Fxyd6 (BC042579) Mouse Recombinant Protein

Specifications

Product Data
Species	Mouse
Expression Host	HEK293T
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) >MR200248 protein sequence Red=Cloning site Green=Tags(s) METVLVLCSLLAPVVLASAAEKEKEKDPFYYDYQTLRIGGLVFAVVLFSVGILLILSRRCKCSFNQKPRA PGDEEAQVENLITTNAAEPQKAEN TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag	C-MYC/DDK
Predicted MW	10.4 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
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 after receiving vials.
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
Locus ID	59095
UniProt ID	Q9D164
Refseq Size	1600
Cytogenetics	9 A5.2
Refseq ORF	282
Synonyms	0610030I18Rik; Php
Summary	This reference sequence was derived from multiple replicate ESTs and validated by similar human genomic sequence. This gene encodes a member of a family of small membrane proteins that share a 35-amino acid signature sequence domain, beginning with the sequence PFXYD and containing 7 invariant and 6 highly conserved amino acids. The approved human gene nomenclature for the family is FXYD-domain containing ion transport regulator. Transmembrane topology has been established for two family members (FXYD1 and FXYD2), with the N-terminus extracellular and the C-terminus on the cytoplasmic side of the membrane. FXYD2, also known as the gamma subunit of the Na,K-ATPase, regulates the properties of that enzyme. FXYD1 (phospholemman), FXYD2 (gamma), FXYD3 (MAT-8), FXYD4 (CHIF), and FXYD5 (RIC) have been shown to induce channel activity in experimental expression systems. This gene product, Fxyd6, is novel and has not been characterized as a protein. [RefSeq curation by Kathleen J. Sweadner, Ph.D., sweadner@helix.mgh.harvard.edu., Jul 2006]

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