ARPC2 Blocking Peptide (C-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O15144 |
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Other Accession | P85970, Q9CVB6, Q3MHR7 |
Gene ID | 10109 |
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Other Names | Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subunit, p34-ARC, ARPC2, ARC34 |
Target/Specificity | The synthetic peptide sequence is selected from aa 278-291 of HUMAN ARPC2 |
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 | ARPC2 |
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Synonyms | ARC34 |
Function | Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). Seems to contact the mother actin filament (PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). |
Cellular Location | Cytoplasm, cytoskeleton. Cell projection. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9CVB6}. Nucleus |
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Provided below are standard protocols that you may find useful for product applications.
Background
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament.
References
Welch M.D.,et al.J. Cell Biol. 138:375-384(1997).
Couch F.J.,et al.Genomics 36:86-99(1996).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Gevaert K.,et al.Nat. Biotechnol. 21:566-569(2003).
Zhang C.,et al.Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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