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AB189863

Anti-Aspartate Aminotransferase antibody - C-terminal

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(5 Publications)

Rabbit Polyclonal Aspartate Aminotransferase antibody. C-terminal. Suitable for WB and reacts with Human, Mouse samples. Cited in 5 publications. Immunogen corresponding to Recombinant Fragment Protein within Human Aspartate aminotransferase, cytoplasmic aa 200 to C-terminus.

View Alternative Names

cAspAT, Glutamate oxaloacetate transaminase 1, Transaminase A, cCAT, GOT1

1 Images
Western blot - Anti-Aspartate Aminotransferase antibody - C-terminal (AB189863)
  • WB

Supplier Data

Western blot - Anti-Aspartate Aminotransferase antibody - C-terminal (AB189863)

All lanes:

Western blot - Anti-Aspartate Aminotransferase antibody - C-terminal (ab189863) at 1/500 dilution

Lane 1:

Jurkat cell extract

Lane 2:

293T cell extract

Lane 3:

HepG2 cell extract

Lane 4:

A549 cell extract

Lane 5:

HeLa cell extract

Lane 6:

mouse liver extract

Lane 7:

mouse kidney extract

Lane 8:

mouse heart extract

Predicted band size: 46 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human

Applications

WB

applications

Immunogen

Recombinant Fragment Protein within Human Aspartate aminotransferase, cytoplasmic aa 200 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

P17174

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.3 Preservative: 0.09% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine)
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

Supplementary information

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

Aspartate Aminotransferase (AST) also known as aspartate transaminase or aspartate transferase is an enzyme important for amino acid metabolism. Mechanically it catalyzes the reversible transfer of an amino group from aspartate to α-ketoglutarate forming oxaloacetate and glutamate. AST has a molecular mass of approximately 92 kDa and is expressed in various tissues with high levels found in liver heart muscle and kidneys. Its presence in these tissues highlights its importance in cellular metabolic processes.
Biological function summary

AST facilitates the interconversion between aspartate and oxaloacetate playing a role in the amino acid and urea cycles. Though not part of a large complex AST works closely with similar enzymes such as alanine aminotransferase (ALT) to maintain amino acid balance and support energy production. This enzymatic activity is important in nitrogen metabolism and glutamate use which are necessary for synthesizing other essential molecules within the cell.

Pathways

AST participates in the citric acid cycle and malate-aspartate shuttle enabling efficient energy production and NADH transport. The enzyme assists in converting oxaloacetate a pivotal intermediate in the citric acid cycle to keep the cycle active ensuring efficient cellular respiration. Additionally in the malate-aspartate shuttle AST works alongside malate dehydrogenase to facilitate the transfer of reducing equivalents across the mitochondrial membrane which is essential for ATP generation.

Elevated AST levels often indicate liver damage such as in hepatitis or cirrhosis reflecting its significant tissue expression. The enzyme is also linked to myocardial infarction as damaged heart muscle releases AST into the bloodstream. In these conditions AST serves as a biomarker for tissue damage often in conjunction with ALT levels allowing clinicians to assess the extent of liver or cardiac injury.

Product protocols

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

Target data

Biosynthesis of L-glutamate from L-aspartate or L-cysteine (PubMed : 21900944). Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. In addition, catalyzes (2S)-2-aminobutanoate, a by-product in the cysteine biosynthesis pathway (PubMed : 27827456).
See full target information Aspartate aminotransferase, cytoplasmic

Publications (5)

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

Nature communications 16:2088 PubMed40025024

2025

In situ valence-transited arsenic nanosheets for multi-modal therapy of colorectal cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Hongyue Zheng,Ke Zhang,Jigang Piao,Chaofeng Mu,Xiaowei Xie,Mengying Cheng,Tianxiang Yue,Jiang Sun,Bin Li,Yinghui Wei,Hangsheng Zheng,Lai Jiang,Douae Nihed Habiballah,Fanzhu Li

International journal of urology : official journal of the Japanese Urological Association 28:459-465 PubMed33403726

2021

Age-related differences in responses to hydrogen sulfide in the bladder of spontaneously hypertensive rats.

Applications

Unspecified application

Species

Unspecified reactive species

Suo Zou,Takahiro Shimizu,Masaki Yamamoto,Shogo Shimizu,Youichirou Higashi,Takashi Karashima,Motoaki Saito

Journal of molecular and cellular cardiology 138:304-317 PubMed31836543

2019

Defining decreased protein succinylation of failing human cardiac myofibrils in ischemic cardiomyopathy.

Applications

Unspecified application

Species

Unspecified reactive species

Hadi R Ali,Cole R Michel,Ying H Lin,Timothy A McKinsey,Mark Y Jeong,Amrut V Ambardekar,Joseph C Cleveland,Richard Reisdorph,Nichole Reisdorph,Kathleen C Woulfe,Kristofer S Fritz

Journal of proteome research 18:1513-1531 PubMed30644754

2019

Quantifying Competition among Mitochondrial Protein Acylation Events Induced by Ethanol Metabolism.

Applications

Unspecified application

Species

Unspecified reactive species

Hadi R Ali,Mohammed A Assiri,Peter S Harris,Cole R Michel,Youngho Yun,John O Marentette,Frank K Huynh,David J Orlicky,Colin T Shearn,Laura M Saba,Richard Reisdorph,Nichole Reisdorph,Matthew D Hirschey,Kristofer S Fritz

Cell metabolism 28:817-832.e8 PubMed30244971

2018

Translational and HIF-1α-Dependent Metabolic Reprogramming Underpin Metabolic Plasticity and Responses to Kinase Inhibitors and Biguanides.

Applications

Unspecified application

Species

Unspecified reactive species

Laura Hulea,Simon-Pierre Gravel,Masahiro Morita,Marie Cargnello,Oro Uchenunu,Young Kyuen Im,Camille Lehuédé,Eric H Ma,Matthew Leibovitch,Shannon McLaughlan,Marie-José Blouin,Maxime Parisotto,Vasilios Papavasiliou,Cynthia Lavoie,Ola Larsson,Michael Ohh,Tiago Ferreira,Celia Greenwood,Gaëlle Bridon,Daina Avizonis,Gerardo Ferbeyre,Peter Siegel,Russell G Jones,William Muller,Josie Ursini-Siegel,Julie St-Pierre,Michael Pollak,Ivan Topisirovic
View all publications

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