The antiserum was produced against synthesized peptide derived from human MARCH2. AA range:191-240

MARCH2 Polyclonal Antibody detects endogenous levels of 40604 protein.

MARCH2

E3 ubiquitin-protein ligase MARCH2

MARCH2 ;
RNF172 ;
HSPC240 ;
E3 ubiquitin-protein ligase MARCH2 ;
Membrane-associated RING finger protein 2 ;
Membrane-associated RING-CH protein II ;
MARCH-II ;
RING finger protein 172

MARCH2 is a member of the MARCH family of membrane-bound E3 ubiquitin ligases (EC 6.3.2.19). MARCH enzymes add ubiquitin (see MIM 191339) to target lysines in substrate proteins, thereby signaling their vesicular transport between membrane compartments. MARCH2 reduces surface accumulation of several glycoproteins and appears to regulate early endosome-to-trans-Golgi network (TGN) trafficking (Bartee et al., 2004 [PubMed 14722266]; Nakamura et al., 2005 [PubMed 15689499]).[supplied by OMIM, Mar 2010],

Caution:The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.,Domain:The RING-CH-type zinc finger domain is required for E3 ligase activity.,Function:E3 ubiquitin-protein ligase that may mediate ubiquitination of TFRC and CD86, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May be involved in endosomal trafficking through interaction with STX6.,pathway:Protein modification; protein ubiquitination.,similarity:Contains 1 RING-CH-type zinc finger.,subunit:Interacts with STX6 (By similarity). Interacts with MARCH3.,tissue specificity:Broadly expressed.,

Endoplasmic reticulum membrane ; Multi-pass membrane protein . Lysosome membrane ; Multi-pass membrane protein . Endosome membrane ; Multi-pass membrane protein . Golgi apparatus membrane ; Multi-pass membrane protein . Cytoplasm . Cell membrane ; Multi-pass membrane protein .

Broadly expressed.