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AB85857

Anti-Aspartate Aminotransferase antibody

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(3 Publications)

Goat Polyclonal Aspartate Aminotransferase antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Synthetic Peptide within Human Aspartate aminotransferase, cytoplasmic aa 150-200.

View Alternative Names

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

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Aspartate Aminotransferase antibody (AB85857)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Aspartate Aminotransferase antibody (AB85857)

ab85857 at 5 µg/ml staining Aspartate Aminotransferase in formalin fixed and paraffin embedded Human Kidney tissue.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Aspartate Aminotransferase antibody (AB85857)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Aspartate Aminotransferase antibody (AB85857)

ab85857 at 5 µg/ml staining Aspartate Aminotransferase in formalin fixed and paraffin embedded Human heart tissue.

Western blot - Anti-Aspartate Aminotransferase antibody (AB85857)
  • WB

Unknown

Western blot - Anti-Aspartate Aminotransferase antibody (AB85857)

All lanes:

Western blot - Anti-Aspartate Aminotransferase antibody (ab85857) at 0.01 µg/mL

All lanes:

Human Liver lysate at 35 µg

Predicted band size: 46 kDa

Observed band size: 46 kDa

true

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, IHC-P

applications

Immunogen

Synthetic Peptide within Human Aspartate aminotransferase, cytoplasmic aa 150-200. 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: 0.02% Sodium azide Constituents: Tris buffered saline, 0.5% 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.

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 (3)

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

Cells 11: PubMed36497150

2022

Tumor Cell Derived Exosomal GOT1 Suppresses Tumor Cell Ferroptosis to Accelerate Pancreatic Cancer Progression by Activating Nrf2/HO-1 Axis via Upregulating CCR2 Expression.

Applications

Unspecified application

Species

Unspecified reactive species

Yao Guo,Taoyu Chen,Xueyi Liang,Shanmiao Gou,Jiongxin Xiong,Jing Cui,Tao Peng

Biochemical pharmacology 149:174-185 PubMed29061341

2017

Drug resistance induces the upregulation of HS-producing enzymes in HCT116 colon cancer cells.

Applications

WB

Species

Unspecified reactive species

Ashley A Untereiner,Athanasia Pavlidou,Nadiya Druzhyna,Andreas Papapetropoulos,Mark R Hellmich,Csaba Szabo

Free radical biology & medicine 53:2092-101 PubMed23010497

2012

Histone deacetylase 6 (HDAC6) plays a crucial role in p38MAPK-dependent induction of heme oxygenase-1 (HO-1) in response to proteasome inhibition.

Applications

Unspecified application

Species

Unspecified reactive species

Marc Kästle,Esther Woschee,Tilman Grune
View all publications

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