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Bov.hsc70.T77.A1-386.wt
(Plasmid #12534)

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This material is available to academics and nonprofits only.
Item Catalog # Description Quantity Price (USD)
Plasmid 12534 Standard format: Plasmid sent in bacteria as agar stab 1 $85
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Backbone

  • Vector backbone
    pT7-7
  • Backbone manufacturer
    William Studier
  • Backbone size w/o insert (bp) 2500
  • Vector type
    Bacterial Expression

Growth in Bacteria

  • Bacterial Resistance(s)
    Ampicillin, 100 μg/mL
  • Growth Temperature
    37°C
  • Growth Strain(s)
    DH5alpha
  • Copy number
    High Copy

Gene/Insert

  • Gene/Insert name
    Bovine 70 kDa heat shock protein ATPase fragment
  • Alt name
    ATPase fragment, bovine Hsc70
  • Species
    B. taurus (bovine)
  • Insert Size (bp)
    1158
  • Mutation
    deletion of residues 387-650 of bovine Hsc70 protein

Cloning Information

  • Cloning method Restriction Enzyme
  • 5′ cloning site NdeI (unknown if destroyed)
  • 3′ cloning site XbaI (unknown if destroyed)
  • 5′ sequencing primer T7
    • (Common Sequencing Primers)

Terms and Licenses

  • Academic/Nonprofit Terms
  • Industry Terms
    • Not Available to Industry
Trademarks:
  • Zeocin® is an InvivoGen trademark.

Depositor Comments

Also see Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment. In J Biol Chem. 1994 Apr 29. 269(17):12899-907. (Pubmed: 8175707).

How to cite this plasmid ( Back to top)

These plasmids were created by your colleagues. Please acknowledge the Principal Investigator, cite the article in which the plasmids were described, and include Addgene in the Materials and Methods of your future publications.

  • For your Materials & Methods section:

    Bov.hsc70.T77.A1-386.wt was a gift from David McKay (Addgene plasmid # 12534 ; http://n2t.net/addgene:12534 ; RRID:Addgene_12534)

  • For your References section:

    Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants. Wilbanks SM, DeLuca-Flaherty C, McKay DB. J Biol Chem. 1994 Apr 29. 269(17):12893-8. PubMed 8175706
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