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Recombinant Human Ras-related GTP-binding protein A(RRAGA),partial

Recombinant Human Ras-related GTP-binding protein A(RRAGA),partial

Hersteller	Cusabio
Kategorie	Metabolism Diabetes Glucose Homeostasis Peptides & Proteins Recombinant Proteins
Typ	Proteins Recombinant
Specific against	other
Format	Liquid or Lyophilized powder
Menge	200ug
Host	E.coli
ArtNr	CSB-RP034654h-200
Konjugat/Tag	GST
eClass 6.1	34160400
eClass 9.0	42020190
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Research Topic	Apoptosis
Uniprot ID	Q7L523
Gene Names	RRAGA
Organism	Homo sapiens (Human)
AA Sequence	MPNTAMKKKVLLMGKSGSGKTSMRSIIFANYIARD TRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFM ENYFTSQRDNIFRNVEVLIYVFDVESRELEKDMHY YQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRDLI FKEREEDLRRLSRPLECACFRTSIWDETLYKAWSS IVYQLIPNVQQLEMNLRNFAQIIEADEVLLFERAT FLVISHYQCKEQRDVHRFEKISNIIKQFKLSCSKL AA
Expression Region	1-247aa
Sequence Info	Partial
Source	E.coli
Tag Info	N-terminal GST-tagged
MW	56.1 kDa
Alternative Name(s)	Adenovirus E3 14.7KDA-interacting protein 1FIP-1
Relevance	Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. May alternatively act as a cellular target for adenovirus E3-14.7K, an inhibitor of TNF-alpha functions, thereby affecting cell death.
Reference	DNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004)
Purity	Greater than 90% as determined by SDS-PAGE.
Storage Buffer	Tris-based buffer, 50% glycerol
Storage	The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4C for up to one week.
Function	Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates in the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. May alternatively act as a cellular target for adenovirus E3-14.7K, an inhibitor of TNF-alpha functions, thereby affecting cell death.
Subcellular Location	Cytoplasm, Nucleus, Lysosome
Protein Families	GTR/RAG GTP-binding protein family
Tissue Specificity	Ubiquitously expressed with highest levels of expression in skeletal muscle, heart, and brain.
Paythway	mTORsignalingpathway
Tag Information	N-terminal GST-tagged

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