Immunogen
Synthesized peptide derived from human EIF6 (Phospho-Ser235)
Specificity
This antibody detects endogenous levels of EIF6 (Phospho-Ser235) at Human, Mouse,Rat
Source
Polyclonal, Rabbit,IgG
Formulation
Liquid in PBS containing 50% glycerol, and 0.155% sodium azide.
Dilution rate
WB 1:500-2000
Purification process (Immunogen)
The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
Background
Hemidesmosomes are structures which link the basal lamina to the intermediate filament cytoskeleton. An important functional component of hemidesmosomes is the integrin beta-4 subunit (ITGB4), a protein containing two fibronectin type III domains. The protein encoded by this gene binds to the fibronectin type III domains of ITGB4 and may help link ITGB4 to the intermediate filament cytoskeleton. The encoded protein, which is insoluble and found both in the nucleus and in the cytoplasm, can function as a translation initiation factor and prevent the association of the 40S and 60S ribosomal subunits. Multiple non-protein coding transcript variants and variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Jun 2012],
Function
function:Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex.,similarity:Belongs to the eIF-6 family.,subunit:Monomer.,
Gene Name
EIF6 EIF3A ITGB4BP OK/SW-cl.27
Protein name
EIF6 (Phospho-Ser235)
Other name
Eukaryotic translation initiation factor 6 (eIF-6) (B(2)GCN homolog) (B4 integrin interactor) (CAB) (p27(BBP))
Fields
>>Ribosome biogenesis in eukaryotes
Human protein sequence Database
P56537
Mouse protein sequence database
O55135
Rat protein sequence database
Q3KRD8
Cellular localization
Cytoplasm. Nucleus, nucleolus. Shuttles between cytoplasm and nucleus/nucleolus.
Tissue expression
Expressed at very high levels in colon carcinoma with lower levels in normal colon and ileum and lowest levels in kidney and muscle (at protein level).
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