MARCH11 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | A6NNE9 |
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Clone Names | 100203027 |
Gene ID | 441061 |
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Other Names | E3 ubiquitin-protein ligase MARCH11, 632-, Membrane-associated RING finger protein 11, Membrane-associated RING-CH protein XI, MARCH-XI, MARCH11 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP13811b was selected from the C-term region of MARCH11. 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 | MARCHF11 (HGNC:33609) |
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Synonyms | MARCH11 |
Function | E3 ubiquitin-protein ligase that mediates polyubiquitination of CD4. 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 play a role in ubuquitin-dependent protein sorting in developmenting spermatids. |
Cellular Location | Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:A6P320}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A6P320} |
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Provided below are standard protocols that you may find useful for product applications.
Background
MARCH11 is a member of the MARCH family of membrane-boundE3 ubiquitin ligases (EC 6.3.2.19). These enzymes add ubiquitin(see MIM 191339) to target lysines in substrate proteins, therebysignaling their intracellular transport. March11 appears to have arole in ubiquitin-mediated protein sorting in the trans-Golginetwork (TGN)-multivesicular body (MVB) transport pathway (Morokumaet al., 2007 [PubMed 17604280]).
References
Rose, J. Phd, et al. Mol. Med. (2010) In press :Morokuma, Y., et al. J. Biol. Chem. 282(34):24806-24815(2007)
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