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AB40850

Anti-Asparagine synthetase antibody [EP282Y]

1

(1 Review)

|

(7 Publications)

Rabbit Recombinant Monoclonal Asparagine synthetase antibody. Suitable for WB and reacts with Human samples. Cited in 7 publications.

View Alternative Names

TS11, ASNS, Asparagine synthetase [glutamine-hydrolyzing], Cell cycle control protein TS11, Glutamine-dependent asparagine synthetase

1 Images
Western blot - Anti-Asparagine synthetase antibody [EP282Y] (AB40850)
  • WB

Unknown

Western blot - Anti-Asparagine synthetase antibody [EP282Y] (AB40850)

All lanes:

Western blot - Anti-Asparagine synthetase antibody [EP282Y] (ab40850) at 1/2000 dilution

All lanes:

K562 cell lysate at 10 µg

Predicted band size: 64 kDa

Observed band size: 60 kDa

false

  • Carrier free

    Anti-Asparagine synthetase antibody [EP282Y] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EP282Y

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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Product details

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 0.05% BSA
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.

Asparagine synthetase (ASNS) is an enzyme that catalyzes the conversion of aspartate and glutamine to asparagine and glutamate. This enzyme is also known by the alternate name ASPG. Asparagine synthetase weighs approximately 64 kDa and it is found in many tissues including the liver and pancreas. The presence of ASNS is important for the synthesis of asparagine an amino acid necessary for protein and nucleotide synthesis.
Biological function summary

ASNS drives the synthesis of asparagine through a mechanism involving the ATP-dependent conversion of substrates. It does not function as part of a larger enzyme complex but operates independently to fulfill its role. In cells asparagine produced serves as a critical building block supporting protein biosynthesis and cell proliferation particularly in rapidly dividing cells such as cancer cells.

Pathways

Asparagine synthetase plays a central role in the asparagine biosynthetic pathway. This enzyme is key for maintaining cellular amino acid homeostasis and is linked to the mTOR pathway which regulates cell growth and metabolism. Additionally ASNS interacts with proteins like glutaminase which supplies one of its essential substrates glutamine.

ASNS has a significant correlation with acute lymphoblastic leukemia (ALL) where asparagine levels affect cancer cell survival. Targeting ASNS can influence chemotherapeutic strategies given its role in providing asparagine to leukemic cells. Additionally ASNS deficiency can lead to severe neurological conditions further highlighting its importance in human health. Its interaction with glutaminase is particularly relevant as both are involved in pathways targeted in ALL treatments.

Product protocols

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

Publications (7)

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

Cells 11: PubMed36291140

2022

Targeting Asparagine Synthetase in Tumorgenicity Using Patient-Derived Tumor-Initiating Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Gen Nishikawa,Kenji Kawada,Keita Hanada,Hisatsugu Maekawa,Yoshiro Itatani,Hiroyuki Miyoshi,Makoto Mark Taketo,Kazutaka Obama

Cancer research 80:5478-5490 PubMed33106333

2020

Brain Tumor Stem Cell Dependence on Glutaminase Reveals a Metabolic Vulnerability through the Amino Acid Deprivation Response Pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Ian J Restall,Orsolya Cseh,Laura M Richards,Trevor J Pugh,H Artee Luchman,Samuel Weiss

International journal of medical sciences 17:510-516 PubMed32174781

2020

Enhanced expression of asparagine synthetase under glucose-deprived conditions promotes esophageal squamous cell carcinoma development.

Applications

Unspecified application

Species

Unspecified reactive species

Kang Fang,Yuan Chu,Ziying Zhao,Qinfang Li,Hongqi Li,Tao Chen,Meidong Xu

Cellular and molecular gastroenterology and hepatology 9:1-13 PubMed31421261

2019

Asparagine Synthetase Is Highly Expressed at Baseline in the Pancreas Through Heightened PERK Signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Amitava Mukherjee,Nayyar Ahmed,Fateema T Rose,Abraheem N Ahmad,Tanveer A Javed,Li Wen,Rita Bottino,Xiangwei Xiao,Michael S Kilberg,Sohail Z Husain

The American journal of pathology 183:745-57 PubMed23886890

2013

Molecular and functional alterations in a mouse cardiac model of Friedreich ataxia: activation of the integrated stress response, eIF2α phosphorylation, and the induction of downstream targets.

Applications

WB

Species

Mouse

Michael Li-Hsuan Huang,Sutharshani Sivagurunathan,Samantha Ting,Patric J Jansson,Christopher J D Austin,Matthew Kelly,Christopher Semsarian,Daohai Zhang,Des R Richardson

PloS one 5:e13892 PubMed21085483

2010

Cell-cycle inhibition by Helicobacter pylori L-asparaginase.

Applications

WB, IHC-P

Species

Human, Human

Claudia Scotti,Patrizia Sommi,Maria Valentina Pasquetto,Donata Cappelletti,Simona Stivala,Paola Mignosi,Monica Savio,Laurent Roberto Chiarelli,Giovanna Valentini,Victor M Bolanos-Garcia,Douglas Scott Merrell,Silvia Franchini,Maria Luisa Verona,Cristina Bolis,Enrico Solcia,Rachele Manca,Diego Franciotta,Andrea Casasco,Paola Filipazzi,Elisabetta Zardini,Vanio Vannini

Cancer research 68:1997-2005 PubMed18339882

2008

Histamine suppresses fibulin-5 and insulin-like growth factor-II receptor expression in melanoma.

Applications

Unspecified application

Species

Unspecified reactive species

Zoltan Pos,Zoltan Wiener,Peter Pocza,Melinda Racz,Sara Toth,Zsuzsanna Darvas,Viktor Molnar,Hargita Hegyesi,Andras Falus
View all publications

Product promise

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