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AB155005

Anti-UGDH antibody

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(6 Publications)

Rabbit Polyclonal UGDH antibody. Suitable for IHC-P, WB, ICC/IF and reacts with Human, Mouse, Rat samples. Cited in 6 publications. Immunogen corresponding to Recombinant Fragment Protein within Human UDP-glucose 6-dehydrogenase aa 1 to C-terminus.

View Alternative Names

UDP-glucose 6-dehydrogenase, UDP-Glc dehydrogenase, UDP-GlcDH, UDPGDH, UGDH

6 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-UGDH antibody (AB155005)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-UGDH antibody (AB155005)

Immunohistochemical analysis of paraffin embedded Human hepatoma tissue labelling UGDH with ab155005 at a 1/500 dilution.

Immunocytochemistry/ Immunofluorescence - Anti-UGDH antibody (AB155005)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-UGDH antibody (AB155005)

Immunofluorescence analysis of HeLa cells fixed in 4% paraformaldehyde at RT for 15 min labelling UGDH protein using ab155005 at a 1/500 dilution (Green).

Western blot - Anti-UGDH antibody (AB155005)
  • WB

Supplier Data

Western blot - Anti-UGDH antibody (AB155005)

Samples were separated by 10% SDS-PAGE. Corresponding RNA expression data for the same cell lines are based on Human Protein Atlas program.

All lanes:

Western blot - Anti-UGDH antibody (ab155005) at 1/10000 dilution

Lane 1:

293T whole cell lysate at 30 µg

Lane 2:

A431 whole cell lysate at 30 µg

Lane 3:

HeLa whole cell lysate at 30 µg

Lane 4:

HepG2 whole cell lysate at 30 µg

Secondary

All lanes:

HRP-conjugated anti-rabbit IgG

Predicted band size: 55 kDa

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Western blot - Anti-UGDH antibody (AB155005)
  • WB

Unknown

Western blot - Anti-UGDH antibody (AB155005)

7.5 % SDS-PAGE

All lanes:

Western blot - Anti-UGDH antibody (ab155005) at 1/2000 dilution

All lanes:

rat liver lysate/extract at 50 µg

Predicted band size: 55 kDa

false

Western blot - Anti-UGDH antibody (AB155005)
  • WB

Unknown

Western blot - Anti-UGDH antibody (AB155005)

7.5% SDS PAGE

All lanes:

Western blot - Anti-UGDH antibody (ab155005) at 1/10000 dilution

All lanes:

mouse liver whole cell lysate at 50 µg

Predicted band size: 55 kDa

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Western blot - Anti-UGDH antibody (AB155005)
  • WB

CiteAb

Western blot - Anti-UGDH antibody (AB155005)

UGDH western blot using anti-UGDH antibody ab155005. Publication image and figure legend from Saito, T., Ichimura, Y., et al., 2016, Nat Commun, PubMed 27345495.

ab155005 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab155005 please see the product overview.

Persistent activation of Nrf2 in autophagy-deficient mouse livers.(a) Immunoblot analysis. Liver homogenates and nuclear fractions of female Atg7f/f, Atg7f/f;Alb-Cre, Atg7f/f;Nrf2f/f and Atg7f/f;Nrf2f/f;Alb-Cre mice aged at 5 weeks were prepared, and were subjected to immunoblot with the indicated antibodies. (b) Immunofluorescence analysis. Liver sections described in a were double-immunostained with a combination of anti-phosphorylated p62 (green) and anti-p62 (red) antibodies, or of anti-Keap1 (green) and anti-p62 (red) antibodies. Scale bars, 20 μm. (c) Nrf2-dependent gene expressions in autophagy-deficient livers. Total RNAs were prepared from livers of female Atg7f/f (n=4), Atg7f/f;Alb-Cre (n=4), Atg7f/f;Nrf2f/f (n=4) and Atg7f/f;Nrf2f/f;Alb-Cre mice (n=4) aged at 5 weeks. Values were normalized to the amount of mRNA in the livers of Atg7f/f or Atg7f/f;Nrf2f/f mice. The experiments were performed three times. Data are means±s.e. *p<0.05, **p<0.01 and ***p<0.001 as determined by the Welch t-test.

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Rat, Human

Applications

ICC/IF, IHC-P, WB

applications

Immunogen

Recombinant Fragment Protein within Human UDP-glucose 6-dehydrogenase aa 1 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

O60701

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.025% Proclin 300 Constituents: PBS, 20% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
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

Supplementary information

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

UDP-glucose 6-dehydrogenase also known as UGDH is an enzyme with a mass of approximately 53 kDa. It catalyzes the oxidation of UDP-glucose to UDP-glucuronic acid in humans. This enzyme plays an important mechanical role in the biosynthesis of glycosaminoglycans and is expressed in various tissues such as the liver kidneys and lungs. Alternate names for UGDH include UDP-GlcDH and UDPGDH frequently used in scientific literature.
Biological function summary

UDP-glucose 6-dehydrogenase contributes to the conversion processes for nucleotide sugar substrates and it is not reported to be part of a larger enzyme complex. It ensures the availability of UDP-glucuronic acid a necessary precursor for glycosaminoglycans which are components of the extracellular matrix and involved in cellular signaling. This activity supports processes like wound healing and tissue regeneration by maintaining structural integrity and facilitating cell-cell communication in various physiological contexts.

Pathways

UDP-glucose 6-dehydrogenase participates in the hexosamine biosynthetic pathway and the UDP-glucuronate pathway. In the hexosamine biosynthetic pathway it works alongside proteins like glutamine-fructose-6-phosphate transaminase to regulate the production of UDP-GlcNAc important for carbohydrate modifications of proteins and lipids. The UDP-glucuronate pathway involves related enzymes such as hyaluronan synthase which utilizes UDP-glucuronic acid generated by UGDH for synthesizing hyaluronan an important glycosaminoglycan in tissue hydration and lubrication.

Abnormal activity or expression of UDP-glucose 6-dehydrogenase links to cancer and fibrosis. Its role in producing glycosaminoglycans makes it significant in the tumor microenvironment and alterations in UGDH activity may support cancer progression by affecting cell adhesion and migration. In fibrosis overactivity of UGDH can lead to excessive glycosaminoglycan production contributing to tissue scarring. Interactions with proteins like hyaluronan synthase hint at potential therapeutic targets for modifying these extracellular matrix components in disease contexts.

Product protocols

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

Target data

Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed : 21502315, PubMed : 21961565, PubMed : 22123821, PubMed : 23106432, PubMed : 25478983, PubMed : 27966912, PubMed : 30420606, PubMed : 30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed : 32001716).
See full target information UDP-glucose 6-dehydrogenase

Publications (6)

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

EMBO reports 26:3384-3410 PubMed40437287

2025

KEAP1 retention in phase-separated p62 bodies drives liver damage under autophagy-deficient conditions.

Applications

Unspecified application

Species

Unspecified reactive species

Shuhei Takada,Nozomi Shinomiya,Gaoxin Mao,Hikaru Tsuchiya,Tomoaki Koga,Satoko Komatsu-Hirota,Yu-Shin Sou,Manabu Abe,Elena Ryzhii,Michitaka Suzuki,Mitsuyoshi Nakao,Satoshi Waguri,Hideaki Morishita,Masaaki Komatsu

The EMBO journal 42:e113349 PubMed37306101

2023

Phosphorylation of phase-separated p62 bodies by ULK1 activates a redox-independent stress response.

Applications

Unspecified application

Species

Unspecified reactive species

Ryo Ikeda,Daisuke Noshiro,Hideaki Morishita,Shuhei Takada,Shun Kageyama,Yuko Fujioka,Tomoko Funakoshi,Satoko Komatsu-Hirota,Ritsuko Arai,Elena Ryzhii,Manabu Abe,Tomoaki Koga,Hozumi Motohashi,Mitsuyoshi Nakao,Kenji Sakimura,Arata Horii,Satoshi Waguri,Yoshinobu Ichimura,Nobuo N Noda,Masaaki Komatsu

EMBO reports 21:e48902 PubMed31916398

2020

NBR1-mediated p62-liquid droplets enhance the Keap1-Nrf2 system.

Applications

Unspecified application

Species

Unspecified reactive species

Pablo Sánchez-Martín,Yu-Shin Sou,Shun Kageyama,Masato Koike,Satoshi Waguri,Masaaki Komatsu

Scientific reports 9:11382 PubMed31388062

2019

Comprehensive Proteomic Analysis Reveals Intermediate Stage of Non-Lesional Psoriatic Skin and Points out the Importance of Proteins Outside this Trend.

Applications

Unspecified application

Species

Unspecified reactive species

Edit Szél,Renáta Bozó,Éva Hunyadi-Gulyás,Máté Manczinger,Kornélia Szabó,Lajos Kemény,Zsuzsanna Bata-Csörgő,Gergely Groma

Molecular and cellular biology 38: PubMed29339380

2018

Negative Regulation of the Keap1-Nrf2 Pathway by a p62/Sqstm1 Splicing Variant.

Applications

Unspecified application

Species

Unspecified reactive species

Shun Kageyama,Tetsuya Saito,Miki Obata,Ryo-Hei Koide,Yoshinobu Ichimura,Masaaki Komatsu

Nature communications 7:12030 PubMed27345495

2016

p62/Sqstm1 promotes malignancy of HCV-positive hepatocellular carcinoma through Nrf2-dependent metabolic reprogramming.

Applications

WB

Species

Unspecified reactive species

Tetsuya Saito,Yoshinobu Ichimura,Keiko Taguchi,Takafumi Suzuki,Tsunehiro Mizushima,Kenji Takagi,Yuki Hirose,Masayuki Nagahashi,Tetsuro Iso,Toshiaki Fukutomi,Maki Ohishi,Keiko Endo,Takefumi Uemura,Yasumasa Nishito,Shujiro Okuda,Miki Obata,Tsuguka Kouno,Riyo Imamura,Yukio Tada,Rika Obata,Daisuke Yasuda,Kyoko Takahashi,Tsutomu Fujimura,Jingbo Pi,Myung-Shik Lee,Takashi Ueno,Tomoyuki Ohe,Tadahiko Mashino,Toshifumi Wakai,Hirotatsu Kojima,Takayoshi Okabe,Tetsuo Nagano,Hozumi Motohashi,Satoshi Waguri,Tomoyoshi Soga,Masayuki Yamamoto,Keiji Tanaka,Masaaki Komatsu
View all publications

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