|Positive WB detected in||COLO 320 cells, A375 cells, HEK-293 cells, HeLa cells, HepG2 cells, mouse liver tissue|
|Positive IHC detected in||human prostate cancer tissue, human colon tissue|
Note: suggested antigen retrieval with TE buffer pH 9.0; (*) Alternatively, antigen retrieval may be performed with citrate buffer pH 6.0
|Positive IF detected in||HeLa cells|
|Positive FC detected in||HeLa cells|
|Western Blot (WB)||WB : 1:500-1:2000|
|Immunohistochemistry (IHC)||IHC : 1:20-1:200|
|Immunofluorescence (IF)||IF : 1:50-1:500|
|Sample-dependent, check data in validation data gallery|
10291-1-AP targets EIF6 in WB, IHC, IF, FC, ELISA applications and shows reactivity with human, mouse, rat samples.
|Tested Reactivity||human, mouse, rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||EIF6 fusion protein Ag0324|
|Full Name||eukaryotic translation initiation factor 6|
|Calculated molecular weight||27 kDa|
|Observed molecular weight||27 kDa|
|GenBank accession number||BC001119|
|Gene ID (NCBI)||3692|
|Purification Method||Antigen affinity purification|
|Storage Buffer||PBS with 0.02% sodium azide and 50% glycerol pH 7.3.|
|Storage Conditions||Store at -20°C. Stable for one year after shipment. Aliquoting is unnecessary for -20oC storage.|
p27(BBP/eIF6) is an evolutionarily conserved protein that was originally identified as p27(BBP), It functions as an interactor of the cytoplasmic domain of integrin 4 and as the putative translation initiation factor eIF6. p27BBP is found in two pools: one nuclear pool enriched in the perinucleolar region, and one cytoplasmic pool. p27BBP binds to the fibronectin type III domains of integrin 4 subunit (ITGB4), an important functional component of hemidesmosomes, and help link ITGB4 to the intermediate filament cytoskeleton. In vitro and in vivo studies demonstrated that p27BBP is essential for cell viability and has a primary function in the biogenesis of the 60S ribosomal subunit. p27BBP protein is increased in rapidly cycling cells and decreased in villous cells committed to apoptotic cell death. In dysplastic colorectal adenomas and carcinomas, p27BBP displayed a large increase of its nucleolar component and was associated with the nuclear matrix. In particular, p27BBP increased progressively from adenomas to carcinomas and was related to the tumor stage.
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