Recombinant Escherichia coli Septum site-determining protein MinD (minD)

Code CSB-YP360190ENV
MSDS
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Source Yeast
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Code CSB-EP360190ENV
MSDS
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Source E.coli
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Code CSB-EP360190ENV-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-BP360190ENV
MSDS
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Source Baculovirus
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Code CSB-MP360190ENV
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
minD
Uniprot No.
Alternative Names
minD; b1175; JW1164; Septum site-determining protein MinD; Cell division inhibitor MinD
Species
Escherichia coli (strain K12)
Expression Region
2-270
Target Protein Sequence
ARIIVVTSG KGGVGKTTSS AAIATGLAQK GKKTVVIDFD IGLRNLDLIM GCERRVVYDF VNVIQGDATL NQALIKDKRT ENLYILPASQ TRDKDALTRE GVAKVLDDLK AMDFEFIVCD SPAGIETGAL MALYFADEAI ITTNPEVSSV RDSDRILGIL ASKSRRAENG EEPIKEHLLL TRYNPGRVSR GDMLSMEDVL EILRIKLVGV IPEDQSVLRA SNQGEPVILD INADAGKAYA DTVERLLGEE RPFRFIEEEK KGFLKRLFGG
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.

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Target Background

Function
ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.
Gene References into Functions
  1. a membrane anchored MinC/MinD complex is targeted to the Z ring through the conserved carboxy tail of FtsZ leading to breakage of FtsZ filaments. PMID: 26268537
  2. The authors observed regular end-to-end oscillation over very short distances along the long axes of minicells, supporting the importance of geometry in MinD localization. PMID: 20543068
  3. average ATP consumption rate per unit length, which is proportional to the ATP consumption rate per MinD, increases with cell length until the transition from stochastic switching to regular oscillations and then remains roughly constant. PMID: 20308588
  4. there are rapid and substantial increases in the average MinD oscillation periods in the presence of any of the polyvalent cations Ca++, Mg++, protamine and gentamicin PMID: 19789705
  5. ATPase activity of MinD activated by positioning of MinE binding site on MinD surface during division site selection. PMID: 15458408
  6. lys 11 required for interaction of MinD with membrane, MinC, MinE & itself; the 3 residues in helix 7 that interact with lys 11 not required for binding to the membrane, activation of MinC or binding MinE but are required for MinE to stimulate MinD ATPase PMID: 15629934
  7. the Min proteins are capable of establishing an axis of oscillation that is the initial step in establishment of polarity in spherical cells PMID: 16262780
  8. it was observed that the oscillation period of MinD within rod-like and filamentous cells of Escherichia coli varied by a factor of 4 in the temperature range from 20 degrees C to 40 degrees C PMID: 16936014
  9. In vivo measurements of the mobility of MinD and MinE using fluorescence correlation spectroscopy shows 2 distinct timescales; the diffusion constant of cytoplasmic MinD to be approximately 16 microm(2) s(-1). PMID: 17200601
  10. Min proteins undergo a periodic pole-to-pole oscillation that involves polymerization and ATPase activity of MinD under the controlling influence of MinE. PMID: 17483175
  11. Reports show that both MinD and FtsZ readily assembled on intracytoplasmic membrane surfaces, and this contributes significantly to the lethal division block seen in all shape mutants under nonpermissive conditions. PMID: 17993535
  12. Overproduction of MinC in the presence of MinD inhibits assembly of Z rings. PMID: 19415799

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Subcellular Location
Cell inner membrane; Peripheral membrane protein.
Protein Families
ParA family, MinD subfamily
Database Links
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