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Atp5d (NM_025313) Mouse Recombinant Protein

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SKU
TP501389
Purified recombinant protein of Mouse ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit (Atp5d), with C-terminal MYC/DDK tag, expressed in HEK293T cells, 20ug
Size:
20 ug
  $1,020.00
4 Weeks*
Bulk/Customize

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Specifications
Specifications
Product Data
Species Mouse
Expression Host HEK293
Expression cDNA Clone or AA Sequence
Protein Sequence
>MR201389 protein sequence
Red=Cloning site Green=Tags(s)

MLPASLLRHPGLRRLMLQARTYAEAAAAPAPAAGPGQMSFTFASPTQVFFDSANVKQVDVPTLTGAFGIL
ASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAARANLEKAQSE
LSGAADEAARAEIQIRIEANEALVKALE

TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag C-MYC/DDK
Predicted MW 17.6 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.
Shipping Dry Ice
Reference Data
RefSeq NP_079589
Locus ID 66043
UniProt ID Q9D3D9
Cytogenetics 10 C1
RefSeq Size 931
RefSeq ORF 504
Synonyms 0610008F14Rik; 1500000I11Rik; AA960090; AI876556; AU020773; C85518
Summary Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.UniProtKB/Swiss-Prot Function
Protein Categories Intracellular Proteins
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*Delivery time may vary from web posted schedule. Occasional delays may occur due to unforeseen complexities in the preparation of your product. International customers may expect an additional 1-2 weeks in shipping.

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