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AB117508

DyLight® 488 Anti-GST antibody

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(1 Publication)

Goat Polyclonal GST antibody - conjugated to DyLight® 488. Suitable for ICC/IF and reacts with Tag samples. Cited in 1 publication.

View Alternative Names

Glutathione S-transferase class-mu 26 kDa isozyme, GST 26, Sj26 antigen, SjGST

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Conjugation

DyLight® 488

Excitation/Emission

Ex: 493nm, Em: 518nm

Carrier free

No

Applications

ICC/IF

applications

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Tag": { "ICCIF-species-checked": "guaranteed", "ICCIF-species-dilution-info": "", "ICCIF-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
pH: 8.2 Constituents: 99% Tris buffered saline
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Storage information
The product can be stored for up to 12 months

Supplementary information

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

GST or Glutathione S-transferase is an enzyme family known for detoxifying endogenous and exogenous compounds through conjugation with glutathione. GSTs are about 23–28 kDa in size and are expressed in various tissues such as the liver kidneys and lungs. The GST proteins play vital roles in cellular processes and are utilized extensively in molecular biology often tagged to proteins to enhance solubility known as GST-tagged proteins.
Biological function summary

GST enzymes participate in critical cellular detoxification processes enhancing the solubility of toxins. As part of these processes GST enzymes do not function as part of a larger complex but are individual actors within the cell. They facilitate the conjugation reactions fundamental to cellular metabolism and detoxification making them essential for maintaining cellular health.

Pathways

GST enzymes contribute significantly to the metabolic breakdown pathways like the xenobiotic metabolism pathway. This pathway involves proteins such as cytochrome P450 enzymes which often function upstream to modify compounds for further GST action. GSTs are important for efficiently detoxifying potentially harmful substances preventing cellular damage.

GSTs have considerable relevance to cancer where their overexpression can confer drug resistance in tumor cells complicating treatment approaches. Additionally these enzymes connect with proteins such as MDR1 influencing multidrug resistance in cancer therapy. GSTs also relate to asthma where altered GST activity can affect the body's response to oxidative stress highlighting the enzyme's role in inflammatory processes.

Product protocols

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

Target data

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
See full target information Glutathione S-transferase class-mu 26 kDa isozyme

Publications (1)

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

Nature communications 12:3970 PubMed34172739

2021

The nanoscale molecular morphology of docked exocytic dense-core vesicles in neuroendocrine cells.

Applications

Unspecified application

Species

Unspecified reactive species

Bijeta Prasai,Gideon J Haber,Marie-Paule Strub,Regina Ahn,John A Ciemniecki,Kem A Sochacki,Justin W Taraska
View all publications

Product promise

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