Syntaxin 1A, 1-226aa, Human, Recombinant

Category: Proteins
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01-2275
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Product Name Syntaxin 1A, 1-226aa, Human, Recombinant
Description Syntaxin is membrane integrated Q-SNARE protein participating in exocytosis. Syntaxin is composed of an N-terminal regulatory domain(Habc), a SNARE domain(known as H3), and a single C-terminal transmembrane domain. The SNARE(H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Recombinant syntaxin 1A protein(1-226aa) contains N-terminal domain(Habc) and t_SNARE domain(H3 domain) and this protein was overexpressed in E.coli and purified by using the conventional column chromatography techniques.
Synonyms STX1A, STX1, Syntaxin 1A, Neuron-specific antigen HPC-1, Syntaxin-1A, HPC 1, Neuron specific antigen HPC1, STX1, Syntaxin 1A brain.
Host E. coli
Molecular Weight 48.2 KDa (444 aa)
Amino Acid Sequence MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQ
Tag His-tag
Reactivity Human
Applications SDS-PAGE
Form Liquid, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM DTT, 10 % glycerol
Concentration 1 mg/ml (determined by Bradford assay)
Purity > 95% by SDS-PAGE
Storage Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles.
References Han X., et al. (2004) Science. 304:289-292 Woodbury DJ. et al. (2000) Cell Biology International. 24(11):809-818.
Background Syntaxin is membrane integrated Q-SNARE protein participating in exocytosis. Syntaxin is composed of an N-terminal regulatory domain(Habc), a SNARE domain(known as H3), and a single C-terminal transmembrane domain. The SNARE(H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Recombinant syntaxin 1A protein(1-226aa) contains N-terminal domain(Habc) and t_SNARE domain(H3 domain) and this protein was overexpressed in E.coli and purified by using the conventional column chromatography techniques.
Supplier ARP

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