phd Antibody

Code CSB-PA312345XA01FTN
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Product Details

Full Product Name
Rabbit anti-Escherichia phage P1 (Bacteriophage P1) phd Polyclonal antibody
Uniprot No.
Target Names
phd
Alternative Names
phd antibody; Antitoxin phd antibody; Addiction protein pdh antibody; Prevent host death protein antibody
Raised in
Rabbit
Species Reactivity
Escherichia phage P1 (Bacteriophage P1)
Immunogen
Recombinant Escherichia phage P1 (Bacteriophage P1) phd protein
Immunogen Species
Escherichia phage P1 (Bacteriophage P1)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB (ensure identification of antigen)
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables
① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee
① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time
Made-to-order (14-16 weeks)

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Target Background

Function
Antitoxin component of a type II toxin-antitoxin (TA) system. A labile antitoxin that binds to cognate doc toxin and neutralizes its ability to phosphorylate host EF-Tu. Does not reverse phosphorylation. Bacteriophage P1 lysogenizes bacteria as a low-copy number plasmid; phd and doc proteins function in unison to stabilize plasmid number by inducing a lethal response to P1 plasmid prophage loss.; Binds to its own promoter repressing its expression; toxin doc acts as a corepressor or derepressor depending on the ratio, repressing or inducing expression.
Gene References into Functions
  1. The intrinsically disordered domain of the antitoxin Phd chaperones the toxin Doc against irreversible inactivation and misfolding. PMID: 25326388
  2. Four mutations (PhdA36H, V37A, I38A, and F44A) had major defects in repressor activity. Five mutations (PhdD53A, D53R, E55A, F56A, and F60A) had major defects in antitoxin activity. PMID: 15629948
  3. Results decribe the crystallization of Phd-Doc compelxes from bacteriophage P1. PMID: 18997335
Protein Families
PhD/YefM antitoxin family
Database Links

KEGG: vg:2777473

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