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Roadblock Domain Containing 3 Human Recombinant ( ROBLD3 Human )

DescriptionROBLD3 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 149 amino acids (1-125 a.a.) and having a molecular mass of 16kDa. The ROBLD3 is

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Data sheet

Formulation The ROBLD3 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M Nacl, 2mM DTT and 10% glycerol.
Purity Greater than 95.0% as determined by SDS-PAGE.
Description ROBLD3 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 149 amino acids (1-125 a.a.) and having a molecular mass of 16kDa. The ROBLD3 is purified by proprietary chromatographic techniques.
Protein Background ROBLD3 is a member of the GAMAD family. ROBLD3 is an adapter protein which enhances the efficiency of the MAP kinase cascade and facilitates the activation of MAPK2. ROBLD3 compels the recruitment of MP1 to late endosomes where they form a very stable heterodimeric complex required for ERK activation on endosomes. In humans, a mutation in the ROBLD3 gene has been associated with a primary immunodeficiency syndrome, and suggests a role for the ROBLD3 protein in endosomal biogenesis.
Expression host Escherichia Coli.
Synonyms Ragulator complex protein LAMTOR2, Endosomal adaptor protein p14, Late endosomal/lysosomal Mp1-interacting protein, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 2, Mitogen-activated protein-binding protein-interacting protein, Roadblock domain-containing protein 3, LAMTOR2, MAPBPIP, ROBLD3, p14, ENDAP, HSPC003, MAPKSP1AP, Ragulator2, RP11-336K24.9.
Reagent Appearance Sterile Filtered colorless solution.
Stability ROBLD3 should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Amino acid sequence MGSSHHHHHH SSGLVPRGSH MGSHMLRPKA LTQVLSQANT GGVQSTLLLN NEGSLLAYSG YGDTDARVTA AIASNIWAAY DRNGNQAFNE DNLKFILMDC MEGRVAITRV ANLLLCMYAK ETVGFGMLKA KAQALVQYLE EPLTQVAAS.

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