SRPR alpha antibody

GeneTex

SRPR alpha antibody

9

This antibody can immunoprecipitate both SRPR alpha and beta under non denaturing conditions.

IP: Use at an assay dependent dilution. Can be used to immunoprecipitate both subunits of SRPR under non-denaturing conditions. WB: Use at a concentration of 1 - 5 microg/ml. Detects a band of approximately 72 kDa. Optimal dilutions/concentrations should be determined by the end user.

ImmunoPrecipitation, Western Blot

Research Use Only

Polyclonal

1 mg/ml

Unconjugated

SRPRA

SRP receptor subunit alpha

Docking protein alpha; DP-alpha; signal recognition particle receptor ('docking protein'); signal recognition particle receptor subunit alpha; SR-alpha; SRP receptor alpha subunit; SRPR

Sheep

IgG

The receptor for Signal Recognition Particle (SRP) is the site on the endoplasmic reticulum that ribosomes translating secreted and integral membrane proteins are initially targeted to. Once the ribosome-SRP complex arrives at the SRP receptor the protein being translated is transferred to the translocation complex (Sec61) in the ER membrane. SRPR is composed of two subunits SRPR alpha and SRPR beta. The SRPR alpha subunit is a translocation GTPase peripherally bound to the endoplasmic reticulum by its interaction with SRPR beta. SRPR alpha also binds to the GTPase of SRP (SRP54) and these two proteins appear to function as each others GTPase activating proteins (GAPs). Hydrolysis of GTP by SRPR alpha and SRP54 is thought to be involved in transfer of the nascent protein to the Sec61 complex in the ER. SRPR alpha has an apparent molecular weight of 72 kDa. SRPR beta is a Type I transmembrane protein that spans the membrane once and contains Ras type GTPase domain. The function of the GTPase in SRPR beta is unknown. The membrane spanning domain is at the amino-terminus of SRPR beta. SRPR alpha binds to the GTPase domain of SRPR beta. Heterodimerization of SRPR alpha and SRPR beta masks the carboxyl-terminal epitope of SRPR beta.

Canine

-20°C or -80°C,2°C to 8°C

12352203