Recombinant Rubredoxin protein (His tag) is a Clostridium pasteurianum Full Length protein, in the 1 to 54 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
>90% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE
No
M K K Y T C T V C G Y I Y N P E D G D P D N G V N P G T D F K D I P D D W V C P L C G V G K D Q F E E V E E
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
Rubredoxin, Rd
Recombinant Rubredoxin protein (His tag) is a Clostridium pasteurianum Full Length protein, in the 1 to 54 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
>90% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE
No
No
Clostridium pasteurianum
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
M K K Y T C T V C G Y I Y N P E D G D P D N G V N P G T D F K D I P D D W V C P L C G V G K D Q F E E V E E
Full Length
22 kDa
1 to 54
Recombinant
His tag N-Terminus
Liquid
Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
Belongs to the rubredoxin family.
Blue Ice
-20°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This supplementary information is collated from multiple sources and compiled automatically.
Rubredoxin also known by fewer alternate names is a small iron-sulfur protein involved in electron transfer processes. The protein which has a molecular mass of approximately 5.8 kDa contains an iron atom coordinated by four cysteine residues forming a simple robust structure. Rubredoxin is found mainly in anaerobic and some facultative anaerobic bacteria particularly in certain thermophilic and hyperthermophilic organisms. This protein plays an important mechanical role in facilitating electron transfer by cycling between oxidized and reduced states essential for various metabolic actions in these organisms.
The key function of rubredoxin lies in its participation as an electron carrier. It is involved in the biological reduction processes possibly functioning within larger electron transfer chains. Rubredoxin is often found associated with membrane-bound proteins or complexes in its native cellular environment although it can function independently as well. Its ability to shuttle electrons enables metabolic energy conversion playing a role in maintaining cell homeostasis and supporting energy production particularly in extreme environmental conditions inhabited by the host bacteria.
Rubredoxin contributes to important metabolic frameworks such as the electron transport chain and oxidative phosphorylation. It transfers electrons to and from other redox proteins enabling efficient energy transformation. Rubredoxin-related pathways interact closely with other proteins like cytochrome P450 and alcohol dehydrogenase thereby supporting diverse biochemical reactions. These interactions highlight the protein's versatility and its integration into broader enzymatic pathways that regulate cellular redox states.
Rubredoxin's relation primarily emerges in the context of host-pathogen interactions and adaptations in extreme environments. Organisms expressing rubredoxin can survive under harsh conditions which are detrimental to human health such as those seen in methanogens or extreme thermophiles. While not directly linked to human diseases its structural homologues like ferredoxin are implicated in disorders related to disrupted electron transport or oxidative stress illustrating the broader relevance of electron carrier proteins in disease mechanisms.
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis of ab225597 with 5% enrichment gel and 15% separation gel.
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