(DANRE) sh3bp4a Blocking Peptide (N-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q1LVQ2 |
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Gene ID | 403082 |
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Other Names | SH3 domain-binding protein 4-A, sh3bp4a, sh3bp4 |
Target/Specificity | The synthetic peptide sequence is selected from aa 132-145 of HUMAN sh3bp4a |
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 | sh3bp4a |
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Synonyms | sh3bp4 |
Function | Possible role in regulating endocytosis of the transferrin receptor at the plasma membrane. Alternatively, may function as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy (By similarity). |
Cellular Location | Membrane, clathrin-coated pit. Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus. Note=Specifically associated with transferrin receptor- containing clathrin-coated pits and clathrin-coated vesicles. May also localize to the nucleus (By similarity). |
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Background
Possible role in regulating endocytosis of the transferrin receptor at the plasma membrane. Alternatively, may function as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy (By similarity).
References
Howe K.,et al.Nature 496:498-503(2013).
Abe S.,et al.Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
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