MARCH8 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q5T0T0 |
---|---|
Other Accession | NP_659458 |
Clone Names | 70319134 |
Gene ID | 220972 |
---|---|
Other Names | E3 ubiquitin-protein ligase MARCH8, 632-, Cellular modulator of immune recognition, c-MIR, Membrane-associated RING finger protein 8, Membrane-associated RING-CH protein VIII, MARCH-VIII, RING finger protein 178, MARCH8, MIR, RNF178 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP1452c was selected from the Center region of human MARCH8. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | MARCHF8 (HGNC:23356) |
---|---|
Synonyms | MARCH8, MIR, RNF178 |
Function | E3 ubiquitin-protein ligase that plays several important roles in innate immunity and adaptive immunity (PubMed:34285233, PubMed:35019698, PubMed:35503863). Mediates ubiquitination of CD86 and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies (PubMed:19117940, PubMed:19566897). Possesses a very broad antiviral activity by specifically inactivating different viral fusion proteins (PubMed:32934085). Targets and ubiquitinates cytoplasmic lysine residues of viral envelope glycoproteins with single transmembrane domains leading to their lysosomal degradation (PubMed:35019698). Therefore, shows broad-spectrum inhibition against many viruses including retroviruses, rhabdoviruses, arenaviruses, sarbecoviruses or influenzaviruses (PubMed:35019698, PubMed:34285233). Strongly blocks human immunodeficiency virus type 1 envelope glycoprotein incorporation into virions by down-regulating its cell surface expression. Blocks also ebola virus glycoprotein/GP incorporation via surface down-regulation (PubMed:32934085). Mediates 'Lys-63'-linked polyubiquitination of influenza M2 to target it to lysosome for degradation (PubMed:34285233). Mediates the regulation of constitutive ubiquitination and trafficking of the viral restriction factor BST2 within the endocytic pathway (PubMed:28320822). Plays a role in maintenance of immune tolerance to self by promoting the turnover and proteasomal degradation of PD-L1/CD274 via ubiquitination (PubMed:34183449). Catalyzes the 'Lys-63'-linked polyubiquitylation of cGAS thereby inhibiting its DNA binding ability and impairing its antiviral innate immunity (PubMed:35503863). |
Cellular Location | Golgi apparatus membrane. Endoplasmic reticulum membrane. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein |
Tissue Location | Broadly expressed. Present in immature dendritic cells (at protein level). |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
MARCH8 is an E3 ubiquitin-protein ligase that may regulate immune responses by promoting ubiquitination of MHC-II and CD86, which leads to their subsequent endocytosis and lysosomal degradation. May also promote ubiquitination and endocytosis of TFRC and FAS. 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.
References
Bartee, E., et al., J. Virol. 78(3):1109-1120 (2004).Goto, E., et al., J. Biol. Chem. 278(17):14657-14668 (2003).
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.