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Addgene

pCIneo-PAM-sig-His6-gamma-PALcc-deltaGlyc
(Plasmid #25458)

Full plasmid sequence is not available for this item.

Ordering

This material is available to academics and nonprofits only.
Item Catalog # Description Quantity Price (USD)
Plasmid 25458 Standard format: Plasmid sent in bacteria as agar stab 1 $85

Backbone

  • Vector backbone
    pCI-neo
  • Backbone manufacturer
    Promega
  • Backbone size w/o insert (bp) 5472
  • Vector type
    Mammalian Expression
  • Selectable markers
    Neomycin (select with G418)

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
    PAM
  • Alt name
    peptidyl-alpha-hydroxyglycine alpha-amidating lyase
  • Species
    R. norvegicus (rat)
  • Insert Size (bp)
    966
  • Mutation
    Contains aa 498-820 (PALcc= PAL catalytic core) Serine 767 mutated to Alanine (delta Glyc)
  • Entrez Gene
    Pam (a.k.a. PHM)
  • Tags / Fusion Proteins
    • PAM signal (N terminal on insert)
    • His6 (N terminal on insert)

Cloning Information

  • Cloning method Restriction Enzyme
  • 5′ cloning site NheI (not destroyed)
  • 3′ cloning site XmaI (not destroyed)
  • 5′ sequencing primer T7, CMV-F
  • 3′ sequencing primer T3
  • (Common Sequencing Primers)

Terms and Licenses

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

    pCIneo-PAM-sig-His6-gamma-PALcc-deltaGlyc was a gift from Betty Eipper (Addgene plasmid # 25458 ; http://n2t.net/addgene:25458 ; RRID:Addgene_25458)
  • For your References section:

    Amidation of bioactive peptides: the structure of the lyase domain of the amidating enzyme. Chufan EE, De M, Eipper BA, Mains RE, Amzel LM. Structure. 2009 Jul 15. 17(7):965-73. 10.1016/j.str.2009.05.008 PubMed 19604476