Recombinant Escherichia coli DnaA-homolog protein hda (hda)

Code CSB-YP304878ENV
MSDS
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Source Yeast
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Code CSB-EP304878ENV
MSDS
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Source E.coli
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Code CSB-EP304878ENV-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-BP304878ENV
MSDS
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Source Baculovirus
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Code CSB-MP304878ENV
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
hda
Uniprot No.
Alternative Names
hda; idaB; yfgE; b2496; JW5397; f248cDnaA regulatory inactivator Hda; DnaA paralog; Dp
Species
Escherichia coli (strain K12)
Expression Region
1-233
Target Protein Sequence
MNTPAQLSLP LYLPDDETFA SFWPGDNSSL LAALQNVLRQ EHSGYIYLWA REGAGRSHLL HAACAELSQR GDAVGYVPLD KRTWFVPEVL DGMEHLSLVC IDNIECIAGD ELWEMAIFDL YNRILESGKT RLLITGDRPP RQLNLGLPDL ASRLDWGQIY KLQPLSDEDK LQALQLRARL RGFELPEDVG RFLLKRLDRE MRTLFMTLDQ LDRASITAQR KLTIPFVKEI LKL
Protein Length
full length 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.
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
Mediates the interactions of DNA replication initiator protein DnaA with DNA polymerase subunit beta sliding clamp (dnaN). Stimulates hydrolysis of ATP-DnaA to ADP-DnaA, rendering DnaA inactive for reinitiation, a process called regulatory inhibition of DnaA or RIDA. ADP-binding activates Hda to hydrolyze DnaA-ATP; Hda monomers bind to ADP with about 200-fold greater affinity than for ATP. RIDA function can be genetically separated from viability, suggesting this protein has another function as well.; Suppresses the toxic effect of overexpressing a TrfA N-terminal 163 residue fragment. Inhibits inner membrane-associated plasmid IncP-alpha RK2 replication probably by interacting with plasmid-encoded TrfA.
Gene References into Functions
  1. structural and mutational analyses of the Hda-beta clamp complex indicate that the interaction of the beta clamp with Hda controls the ability of Hda to interact with DnaA. PMID: 28168278
  2. results establish a model in which interaction between DnaA Asn-44 and Hda stabilizes the association between the AAA+ domains of DnaA and Hda to facilitate DnaA-ATP hydrolysis during RIDA(regulatory inactivation of DnaA) PMID: 23679057
  3. Taken together, these findings suggest that although one or more Hda functions are essential for cell viability, regulatory inactivation of DnaA may be dispensable. PMID: 22716942
  4. functional DnaA-Hda interactions require a second interaction site within DnaA domain IV in addition to the AAA+ domain PMID: 21708944
  5. Here, the authors demonstrate that direct and functional interaction of ADP-Hda with DnaA requires the Hda residues Ser-152, Phe-118 and Asn-122 as well as Hda Arg-153 and DnaA Arg-334. PMID: 20132442
  6. data suggest the model: DnaA-ATP is hydrolyzed at a binding interface between the AAA(+) domains of DnaA and Hda; the DnaA N-terminal domain supports this interaction; the interaction of DnaA-ATP with the Hda-clamp complex occurs in a catalytic mode PMID: 15611053
  7. Inactivation of active ATP-DnaA by the Hda protein and the sliding clamp of the polymerase was found to be required to prevent reinitiation and asynchrony of replication. PMID: 15939703
  8. Hda inactivaes DnaA, which prevents hyperinitiation of Escherichia coli DNA replication PMID: 16041320
  9. Overexpression of the Hda DnaA-related protein in Escherichia coli inhibits multiplication, affects membrane permeability, and induces the SOS response. PMID: 16321957
  10. The presence of genes encoding a previously unpublished adhesin termed Hda was found in several EAEC strains isolated from Denmark, suggesting that this adhesin represents an important variant in the Afa/Dr/AAF family. PMID: 18443096
  11. Hda monomerization by ADP binding promotes replicase clamp-mediated DnaA-ATP hydrolysis PMID: 18977760
  12. Mutations that reduce initiation frequency from oriC suppress the growth defect of Hda-deficient cells. PMID: 19007419

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Subcellular Location
Cell inner membrane. Note=More protein is found in the inner than outer membrane fractions.
Protein Families
DnaA family, HdA subfamily
Database Links
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