O-mannosylation is an essential protein modification in eukaryotes that is initiated by an evolutionarily conserved family of protein O-mannosyltransferases. POMT2 encodes an integral membrane protein which localizes to the endoplasmic reticulum (ER) and shares significant sequence similarity with a family of protein O-mannosyltransferases of S. cerevisiae. The deduced 750 amino acid protein has a seven transmembrane helical structure with a central hydrophilic domain surrounded by five N-terminal and two C-terminal transmembrane regions. Like other known members of its family, POMT2 lacks a characteristic ER-targeting or -retention signal and contains five N-glycosylation sites. POMT2 shares 36% sequence identity with human POMT1 and RNA dot blot analysis reveals highest expression of mouse POMT2 in testis.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of POMT2 of human and, to a lesser extent, mouse and rat origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 1-52 mapping at the N-terminus of POMT2 of human origin
Tissue Specificity
epitope corresponding to amino acids 1-52 mapping at the N-terminus of POMT2 of human origin