ELISA Kit FOR Cadherin-1

B0017r

Description

Gene name:	Cdh1;
Protein name:Alternative: CD:	Cadherin-1; Epithelial cadherin(E-cadherin);Uvomorulin; CD324;
Organism:	Rat (Rattus norvegicus).

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:	886
Sequence:
50:	MGARCRSFSA \| LLLLLQVSSW \| LCQQPESESD \| SCRPGFSSEV \| YTFLVPERHL \|
100:	ERGHILGRVK \| FEGCTGRPRT \| AFFSEDSRFK \| VSTDGVITVK \| RHLKLHKLET \|
150:	SFLVHAWDSS \| YRKLSTKVTL \| KSLGHHHHRH \| HHRDPVSESN \| PELLTFPSFH \|
200:	QGLRRQKRDW \| VIPPINCPEN \| QKGEFPQRLV \| QIKSNRDKET \| TVFYSITGPG \|
250:	ADKPPVGVFI \| IERETGWLKV \| TQPLDREAID \| KYLLYSHAVS \| SNGEAVEDPM \|
300:	EIVVTVTDQN \| DNRPEFIQEV \| FEGSVAEGAL \| PGTSVMQVSA \| TDADDDINTY \|
350:	NAAIAYTILS \| QDPELPHKNM \| FTVNRDTGVI \| SVVTSGLDRE \| SYPTYTLVVQ \|
400:	AADLQGEGLS \| TTAKAVITVK \| DINDNAPIFN \| PSTYQGQVLE \| NEVGARIATL \|
450:	KVTDDDAPNT \| PAWNAVYTVV \| NDPDHQFTVI \| TDPKTNEGIL \| KTAKGLDFEA \|
500:	KQQYILHVTV \| ENEEPFEGSL \| VPSTATVTVD \| VVDVNEAPIF \| VPAEKRVEVP \|
550:	EDFGVGLEIA \| SYTAREPDTF \| MEQKITYRIW \| RDTANWLEIN \| PETGVISTRA \|
600:	EMDREDSEHV \| KNSTYTALII \| ATDDGSPIAT \| GTGTLLLVLS \| DVNDNAPIPE \|
650:	PRNMQFCQRN \| PKPHVITILD \| PDLPPNTSPF \| TAELTHGASV \| NWTIEYNDAE \|
700:	QESLILQPRK \| DLEIGEYKIN \| LKLSDNQNKD \| QVTTLEVHVC \| DCEGTVNNCM \|
750:	KAISLEAGLQ \| VPAILGILGG \| ILALLILILL \| LLLFLRRRTV \| VKEPLLPPDD \|
800:	DTRDNVYYYD \| EEGGGEEDQD \| FDLSQLHRGL \| DARPEVIRND \| VAPTLMSMPQ \|
850:	YRPRPANPDE \| IGNFIDENLK \| AADSDPTAPP \| YDSLLVFDYE \| GSGSEAASLS \|
886:	SLNSSESDQD \| QDYDYLNEWG \| NRFKKLADMY \| GGGEED
3D Structure:	N/A