LRRC29 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | Q8WV35 |
Other Accession | NP_001004055.1, NP_036295.1 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Antigen Region | 32-60 aa |
Other Names | Leucine-rich repeat-containing protein 29, F-box and leucine-rich repeat protein 9, F-box protein FBL9, F-box/LRR-repeat protein 9, LRRC29, FBL9, FBXL9 |
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Target/Specificity | This LRRC29 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 32-60 amino acids from the N-terminal region of human LRRC29. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | LRRC29 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbls class and, in addition to an F-box, contains 9 tandem leucine-rich repeats. Two transcript variants encoding the same protein have been found for this gene. Other variants may occur, but their full-length natures have not been characterized.
References
Winston, J.T., et al. Curr. Biol. 9(20):1180-1182(1999)
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