epitope mapping near the C-terminus of LRRC43 of human origin
Modification Notes
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC43 (leucine rich repeat containing 43) is a 656 amino acid protein containing four LRR (leucine-rich) repeats and one LRRCT domain. LRRC43 exists as three alternatively spliced isoforms and is encoded by a gene located on human chromosome 12q24.31.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of LRRC43 of mouse and human origin by WB, IP, IF and ELISA non cross-reactive with other LRRC family members also reactive with additional species, including equine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping near the C-terminus of LRRC43 of human origin
Tissue Specificity
epitope mapping near the C-terminus of LRRC43 of human origin
Western blot analysis of LRRC43 expression in NRK whole cell lysate.
Application Notes
recommended for detection of LRRC43 of mouse and human origin by WB, IP, IF and ELISA non cross-reactive with other LRRC family members also reactive with additional species, including equine:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.