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Recombinant Human SESTD1 protein, His-tagged

Cat.No. : SESTD1-92H
Product Overview : Recombinant Human SESTD1, fused with N-His tag, was expressed in E. coli.
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  • Gene Information
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Description : May act as the primary docking protein directing membrane turn over and assembly of the transient receptor potential channels TRPC4 and TRPC5. Binds phospholipids such as phosphatidylinositol monophosphates, phosphatidylinositol diphosphates (PIP2s) and phosphatidic acid, but not less polar lipids including phosphatidylcholine, phosphatidylserine, and phosphatidylinositol. The binding to PIP2s is calcium dependent. Might be involved in the plasma membrane localization of CTNNB1.
Source : E.coli
Species : Human
Tag : His
Form : 20mM Tris.Cl, 50mM NaCl, 50% Glycerol, pH8.0.
Molecular Mass : 28kDa(including fusion tag)
Protein length : 240aa(including fusion tag)
Applications : WB, ELISA, IP, antibody production, protein array
Storage : Store at -80centigrade and avoid repeated freeze-thaw cycles
Gene Name : SESTD1 SEC14 and spectrin domains 1 [ Homo sapiens ]
Official Symbol : SESTD1
Synonyms : SESTD1; SEC14 and spectrin domains 1; SEC14 domain and spectrin repeat-containing protein 1; DKFZp434O0515; Solo; protein Solo; huntingtin-interacting protein-like protein; SOLO;
Gene ID : 91404
mRNA Refseq : NM_178123
Protein Refseq : NP_835224
MIM :
UniProt ID : Q86VW0
Chromosome Location : 2q31.3
Function : NOT 1-phosphatidylinositol binding; phosphatidic acid binding; NOT phosphatidylcholine binding; phosphatidylinositol-3,4-bisphosphate binding; phosphatidylinositol-3,5-bisphosphate binding; phosphatidylinositol-3-phosphate binding; phosphatidylinositol-4,5-bisphosphate binding; phosphatidylinositol-4-phosphate binding; phosphatidylinositol-5-phosphate binding; NOT phosphatidylserine binding; protein binding;

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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