ELISA Kit FOR Cadherin-1

B0017b

Description

Gene name:	CDH1;
Protein name:Alternative: CD:	Cadherin-1; Epithelial cadherin(E-cadherin); CD324;
Organism:	Bovine (Bos taurus).

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 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 (By similarity). Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane.

Sequence length:	882
Sequence:
50:	MGPWSRSLSA \| LCCCCRCNPW \| LCREPEPCIP \| GFGAESYTFT \| VPRRNLERGR \|
100:	VLGRVSFEGC \| AGLPRTVYVS \| DDTRFKVHTD \| GVLTVRRPVH \| LHRPELSFLV \|
150:	HAWDSTHRKL \| STKVTLEVSA \| HHHHHHSHHD \| SPSGTQTEVL \| TFPGPHHGLR \|
200:	RQKRDWVIPP \| ISCPENEKGP \| FPKSLVQIKS \| NKEKETQVFY \| SITGQRADTP \|
250:	PVGVFIIERE \| TGWLKVTQPL \| DREQIAKYIL \| FSHAVSSNGQ \| AIEEPMEIVI \|
300:	TVTDQNDNKP \| QFTQEVFKAS \| ALEGALPGTS \| VMQVTATDID \| DEVNTYTAAI \|
350:	GYTIPAQDPM \| LPHNKMFTIN \| KETGVISVLT \| TGLDRESFPT \| YTLMVQAADL \|
400:	NGEGLSTTAT \| AVITVLDTND \| NAPRFNPTTY \| VGSVPENEAN \| VAITTLTVTD \|
450:	ADDPNTPAWE \| AVYTVLNDNE \| KQFIVVTDPV \| TNEGTLKTAK \| GLDFEAKQQY \|
500:	ILYVAVTNVA \| PFEVTLPTST \| ATVTVDVIDV \| NEAPIFVPPQ \| KRVEVPEDFG \|
550:	VGLEITSYTA \| REPDTFMEQK \| ITYRIWRDTA \| NWLEINPETG \| AISTRAELDR \|
600:	EDVDHVKNST \| YTALIIATDN \| GSPPATGTGT \| LLLFLDDVND \| NGPVPEPRTM \|
650:	DFCQRNPEPH \| IININDPDLP \| PNTSPFTAEL \| THGASVNWTI \| EYNDQERESL \|
700:	ILKPKKTLEL \| GDHKINLKLI \| DNQNKDQVTT \| LDVHVCDCDG \| IVSNCRKARP \|
750:	AEAGLQVPAI \| LGILGGILAF \| LILILLLLLL \| VRRRRVVKEP \| LLPPEDDTRD \|
800:	NVYYYDEEGG \| GEEDQDFDLS \| QLHRGLDARP \| EVTRNDVAPT \| LMSVPQYRPR \|
850:	PANPDEIGNF \| IDENLKAADS \| DPTAPPYDSL \| LVFDYEGSGS \| EAATLSSLNS \|
882:	SESDQDQDYD \| YLNEWGNRFK \| KLADMYGGGE \| DD
3D Structure:	N/A