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Mouse Anti-DHPS Recombinant Antibody (EG959) (CBMAB-EN1138-LY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
EG959
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 70-369 mapping at the C-terminus of human DHS.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
Gelatin & PBS
Preservative
Sodium Azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Deoxyhypusine Synthase
Introduction
This gene encodes a protein that is required for the formation of hypusine, a unique amino acid formed by the posttranslational modification of only one protein, eukaryotic translation initiation factor 5A. The encoded protein catalyzes the first step in hypusine formation by transferring the butylamine moiety of spermidine to a specific lysine residue of the eukaryotic translation initiation factor 5A precursor, forming an intermediate deoxyhypusine residue. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, May 2011]
Entrez Gene ID
1725
UniProt ID
P49366
Alternative Names
Deoxyhypusine Synthase; Migration-Inducing Gene 13; EC 2.5.1.46; DHS; DS; EC 2.5.1; MIG13;
Function
Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue (PubMed:30661771).

This is the first step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function.
Biological Process
Peptidyl-lysine modification to peptidyl-hypusine Source: UniProtKB
Positive regulation of cell population proliferation Source: ProtInc
Spermidine metabolic process Source: UniProtKB
Translation Source: ProtInc
Cellular Location
Cytosol; Cytoplasm
Involvement in disease
Neurodevelopmental disorder with seizures and speech and walking impairment (NEDSSWI):
An autosomal recessive disorder characterized by global developmental delay with intellectual disability and poor speech acquisition, and walking difficulties due to hypotonia, hypertonia, spasticity, or poor coordination. Additional features include seizures, mild dysmorphic features, and variable short stature.
More Infomation

Kar, R. K., Hanner, A. S., Starost, M. F., Springer, D., Mastracci, T. L., Mirmira, R. G., & Park, M. H. (2021). Neuron-specific ablation of eIF5A or deoxyhypusine synthase leads to impairments in growth, viability, neurodevelopment, and cognitive functions in mice. Journal of Biological Chemistry, 297(5).

Padgett, L. R., Robertson, M. A., Anderson‐Baucum, E. K., Connors, C. T., Wu, W., Mirmira, R. G., & Mastracci, T. L. (2021). Deoxyhypusine synthase, an essential enzyme for hypusine biosynthesis, is required for proper exocrine pancreas development. The FASEB Journal, 35(5), e21473.

Anderson-Baucum, E., Piñeros, A. R., Kulkarni, A., Webb-Robertson, B. J., Maier, B., Anderson, R. M., ... & Mirmira, R. G. (2021). Deoxyhypusine synthase promotes a pro-inflammatory macrophage phenotype. Cell Metabolism, 33(9), 1883-1893.

Kar, R. K., Hanner, A. S., Starost, M. F., Springer, D., Mastracci, T. L., Mirmira, R. G., & Park, M. H. (2021). Neuron specific ablation of eIF5A or deoxyhypusine synthase leads to impairment in development and cognitive functions in mice. bioRxiv.

Liu, K. L., Li, X. Y., Wang, D. P., Xue, W. H., Qian, X. H., Li, Y. H., ... & Meng, F. H. (2021). Novel Allosteric Inhibitors of Deoxyhypusine Synthase against Malignant Melanoma: Design, Synthesis, and Biological Evaluation. Journal of Medicinal Chemistry, 64(18), 13356-13372.

Tanaka, Y., Kurasawa, O., Yokota, A., Klein, M. G., Ono, K., Saito, B., ... & Imamura, S. (2020). Discovery of novel allosteric inhibitors of deoxyhypusine synthase. Journal of Medicinal Chemistry, 63(6), 3215-3226.

Tanaka, Y., Kurasawa, O., Yokota, A., Klein, M. G., Saito, B., Matsumoto, S., ... & Imamura, S. (2020). New series of potent allosteric inhibitors of deoxyhypusine synthase. ACS Medicinal Chemistry Letters, 11(8), 1645-1652.

Ganapathi, M., Padgett, L. R., Yamada, K., Devinsky, O., Willaert, R., Person, R., ... & Chung, W. K. (2019). Recessive rare variants in deoxyhypusine synthase, an enzyme involved in the synthesis of hypusine, are associated with a neurodevelopmental disorder. The American Journal of Human Genetics, 104(2), 287-298.

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For research use only. Not intended for any clinical use.

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