HERC4 Blocking Peptide (Center)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q5GLZ8 |
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Gene ID | 26091 |
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Other Names | Probable E3 ubiquitin-protein ligase HERC4, 632-, HECT domain and RCC1-like domain-containing protein 4, HERC4, KIAA1593 |
Target/Specificity | The synthetic peptide sequence is selected from aa 445-459 of HUMAN HERC4 |
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 | HERC4 |
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Synonyms | KIAA1593 |
Function | Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates. |
Cellular Location | Cytoplasm, cytosol. Note=shows a punctate cytoplasmic distribution |
Tissue Location | Expressed in brain and testis and detected in heart and placenta. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates (By similarity).
References
Hochrainer K.,et al.Genomics 85:153-164(2005).
Nagase T.,et al.DNA Res. 7:273-281(2000).
Deloukas P.,et al.Nature 429:375-381(2004).
Burkard T.R.,et al.BMC Syst. Biol. 5:17-17(2011).
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