SID-1 and SID-2 belong to the systemic RNA interference defective-1 (SID1) family of transmembrane proteins. SID-1, originally identified in C. elegans, is an 827 amino acid protein. It localizes to the cell membrane and contains eleven transmembrane domains. This suggests that SID-1 possibly functions as a channel protein. The overexpression of SID-1 enhances double stranded RNA (dsRNA) uptake in pancreatic ductal adenocarcinoma cells. SID-2, also first identified in C. elegans, is an 832 amino acid protein with multiple transmembrane domains. At least two isoforms exist for SID-2 due to alternative splicing. Isoform 2 contains an additional 21 amino acids after residue 387 and has an alternate sequence that is 8 amino acids shorter for residues 814 to 832 of isoform 1.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of SID-1 of mouse, rat and, to a lesser extent, human origin by WB, IP, IF and ELISA non cross-reactive with isoform 2
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 1-95 mapping within an N-terminal extracellular domain of SID-1 of mouse origin
Tissue Specificity
epitope corresponding to amino acids 1-95 mapping within an N-terminal extracellular domain of SID-1 of mouse origin