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Recombinant Escherichia coli Small-conductance mechanosensitive channel (mscS), partial

Recombinant Escherichia coli Small-conductance mechanosensitive channel (mscS), partial

Code	CSB-YP314762ENV1
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP314762ENV1
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP314762ENV1-B
MSDS	MSDS
Size	Pls inquire
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-BP314762ENV1
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP314762ENV1
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

mscS

Uniprot No.

P0C0S1

Alternative Names

mscS; yggB; b2924; JW2891; Small-conductance mechanosensitive channel

Species

Escherichia coli (strain K12)

Protein Length

Partial

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

Protein 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

Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds.

Gene References into Functions

inactivation process of wild-type MscS was strongly affected by voltage. The wild-type MscS inactivated at +60 to +80 mV but not at -60 to +40 mV. PMID: 28101504
Mutations in a conserved domain of E. coli MscS to the most conserved superfamily residue leads to kinetic changes. PMID: 26340270
Molecular dynamics and biophysical analyses show that the volume of the pockets and thus the number of lipid acyl chains within them decreases upon channel opening. PMID: 26551077
Data show that trifluoroethanol (TFE) affects mechanosensitive channel of small conductance (MscS) channel gating kinetics in spheroplasts and liposomes. PMID: 26116700
Data indicate that mechanosensitive channel of small conductance (MscS) protein opens in response to a relief of intrinsic lipid bilayer pressure. PMID: 25450806
We report here crystal structures of MscS from E. coli and Helicobacter pylori solubilized in the detergent beta-dodecylmaltoside at resolutions of 4.4 and 4.2 A, respectively. PMID: 23339071
Article reviews the science that led to the isolation and identification of MscS. structure-function relationship of the channel, in particular the structural and biochemical approaches to understanding channel gating. [Review] PMID: 22404681
Data show that the MscL/MscS threshold ratio dramatically decreased in thinner compared with thicker bilayers. PMID: 22586095
Tension dependencies of both inactivation and recovery rates suggest the spatial scale of the inactivating transition, which guides the modeling of the inactivated state of MscS. PMID: 21670207
Both F68S and L111S in MscS substitutions produced severe loss-of-function phenotypes in vivo by increasing the inactivation rate and promoting unusual 'silent' inactivation from the resting state PMID: 20208543
the crystal structure of MscS does not represent an open state; MscS gate involves a vapor-lock mechanism where limited changes of geometry or surface polarity can locally switch the regime between water-filled (conducting)& empty (nonconducting) states PMID: 15111405
The crystal structure of MscS reveals a homoheptamer with three transmembrane segments and a large cytoplasmic domain PMID: 17500538
Analysis of the fluorescence properties of purified mutant MscS proteins containing single Trp residues revealed that W16 and W251 are relatively inaccessible, whereas W240 is accessible to quenching agents. PMID: 17718516
Transition to this unique mechanosensitive channel state is discussed in terms of existing data. PMID: 18065458
study presents a 3.45 angstrom-resolution structure for the MscS channel in an open conformation; structure suggests a molecular mechanism that underlies MscS gating and its decay of conductivity during prolonged activation PMID: 18755969
determination of structural rearrangements associated with MscS activation in membranes; transition from closed to open state is accompanied by downward tilting of the transmembrane TM1-TM2 hairpin & by expansion, tilt & rotation of the TM3 helices PMID: 18755978
MscL and MscS are tangible models for studying conformational transitions in membrane proteins driven directly by membrane tension. PMID: 19383606