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Recombinant Mouse Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (Cox4i1), partial

Recombinant Mouse Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (Cox4i1), partial

Code: CSB-EP005832MO1

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Size:

20ug100ug1mg

US$306

Quantity:

Express system: E.coli

Species: Mus musculus (Mouse)

Tag Info: C-terminal 6xHis-tagged

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Product Details
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Target Background

Product Details

Purity

Greater than 95% as determined by SDS-PAGE.

Target Names

Cox4i1

Uniprot NO.

P19783

Research Area

Others

Species

Mus musculus (Mouse)

Source

E.coli

Expression Region

23-98aa

Target Protein Sequence

AHGSVVKSEDYAFPTYADRRDYPLPDVAHVTMLSASQKALKEKEKADWSSLSRDEKVQLYRIQFNESFAEMNRGTN
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

15.6 kDa

Protein Length

Partial

Tag Info

C-terminal 6xHis-tagged
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

Liquid or 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

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

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.

Storage

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.

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.

Troubleshooting and FAQs

Protein FAQs

Datasheet & COA

Please contact us to get it.

Images

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Customer Reviews and Q&A

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Target Background

Function(From Uniprot)

Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunbit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.

Gene References into Functions

exercise training caused an increase in mRNA and protein levels of COXIV, whereas NAC intervention lowered the two so significantly that even exercise training could not reverse the effect of NAC intervention PMID:26159509
Data suggest that that obesity affects both sperm and seminal plasma composition; Cox4i1 mRNA is up-regulated in spermatozoa of obese mice compared to control mice. PMID:25731709
Our data suggest that MPP(+) acts on astrocytes in a sex- and brain region-specific manner involving cytochrome c oxidase isoform expression in an impairment of energy production and elevated oxidative stress levels PMID:21598289
Knockdown of small interfering RNA-mediated COX subunit IV decreases progesterone synthesis in steroidogenic cells. PMID:21558439
Under conditions of reduced oxygen availability, hypoxia-inducible factor 1 reciprocally regulates COX4 subunit expression by activating transcription of the genes encoding COX4-2 and LON, a mitochondrial protease that is required for COX4-1 degradation. PMID:17418790