Atp5c1 (BC010700) Mouse Tagged ORF Clone

Specifications

Product Data
Type	Mouse Tagged ORF Clone
Tag	TurboGFP
Synonyms	1700094F02Rik
Vector	pCMV6-AC-GFP
E. coli Selection	Ampicillin (100 ug/mL)
Mammalian Cell Selection	Neomycin
Sequence Data	ORF Nucleotide Sequence (showhide) >MG204152 representing BC010700 Red=Cloning site Blue=ORF Green=Tags(s) TTTTGTAATACGACTCACTATAGGGCGGCCGGGAATTCGTCGACTGGATCCGGTACCGAGGAGATCTGCC GCCGCGATCGCC ATGTTCTCGCGGGCGAGCGTTGTCGGGCTGTCGGCCTGCGCCGTGCAGCCGCAATGGATCCAAGTTCGAA ACATGGCAACTCTGAAAGATATTACCAGGAGACTGAAGTCCATCAAAAACATCCAGAAAATTACCAAGTC TATGAAGATGGTGGCAGCTGCAAAGTATGCCCGGGCTGAGCGGGAGCTGAAGCCTGCCCGAGTGTATGGG ACAGGTTCTTTGGCTCTGTATGAGAAGGCTGATATTAAGGCACCTGAGGACAAGAAGAAGCACCTCATTA TTGGTGTGTCCTCAGATAGAGGGCTTTGTGGTGCTATTCACTCCTCAGTGGCTAAACAGATGAAGAATGA AGTGGCTGCCCTCACAGCAGCTGGGAAAGAAGTTATGATTGTTGGAGTTGGTGAAAAAATCAAGGGCATA CTTTATAGGACTCATTCTGATCAGTTTTTGGTGTCATTCAAAGATGTGGGACGGAAGCCTCCTACTTTTG GAGATGCATCAGTCATTGCCCTTGAGTTGTTAAATTCTGGATATGAATTTGATGAAGGCTCTATCATTTT TAATCAGTTCAAGTCTGTTATCTCCTACAAGACAGAAGAGAAGCCCATCTTCTCTCTGAATACCATTGCG ACTGCTGAGACCATGAGCATCTATGATGACATTGATGCTGATGTGCTGCAGAATTACCAGGAGTACAATC TGGCCAACCTCATCTACTACTCCCTGAAGGAGTCCACCACCAGTGAGCAGAGTGCCAGGATGACCGCCAT GGACAACGCCAGCAAGAACGCTTCTGATATGATTGACAAATTGACCTTGACTTTCAACCGCACCCGCCAG GCTGTCATCACAAAGGAGTTGATTGAAATCATCTCTGGGGCTGCTGCTCTGGAT ACGCGTACGCGGCCGCTCGAG - GFP Tag - GTTTAA Protein Sequence (showhide) >MG204152 representing BC010700 Red=Cloning site Green=Tags(s) MFSRASVVGLSACAVQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYG TGSLALYEKADIKAPEDKKKHLIIGVSSDRGLCGAIHSSVAKQMKNEVAALTAAGKEVMIVGVGEKIKGI LYRTHSDQFLVSFKDVGRKPPTFGDASVIALELLNSGYEFDEGSIIFNQFKSVISYKTEEKPIFSLNTIA TAETMSIYDDIDADVLQNYQEYNLANLIYYSLKESTTSEQSARMTAMDNASKNASDMIDKLTLTFNRTRQ AVITKELIEIISGAAALD TRTRPLE - GFP Tag - V
Restriction Sites	SgfI-MluI      Cloning Scheme for this gene      Plasmid Map
ACCN	BC010700
ORF Size	896 bp
OTI Disclaimer	The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info
OTI Annotation	This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene.
Product Components	The ORF clone is ion-exchange column purified and shipped in a 2D barcoded Matrix tube containing 10ug of transfection-ready, dried plasmid DNA (reconstitute with 100 ul of water).
Reconstitution	1. Centrifuge at 5,000xg for 5min. 2. Carefully open the tube and add 100ul of sterile water to dissolve the DNA. 3. Close the tube and incubate for 10 minutes at room temperature. 4. Briefly vortex the tube and then do a quick spin (less than 5000xg) to concentrate the liquid at the bottom. 5. Store the suspended plasmid at -20°C. The DNA is stable for at least one year from date of shipping when stored at -20°C.
Note	Plasmids are not sterile.  For experiments where strict sterility is required, filtration with 0.22um filter is required.
Reference Data
RefSeq	BC010700, AAH10700
RefSeq Size	1125 bp
RefSeq ORF	896 bp
Locus ID	11949
Gene 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 synthesis 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 the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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]

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