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AB202133

Anti-DHPS/DHS antibody

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(2 Publications)

Rabbit Polyclonal DHPS/DHS antibody. Suitable for WB and reacts with Human, Mouse, Rat samples. Cited in 2 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human DHPS.

View Alternative Names

DS, DHPS, Deoxyhypusine synthase, DHS

1 Images
Western blot - Anti-DHPS/DHS antibody (AB202133)
  • WB

Supplier Data

Western blot - Anti-DHPS/DHS antibody (AB202133)

All lanes:

Western blot - Anti-DHPS/DHS antibody (ab202133) at 1/500 dilution

Lane 1:

MCF7 cell extract

Lane 2:

BT474 cell extract

Lane 3:

293T cell extract

Lane 4:

Jurkat cell extract

Lane 5:

SGC7901 cell extract

Lane 6:

Mouse testis cell extract

Lane 7:

Mouse brain cell extract

Lane 8:

Mouse skeletal muscle cell extract

Lane 9:

Rat brain cell extract

Predicted band size: 41 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Rat, Human

Applications

WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Human DHPS.

P49366

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/2000", "WB-species-notes": "<p></p>" }, "Mouse": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/2000", "WB-species-notes": "<p></p>" }, "Rat": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/2000", "WB-species-notes": "<p></p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.3 Preservative: 0.02% Sodium azide Constituents: 50% Glycerol (glycerin, glycerine), 49% PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The dihydropteroate synthase (DHPS) also known as dihydropteroate synthase (synonymously notated as 'DHPS/DHS') is an enzyme that catalyzes the condensation of para-aminobenzoic acid (pABA) with pterin pyrophosphate to form dihydropteroate an important intermediate in folate biosynthesis. It possesses a molecular mass of approximately 30 kDa. This enzyme is known to be expressed in a diverse range of prokaryotic organisms certain lower eukaryotes and plants playing an important role in the folate biosynthesis pathways essential for cellular processes.
Biological function summary

Dihydropteroate synthase serves a fundamental role in the synthesis of folic acid a critical cofactor in the transfer of one-carbon units in cellular metabolism. DHPS functions within the larger multi-enzyme complex of folate synthesis. The enzyme's activity directly influences the production of tetrahydrofolate (THF) which is critical in nucleic acid and amino acid biosynthesis thereby impacting cell growth and replication in these organisms.

Pathways

DHPS plays an essential role in the folate biosynthesis and subsequent nucleotide biosynthesis pathways. The DHPS enzyme's activity directly affects the folate cycle by producing dihydropteroate a precursor to tetrahydrofolate. Proteins such as dihydrofolate reductase (DHFR) are closely related within these biological pathways facilitating the eventual reduction of dihydrofolate to THF therefore enabling critical biosynthetic reactions necessary for cell viability.

DHPS activity is notably implicated in bacterial resistance to sulfonamide antibiotics which target and inhibit DHPS function to disrupt folate synthesis. This enzyme's presence and alteration are associated with infections caused by sulfonamide-resistant bacteria including Streptococcus pneumoniae and Plasmodium falciparum. In these instances the protein interacts or associates with enzymes like DHFR which can likewise mutate to confer resistance complicating treatment strategies and necessitating the development of novel therapeutic approaches to target resistant strains effectively.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

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.
See full target information DHPS
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Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Cell reports 33:108510 PubMed33326776

2020

Hypusination Orchestrates the Antimicrobial Response of Macrophages.

Applications

Unspecified application

Species

Unspecified reactive species

Alain P Gobert,Jordan L Finley,Yvonne L Latour,Mohammad Asim,Thaddeus M Smith,Thomas G Verriere,Daniel P Barry,Margaret M Allaman,Alberto G Delagado,Kristie L Rose,M Wade Calcutt,Kevin L Schey,Johanna C Sierra,M Blanca Piazuelo,Raghavendra G Mirmira,Keith T Wilson

Scientific reports 9:1533 PubMed30733517

2019

eIF5A inhibition influences T cell dynamics in the pancreatic microenvironment of the humanized mouse model of Type 1 Diabetes.

Applications

Unspecified application

Species

Unspecified reactive species

Shahnawaz Imam,R Prathibha,Pervaiz Dar,Khalil Almotah,Ahmed Al-Khudhair,Syed Abdul-Moiz Hasan,Nancy Salim,Talha Naser Jilani,Raghavendra G Mirmira,Juan Carlos Jaume
View all publications
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