DPH2 antibody

Este producto es parte de DPH - diphthamide biosynthesis
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935106861
info@markelab.com
name
DPH2 antibody
category
Primary Antibodies
provider
FineTest
reference
FNab02516
tested applications
ELISA, WB, IHC, IP, IF

Description

Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2(EEF2).

Documents del producto

Instrucciones
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Data sheet
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Product specifications

Category
Primary Antibodies
Immunogen Target
DPH2 homolog (DPH2)
Host
Rabbit
Reactivity
Human, Mouse
Recommended Dilution
WB: 1:500-1:2000; IP: 1:200-1:2000; IHC: 1:20-1:200; IF: 1:20-1:200
Clonality
polyclonal
Conjugation
Unconjugated
Isotype
IgG
Observed MW
52kd
Purity
≥95% as determined by SDS-PAGE
Purification
Immunogen affinity purified
Size 1
100µg
Form
liquid
Tested Applications
ELISA, WB, IHC, IP, IF
Storage
PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.)
UniProt ID
Q9BQC3
Gene ID
1802
Alias
DPH2L2,DEDSSH2,Diphthamide biosynthesis protein 2,Diphtheria toxin resistance protein 2
Background
Antibody anti-DPH2
Status
RUO
Note
Mol. Weight 52 kDa

Descripción

DPH2 is an essential enzyme that works in concert with DPH1 to catalyze the first step of diphthamide biosynthesis on eukaryotic elongation factor 2 (eEF2), forming a critical intermediate for subsequent modifications. It interacts directly with DPH1 to mediate the transfer of a 3-amino-3-carboxypropyl group from S-adenosylmethionine (SAM) to the imidazole ring of a specific histidine residue. DPH2 mutations are associated with defects in protein translation fidelity and resistance to diphtheria toxin, as this toxin specifically targets diphthamide. Structural studies of DPH2 reveal conserved binding sites for SAM, emphasizing its central role in catalytic function. In addition to its enzymatic role, DPH2 is required for maintaining normal cellular physiology, particularly in protein synthesis and stress responses. DPH2 expression is tightly regulated and primarily localized in the cytoplasm, where it coordinates with other diphthamide biosynthesis factors. Deficiencies in DPH2 activity result in incomplete diphthamide synthesis, impacting cellular growth and proliferation. Its evolutionary conservation highlights its critical role in cellular and organismal viability.

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