Recombinant Human SRP14 protein is a Human Full Length protein, in the 1 to 160 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M G S H M V L L E S E Q F L T E L T R L F Q K C R T S G S V Y I T L K K Y D G R T K P I P K K G T V E G F E P A D N K C L L R A T D G K K K I S T V V S S K E V N K F Q M A Y S N L L R A N M D G L K K R D K K N K T K K T K A A A A A A A A A P A A A A T A A T T A A T T A A T A A Q
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:11089964). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP (PubMed:11089964). The complex of SRP9 and SRP14 is required for SRP RNA binding (PubMed:11089964).
Signal recognition particle 14 kDa protein, SRP14, 18 kDa Alu RNA-binding protein
Recombinant Human SRP14 protein is a Human Full Length protein, in the 1 to 160 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab101206 was purified by using conventional chromatography and is >85 % pure by SDS-PAGE.
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:11089964). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP (PubMed:11089964). The complex of SRP9 and SRP14 is required for SRP RNA binding (PubMed:11089964).
Belongs to the SRP14 family.
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ab101206 (3 μg) analysed by 15% SDS PAGE.
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