ELISA Kit FOR Cadherin-1

B0017m

Description

Gene name:	Cdh1;
Protein name:Alternative: CD:	Cadherin-1; Uvomorulin;ARC-1;Epithelial cadherin(E-cadherin); CD324;
Organism:	Mouse (Mus musculus).

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 (By similarity). 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:	884
Sequence:
50:	MGARCRSFSA \| LLLLLQVSSW \| LCQELEPESC \| SPGFSSEVYT \| FPVPERHLER \|
100:	GHVLGRVRFE \| GCTGRPRTAF \| FSEDSRFKVA \| TDGTITVKRH \| LKLHKLETSF \|
150:	LVRARDSSHR \| ELSTKVTLKS \| MGHHHHRHHH \| RDPASESNPE \| LLMFPSVYPG \|
200:	LRRQKRDWVI \| PPISCPENEK \| GEFPKNLVQI \| KSNRDKETKV \| FYSITGQGAD \|
250:	KPPVGVFIIE \| RETGWLKVTQ \| PLDREAIAKY \| ILYSHAVSSN \| GEAVEDPMEI \|
300:	VITVTDQNDN \| RPEFTQEVFE \| GSVAEGAVPG \| TSVMKVSATD \| ADDDVNTYNA \|
350:	AIAYTIVSQD \| PELPHKNMFT \| VNRDTGVISV \| LTSGLDRESY \| PTYTLVVQAA \|
400:	DLQGEGLSTT \| AKAVITVKDI \| NDNAPVFNPS \| TYQGQVPENE \| VNARIATLKV \|
450:	TDDDAPNTPA \| WKAVYTVVND \| PDQQFVVVTD \| PTTNDGILKT \| AKGLDFEAKQ \|
500:	QYILHVRVEN \| EEPFEGSLVP \| STATVTVDVV \| DVNEAPIFMP \| AERRVEVPED \|
550:	FGVGQEITSY \| TAREPDTFMD \| QKITYRIWRD \| TANWLEINPE \| TGAIFTRAEM \|
600:	DREDAEHVKN \| STYVALIIAT \| DDGSPIATGT \| GTLLLVLLDV \| NDNAPIPEPR \|
650:	NMQFCQRNPQ \| PHIITILDPD \| LPPNTSPFTA \| ELTHGASVNW \| TIEYNDAAQE \|
700:	SLILQPRKDL \| EIGEYKIHLK \| LADNQNKDQV \| TTLDVHVCDC \| EGTVNNCMKA \|
750:	GIVAAGLQVP \| AILGILGGIL \| ALLILILLLL \| LFLRRRTVVK \| EPLLPPDDDT \|
800:	RDNVYYYDEE \| GGGEEDQDFD \| LSQLHRGLDA \| RPEVTRNDVA \| PTLMSVPQYR \|
850:	PRPANPDEIG \| NFIDENLKAA \| DSDPTAPPYD \| SLLVFDYEGS \| GSEAASLSSL \|
884:	NSSESDQDQD \| YDYLNEWGNR \| FKKLADMYGG \| GEDD
3D Structure:	N/A