Recombinant Human Citrate Synthase Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1274

Recombinant Human Citrate Synthase Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1274
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Product Overview

Tag His
Host Species Human
Accession O75390
Background Chondroitin sulphate (CS) glycosaminoglycan chains on cell and extracellular matrix proteoglycans (PGs) can no longer be regarded as merely hydrodynamic space fillers. Overwhelming evidence over recent years indicates that sulphation motif sequences within the CS chain structure are a source of significant biological information to cells and their surrounding environment. CS sulphation motifs have been shown to interact with a wide variety of bioactive molecules, e.g. cytokines, growth factors, chemokines, morphogenetic proteins, enzymes and enzyme inhibitors, as well as structural components within the extracellular milieu. They are therefore capable of modulating a panoply of signalling pathways, thus controlling diverse cellular behaviours including proliferation, differentiation, migration and matrix synthesis. Chondroitin sulfate (CS) is a sulfated glycosaminoglycan composed of a long chain of repeating disaccharide units that are attached to core proteins, resulting in CS proteoglycans (CSPGs). In the mature brain, CS is concentrated in perineuronal nets (PNNs), which are extracellular structures that surround synapses and regulate synaptic plasticity. In addition, CS is rapidly synthesized after CNS injury to create a physical and chemical barrier that inhibits axon growth.
Description A DNA sequence encoding the human CS (O75390) (Met1-Gly466) was expressed with a C-terminal His tag.
Source Baculovirus-Insect Cells
Predicted N Terminal Ala 28
AA Sequence Met1-Gly466
Molecular Weight The secreted recombinant human CS consists of 449 a.a. and predicts a molecular mass of 50.4 KDa. The apparent molecular mass of the protein is approximately 46 KDa in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 7.0..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Subcellular Location Mitochondrion matrix.
Protein Families Citrate synthase family
Database References

Gene Functions References

  1. citrate synthase and ACSS1 have tumorigenic functions in hepatocellular carcinoma PMID: 27363021
  2. Citrate synthase activity was lower in patients with heart failure with preserved ejection fraction compared to controls. PMID: 27179829
  3. mir-122 and its targets G6PC3, ALDOA and CS play roles in the hypoxia responses that regulate glucose and energy metabolism and can serve as hypoxia biomarkers. PMID: 27793029
  4. METTL12 methylates CS on Lys-395, which is localized in the CS active site. Interestingly, the METTL12-mediated methylation inhibited CS activity and was blocked by the CS substrate oxaloacetate. PMID: 28887308
  5. Data suggest that METTL12, localized in mitochondrial matrix, modifies/methylates Lys368 of citrate synthase in external surface region close to its catalytic site; addition/removal of methylation has no effect on citrate synthase activity; Lys368 occurs in highly conserved sequence of amino acid residues of citrate synthase. (METTL12 = methyltransferase-like protein 12) PMID: 28391595
  6. Data suggest that downregulation of citrate synthase (CS) expression in 293T cells leads to low level of ATP production, excessive superoxide formation and cell apoptosis, which implies a possible mechanism for hearing loss in A/J mice. PMID: 28216161
  7. Hence, we conclude that SIRT3 exhibits neuroprotection via deacetylating and increasing mitochondrial enzyme activities. PMID: 28161643
  8. Paretic muscle in hemiparetic stroke survivors had lower CS concentration. PMID: 26361074
  9. The citrate synthase knockdown cells exhibited severe defects in respiratory activity and marked decreases in ATP production, but great increases in glycolytic metabolism. PMID: 23139858
  10. Citrate synthase (CS) is a direct RORalpha target gene and one mechanism by which RORalpha regulates lipid metabolism is via regulation of CS expression. PMID: 22485150
  11. Responses of skeletal and cardiac muscles in CS activity and gene expression at 1 and 48 h after endurance training. Acute effect of exercise on training-induced elevation in CS activity in rat soleus but not ventricle muscles. PMID: 12531911
  12. possible role of CS-specific autoantibodies in the pathomechanism of allograft vasculopathy PMID: 15711981
  13. It is likely that enhanced citrate synthase activity contributes to the conversion of glucose to lipids in pancreatic cancer providing substrate for membrane lipids synthesis. PMID: 15714131
  14. These results provide an important basis for the study of mitochondrial dysfunction due to aberrant CSa trafficking. PMID: 19479947

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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