Anti-ARP8 Antibodies
These mouse IgG1 monoclonal antibodies were generated against protein and recognize A. thaliana, Brassica and other closely related eukaryotes Actin-related protein 8 (ARP8).
Highlights:
- Recognizes A. thaliana, Brassica and other closely related eukaryotes Actin-related protein 8 (ARP8)
- Clone 13F10 is specific for ARP8 N-terminal amino acids 2–26
- Clone 12F5 is specific for ARP8 C-terminal amino acids 447–471
- Suitable for ELISA, Immunoblot, Immunocytochemistry, Immunofluorescence and Western Blot applications
Actin-related proteins (ARPs) are found in the nuclei of all eukaryotic cells, but their functions are generally understood only in the context of their presence in various yeast and animal chromatin-modifying complexes. Arabidopsis ARP8 shows 30 and 29% amino acid identity to yeast actin and Arabidopsis ACT2 in the regions of alignment, respectively. Because it is not closely related to yeast or human ARP8 and shows similar weak homology to yeast ARP8 and ARP9, the Arabidopsis ARP8 is considered a plant-specific orphan ARP.
From the laboratory of Richard B. Meagher, PhD, University of Georgia.
These mouse IgG1 monoclonal antibodies were generated against protein and recognize A. thaliana, Brassica and other closely related eukaryotes Actin-related protein 8 (ARP8).
Highlights:
- Recognizes A. thaliana, Brassica and other closely related eukaryotes Actin-related protein 8 (ARP8)
- Clone 13F10 is specific for ARP8 N-terminal amino acids 2–26
- Clone 12F5 is specific for ARP8 C-terminal amino acids 447–471
- Suitable for ELISA, Immunoblot, Immunocytochemistry, Immunofluorescence and Western Blot applications
Actin-related proteins (ARPs) are found in the nuclei of all eukaryotic cells, but their functions are generally understood only in the context of their presence in various yeast and animal chromatin-modifying complexes. Arabidopsis ARP8 shows 30 and 29% amino acid identity to yeast actin and Arabidopsis ACT2 in the regions of alignment, respectively. Because it is not closely related to yeast or human ARP8 and shows similar weak homology to yeast ARP8 and ARP9, the Arabidopsis ARP8 is considered a plant-specific orphan ARP.
From the laboratory of Richard B. Meagher, PhD, University of Georgia.
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Antibody |
| Antigen: | Actin-related protein 8 (ARP8), including recombinant forms |
| Accession ID: | Q9H981 |
| Molecular Weight: | 52 kDa |
| Isotype: | IgG1 |
| Clonality: | Monoclonal |
| Clone Name: | 13F10.A4.G6 or 13F10.A4.G6 |
| Reactivity: | A. thaliana,Brassica and other eukaryotes for which ARP8 is closely related to thaliana?s |
| Immunogen: | Protein |
| Species Immunized: | Mouse |
| Purification Method: | Not purified, available as antibody supernatant |
| Buffer: | Cell Culture Supernatant |
| Tested Applications: | WB, ELISA, IF, IB, Immunocytochemistry |
| Storage: | -80C |
| Shipped: | Cold Packs |
MAbARP8-N reacted with the full-length 52 kDa recombinant ARP8 protein expressed in Escherichia coli and endogenous ARP8 of identical molecular weight in Arabidopsis plant extracts.. MAbARP8-N detected ARP8 protein in all vegetative and reproductive organs examined including seedlings, roots and siliques, although higher concentrations were observed in developing flower buds and flowers within the inflorescence
- Kandasamy MK, McKinney EC, Meagher RB. ACTIN-RELATED PROTEIN8 encodes an F-box protein localized to the nucleolus in Arabidopsis. Plant Cell Physiol. 2008 May;49(5):858-63.
- Li Y, Kandasamy MK, Meagher RB. Rapid isolation of monoclonal antibodies. Monitoring enzymes in the phytochelatin synthesis pathway. Plant Physiol. 2001 Nov;127(3):711-9.
- Kandasamy MK, McKinney EC, Meagher RB. Differential sublocalization of actin variants within the nucleus. Cytoskeleton (Hoboken). 2010 Nov;67(11):729-43.
- Meagher RB, Kandasamy MK, Smith AP, McKinney EC. Nuclear actin-related proteins at the core of epigenetic control. Plant Signal Behav. 2010 May;5(5):518-22.
- Kristó I, Bajusz I, Bajusz C, Borkúti P, Vilmos P. Actin, actin-binding proteins, and actin-related proteins in the nucleus. Histochem Cell Biol. 2016 Apr;145(4):373-88.
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