Recombinant Human NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (NDUFS1)

Code CSB-YP015660HU
MSDS
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Source Yeast
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Code CSB-EP015660HU
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Source E.coli
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Code CSB-EP015660HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP015660HU
MSDS
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Source Baculovirus
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Code CSB-MP015660HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
NDUFS1
Uniprot No.
Alternative Names
CI-75kD; Complex I 75Kd; Complex I, mitochondrial respiratory chain, 75 kD subunit; Complex I-75kD; mitochondrial; NADH coenzyme Q reductase; NADH dehydrogenase (ubiquinone) FeS protein 1 (75kD) (NADH coenzyme Q reductase); NADH ubiquinone oxidoreductase 75 kDa subunit mitochondrial ; NADH-ubiquinone oxidoreductase 75 kDa subunit; NDUFS1; NDUS1_HUMAN; PRO1304
Species
Homo sapiens (Human)
Expression Region
24-727
Target Protein Sequence
TATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGNDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA LVALKDLLNR VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK ILQDIASGSH PFSQVLKEAK KPMVVLGSSA LQRNDGAAIL AAVSSIAQKI RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKVLFLLGA DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS PNLVRYDDIE GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA VEEPSIC
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I. Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes.
Gene References into Functions
  1. Results show that NDUFS1 protein and mRNA levels are down-regulated in lung neoplasm and correlate with poor overall survival. PMID: 27516145
  2. High NDUFS1 expression is associated with cognitive impairment in lung cancer. PMID: 26987334
  3. Results found nominal significant associations of 2 SNPs in the NDUFS1 gene and 4 SNPs in the NDUFS2 gene with early onset schizophrenia (EOS), but none of these associations survived the Bonferroni correction. PMID: 26053550
  4. Loss of FOXRED1, coupled with protein, choline and/or folate-deficient diets results in the depletion of glutathione, the dysregulation of nitric oxide metabolism and the peroxynitrite-mediated inactivation of complex I. PMID: 26235939
  5. NDUFS1 may confer susceptibility to schizophrenia in male subjects, acting as a causative factor for the severity of negative symptoms in schizophrenia. PMID: 25354934
  6. The presented clinical courses of NDUFV1 and NDUFS1 mutation-based complex I deficiencies are characterized by leukoencephalopathy or early death and expand the already heterogeneous phenotypic spectrum. PMID: 25615419
  7. Some mutations in NDUFS1 cause a milder phenotype with a more benign course despite the initial decompensation phase. Homozygosity for the c.755A > G missense mutation may correlate with the milder clinical picture in the patient. PMID: 24952175
  8. The peripheral leukocyte oxidative phosphorylation enzyme activity assay was found to be a reliable method for the diagnosis of mitochondrial diseases. PMID: 21540367
  9. A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration. PMID: 22360420
  10. homozygous c.1783A>G (p.Thr595Ala) mutation in NDUFS1 in two inbred siblings with isolated complex I deficiency associated to a progressive cavitating leukoencephalopathy PMID: 21203893
  11. data suggest that gamma oscillations are especially energy demanding and require both high complex I expression and strong functional performance of mitochondria. PMID: 21183487
  12. report 3 patients with low residual complex I activity who displayed novel mutations in the NDUFS1 gene. One mutation introduces a premature stop codon, 3 mutations cause a substitution of amino acids and another mutation a deletion of one amino acid. PMID: 20382551
  13. Mutations in electron Transport Complex I is associated with Leber hereditary optic neuropathy failing to compensate for impaired oxidative phosphorylation. PMID: 19836344
  14. A patient with Leigh syndrome had a mutation in the NDUFS1 protein of Complex I of the Respiratory Chain. Identifying nuclear mutations will help us understand how molecular defects can lead to complex I deficiency. PMID: 15824269
  15. mutations in the NDUFS1 and NDUFS4 genes of complex I cause dysfunction in cellular oxidative metabolism PMID: 16478720
  16. This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia. PMID: 19405953

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Involvement in disease
Mitochondrial complex I deficiency (MT-C1D)
Subcellular Location
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Protein Families
Complex I 75 kDa subunit family
Database Links

HGNC: 7707

OMIM: 157655

KEGG: hsa:4719

STRING: 9606.ENSP00000392709

UniGene: Hs.471207

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