elF2 alpha (EIF2S1) (NM_004094) Human Recombinant Protein

Specifications

Product Data
Species	Human
Expression Host	HEK293T
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) >RC200368 protein sequence Red=Cloning site Green=Tags(s) MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNEC VVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDD KYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKE ALRAGLNCSTENMPIKINLIAPPRYVMTTTTLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTD TDETELARQMERLERENAEVDGDDDAEEMEAKAED TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag	C-Myc/DDK
Predicted MW	35.9 kDa
Concentration	>0.05 µg/µL as determined by microplate BCA method
Purity	> 80% as determined by SDS-PAGE and Coomassie blue staining
Buffer	25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
Preparation	Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
Note	For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
Storage	Store at -80°C.
Stability	Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Reference Data
RefSeq	NP_004085
Locus ID	1965
UniProt ID	P05198, Q53XC0
Refseq Size	4165
Cytogenetics	14q23.3
Refseq ORF	945
Synonyms	EIF-2; EIF-2A; EIF-2alpha; EIF2; EIF2A
Summary	The translation initiation factor EIF2 catalyzes the first regulated step of protein synthesis initiation, promoting the binding of the initiator tRNA to 40S ribosomal subunits. Binding occurs as a ternary complex of methionyl-tRNA, EIF2, and GTP. EIF2 is composed of 3 nonidentical subunits, the 36-kD EIF2-alpha subunit (EIF2S1), the 38-kD EIF2-beta subunit (EIF2S2; MIM 603908), and the 52-kD EIF2-gamma subunit (EIF2S3; MIM 300161). The rate of formation of the ternary complex is modulated by the phosphorylation state of EIF2-alpha (Ernst et al., 1987 [PubMed 2948954]).[supplied by OMIM, Feb 2010]

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