTNNB1 complex.
Function:	E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production.
Subcellular Location:	Cell junction Cell membrane Single-pass type I membrane protein Endosome Golgi apparatus trans-Golgi network Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane.

Sequence length:	882
Sequence:
50:	MGPWSRSLSA \| LLLLLQVSSW \| LCQEPEPCHP \| GFDAESYTFT \| VPRRHLERGR \|
100:	VLGRVNFEDC \| TGRQRTAYFS \| LDTRFKVGTD \| GVITVKRPLR \| FHNPQIHFLV \|
150:	YAWDSTYRKF \| STKVTLNTVG \| HHHRPPPHQA \| SVSGIQAELL \| TFPNSSPGLR \|
200:	RQKRDWVIPP \| ISCPENEKGP \| FPKNLVQIKS \| NKDKEGKVFY \| SITGQGADTP \|
250:	PVGVFIIERE \| TGWLKVTEPL \| DRERIATYTL \| FSHAVSSNGN \| AVEDPMEILI \|
300:	TVTDQNDNKP \| EFTQEVFKGS \| VMEGALPGTS \| VMEVTATDAD \| DDVNTYNAAI \|
350:	AYTILSQDPE \| LPDKNMFTIN \| RNTGVISVVT \| TGLDRESFPT \| YTLVVQAADL \|
400:	QGEGLSTTAT \| AVITVTDTND \| NPPIFNPTTY \| KGQVPENEAN \| VVITTLKVTD \|
450:	ADAPNTPAWE \| AVYTILNDDG \| GQFVVTTNPV \| NNDGILKTAK \| GLDFEAKQQY \|
500:	ILHVAVTNVV \| PFEVSLTTST \| ATVTVDVLDV \| NEAPIFVPPE \| KRVEVSEDFG \|
550:	VGQEITSYTA \| QEPDTFMEQK \| ITYRIWRDTA \| NWLEINPDTG \| AISTRAELDR \|
600:	EDFEHVKNST \| YTALIIATDN \| GSPVATGTGT \| LLLILSDVND \| NAPIPEPRTI \|
650:	FFCERNPKPQ \| VINIIDADLP \| PNTSPFTAEL \| THGASANWTI \| QYNDPTQESI \|
700:	ILKPKMALEV \| GDYKINLKLM \| DNQNKDQVTT \| LEVSVCDCEG \| AAGVCRKAQP \|
750:	VEAGLQIPAI \| LGILGGILAL \| LILILLLLLF \| LRRRAVVKEP \| LLPPEDDTRD \|
800:	NVYYYDEEGG \| GEEDQDFDLS \| QLHRGLDARP \| EVTRNDVAPT \| LMSVPRYLPR \|
850:	PANPDEIGNF \| IDENLKAADT \| DPTAPPYDSL \| LVFDYEGSGS \| EAASLSSLNS \|
882:	SESDKDQDYD \| YLNEWGNRFK \| KLADMYGGGE \| DD
3D Structure:	N/A