Analytical Data
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Gene name
Gapdh1
- Application
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Alternative Names
Gapdh1；Gadph-1；Glyceraldehyde-3-phosphate dehydrogenase 1
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P07486
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Expression Region
1-332aa
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AA Sequence
MSKIGINGFGRIGRLVLRAAIDKGASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPANINWASAGAEYVVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYSPDMKVVSNASCTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPAATGAAKAVGKVIPALNGKLTGMAFRVPTPNVSVVDLTVRLGKGATYDEIKAKVEEASKGPLKGILGYTDEEVVSTDFFSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSNRVIDLIKYMQSKD
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Molecular Weight
35.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
GAPDH1, or Glyceraldehyde-3-phosphate dehydrogenase 1, is a key enzyme in the glycolytic pathway, playing a vital role in cellular metabolism by catalyzing the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. Beyond its classical function in energy metabolism, GAPDH1 has garnered attention for its involvement in various cellular processes, including apoptosis, oxidative stress response, and transcriptional regulation. The study of GAPDH1 recombinant protein has become increasingly relevant in biomedical research due to its potential implications in numerous diseases, particularly cancer and neurodegenerative disorders. Recombinant GAPDH1 can be produced through genetic engineering techniques, enabling the generation of sufficient quantities for detailed biochemical analysis. This approach allows researchers to investigate the enzyme's structural properties, kinetic behavior, and interaction with other cellular proteins. Furthermore, understanding the mechanisms by which GAPDH1 is regulated in different physiological and pathological contexts could provide novel insights into therapeutic targets. As such, the exploration of GAPDH1 recombinant protein serves not only to elucidate its enzymatic functions but also to pioneer innovative strategies for disease intervention and management.
