Recombinant Escherichia coli DNA polymerase III subunit tau (dnaX)

Code CSB-YP356921ENV
MSDS
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Source Yeast
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Code CSB-EP356921ENV
MSDS
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Source E.coli
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Code CSB-EP356921ENV-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-BP356921ENV
MSDS
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Source Baculovirus
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Code CSB-MP356921ENV
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
dnaX
Uniprot No.
Alternative Names
dnaX; dnaZ; dnaZX; b0470; JW0459; DNA polymerase III subunit tau; EC 2.7.7.7; DNA polymerase III subunit gamma
Species
Escherichia coli (strain K12)
Expression Region
2-643
Target Protein Sequence
SYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG KTSIARLLAK GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK VEDTRDLLDN VQYAPARGRF KVYLIDEVHM LSRHSFNALL KTLEEPPEHV KFLLATTDPQ KLPVTILSRC LQFHLKALDV EQIRHQLEHI LNEEHIAHEP RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM LGTLDDDQAL SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE MTLLRALAFH PRMPLPEPEV PRQSFAPVAP TAVMTPTQVP PQPQSAPQQA PTVPLPETTS QVLAARQQLQ RVQGATKAKK SEPAAATRAR PVNNAALERL ASVTDRVQAR PVPSALEKAP AKKEAYRWKA TTPVMQQKEV VATPKALKKA LEHEKTPELA AKLAAEAIER DPWAAQVSQL SLPKLVEQVA LNAWKEESDN AVCLHLRSSQ RHLNNRGAQQ KLAEALSMLK GSTVELTIVE DDNPAVRTPL EWRQAIYEEK LAQARESIIA DNNIQTLRRF FDAELDEESI RPI
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
Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open them at one interface. Primed DNA is recognized, ATP is hydrolyzed releasing the gamma complex and closing the beta sliding clamp ring around the primed DNA.; serves as a scaffold to trimerize the core complex.; interacts with the delta and delta' subunits to transfer the beta subunit on the DNA. Interacts with ATP, drives ATP-induced conformational changes in the gamma complex that opens the beta sliding clamp ring. After loading of primed DNA ATP is hydrolyzed and the beta sliding clamp ring closes.
Gene References into Functions
  1. study characterized the dnaXE145A clamp loader mutant; found that the naturally occurring obstacles encountered by a replication fork are not tackled in a proper way by the mutant clamp loader and suggest a role for the clamp loader in the restart of stalled replication forks PMID: 28947673
  2. Ribosome frameshifting during translation of bacterial dnaX can proceed via different routes, generating a variety of distinct polypeptides. PMID: 28525745
  3. Data show that expression from DNA polymerase III dnaX to produce gamma subunit is essential for normal cellular function. PMID: 26786318
  4. Destabilization of the single-stranded DNA-chi subunit of DNA polymerase III complex in vivo produces cells with temperature- dependent cell cycle defects that appear to arise from replisome instability. PMID: 21857649
  5. Analyzing DnaX complexes containing one or more K51E variant DnaX subunits demonstrated that only one active ATP binding site is required to form initiation complexes, but the two additional sites increase the rate by ca 1000-fold. PMID: 21820444
  6. Only one ATP-binding DnaX subunit is required for initiation complex formation by the Escherichia coli DNA polymerase III holoenzyme. PMID: 20675375
  7. tau subunit plays an important role in determining the fidelity of the chromosomal replication, specifically in the avoidance of transversions and frameshift mutations. PMID: 16430690
  8. data suggest that the unstructured C-terminus of tau subunit of Escherichia coli DNA polymerase III holoenzyme becomes folded into a helix-loop-helix in its complex with alpha subunit. PMID: 17355988
  9. The interaction site of protein domains of of the tau subunit of Escherichia coli DNA polymerase III on the alpha subunit was mapped by NMR experiments. PMID: 17452361
  10. Data support the assumption that dnaX36-mediated mutations originate as errors of replication rather than DNA damage-related events. PMID: 18156258
  11. The DNA polymerase III clamp loading reaction can be divided into two stages: formation of a ternary clamp loader.clamp.DNA complex, and decay of the ternary complex to produce a clamp.DNA complex. Clamp release is likely to be the rate-limiting step. PMID: 19663416

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Protein Families
DnaX/STICHEL family
Database Links
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