GAPDH Antibody #abs132004

abs132004-50ug

In Stock

201

abs132004-100ug

In Stock

301

Description

Undoubtedly, glyceraldehyde 3 phosphate dehydrogenase (GAPDH) is a well-known glycolytic enzyme present in the cytoplasm. However, it is now clear that mammalian GAPDH is not limited to just glycolysis. Recent evidence indicates that it plays a crucial role in several other intracellular processes, including membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication, and DNA repair. In essence, GAPDH has become a central player in various biological pathways, making it a potential target for novel therapeutic approaches.

Source

Rabbit

Specificity

The GAPDH antibody is capable of recognizing the natural quantity of total GAPDH in a sample.

Species Reactivity

Human;Mouse;Rat;Pig;Bovine;Goat;Monkey;Chicken

Predictive reaction species

Chicken;Rabbit;Pig;Dog;Sheep;Horse;Bovine

Application

。（WB），1:3000-1:30000；（IHC），1:200；（IF），1:200；（ELISA），1:20000-1:40000。，。

Immunogen

A synthesized peptide derived from human GAPDH.

Properties

Concentration

1mg/ml

Purification

Peptide affinity chromatography using SulfoLink™ Coupling Resin was employed to purify the antiserum. The resulting antiserum was highly purified and suitable for use in various applications. This purification method is efficient and enables the isolation of highly specific antibodies. With this technology, it is possible to obtain an antiserum that is free from contaminants and has high activity against the target antigen. In conclusion, SulfoLink™ Coupling Resin-based peptide affinity chromatography is a reliable, cost-effective, and highly effective method for antiserum purification.

Clonality

Polyclonal Antibody

Stability & Storage

To ensure maximum storage stability, it is recommended to keep the product at a temperature of -20 °C for a duration of one year. It is important to avoid subjecting the product to multiple freeze/thaw cycles as this could compromise its quality.

Storage buffer

：IgG-20°C，pH7.4，150mM，0.02%50%。，12。

Target

Background

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a versatile enzyme that possesses both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities. Its involvement in glycolysis and nuclear functions makes it a crucial player in various cellular processes. Within the nucleus, GAPDH participates in important events such as transcription, RNA transport, DNA replication, and apoptosis. The nitrosylase activity of GAPDH is responsible for its nuclear functions, as it facilitates the cysteine S-nitrosylation of nuclear target proteins like SIRT1, HDAC2, and PRKDC. This modification is thought to regulate their functions.
Apart from its nuclear roles, GAPDH also influences the organization and assembly of the cytoskeleton. It achieves this by promoting the binding of CHP1 to microtubules, which in turn facilitates the interaction between microtubules and membranes. This interaction is crucial for maintaining the structural integrity of the cytoskeleton.
In the context of glycolysis, GAPDH acts as a key enzyme that catalyzes the conversion of D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate, thus initiating the glycolytic pathway.
Additionally, GAPDH is involved in the regulation of translation during inflammation processes. It forms a complex known as the GAIT complex in response to interferon-gamma treatment. This complex binds to specific RNA elements called GAIT elements, which are present in the 3'-UTR of inflammatory mRNAs such as ceruloplasmin. By binding to these elements, the GAIT complex inhibits the translation of these mRNAs, thereby mediating the selective suppression of inflammatory protein synthesis.
In summary, GAPDH is a multifunctional enzyme that plays critical roles in glycolysis, nuclear functions, cytoskeleton organization, and translation regulation during inflammation. Its diverse activities contribute to the proper functioning of various cellular processes.

Posttranslational modification

S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus (By similarity). S-nitrosylation of Cys-247 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity.ISGylated.Sulfhydration at Cys-152 increases catalytic activity.Oxidative stress can promote the formation of high molecular weight disulfide-linked GAPDH aggregates, through a process called nucleocytoplasmic coagulation. Such aggregates can be observed in vivo in the affected tissues of patients with Alzheimer disease or alcoholic liver cirrhosis, or in cell cultures during necrosis. Oxidation at Met-46 may play a pivotal role in the formation of these insoluble structures. This modification has been detected in vitro following treatment with free radical donor (+/-)-(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide. It has been proposed to destabilize nearby residues, increasing the likelihood of secondary oxidative damages, including oxidation of Tyr-45 and Met-105. This cascade of oxidations may augment GAPDH misfolding, leading to intermolecular disulfide cross-linking and aggregation.

Celluar localization

Cytoskeleton;Cytosol;Extracellular region or secreted;Nucleus;Plasma Membrane;

UniPort

P04406