Rabbit anti-Human EMC8 Polyclonal Antibody

Uniprot Id

O43402

Target Species

Human

Target Name

EMC8

Target Full Name

ER membrane protein complex subunit 8

Target Function

Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).

Target Subcellular Location

Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.

Target Protein Families

EMC8/EMC9 family

Target Tissue Specificity

Expressed in liver, pancreas, heart, lung, kidney, brain, skeletal muscle, and placenta. Expression levels are highest in pancreas and moderate in heart, skeletal muscle, and placenta.

Target Synonyms

C16orf2; C16orf4; COX4 neighbor; COX4; neighbor of; COX4AL; Cox4nb; CX4NB_HUMAN; ER membrane protein complex subunit 8; FAM158B; family with sequence similarity 158; member B; Neighbor of COX4; NOC4; Protein FAM158B

Target Background

Contributes to membrane insertase activity. Involved in protein insertion into ER membrane by stop-transfer membrane-anchor sequence and tail-anchored membrane protein insertion into ER membrane. Located in cytosol. Part of EMC complex.