Analytical Data
-
Gene name
GLO2
- Application
-
Alternative Names
GLO2；GLO2；HAGH1；Hydroxyacylglutathione hydrolase. mitochondrial
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q16775
-
Expression Region
1-260aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMKVEVLPALTDNYMYLVIDDETKEAA IVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVY GGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSE PPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYT INNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMR VREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD
-
Molecular Weight
31 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
GLO2, or Golgi-associated protein 2, is an important protein involved in various cellular processes, including protein sorting and transport within the Golgi apparatus. Its role is particularly significant in the post-translational modification and dispatching of proteins and lipids, which are crucial for maintaining cellular homeostasis and function. Recent studies have highlighted the involvement of GLO2 in disease mechanisms, particularly in cancer and neurodegenerative disorders, where its dysregulation can lead to impaired cellular communication and increased susceptibility to stress. Understanding the structure and function of GLO2 through recombinant protein techniques has garnered interest in the scientific community, as it may provide insights into its specific roles in these conditions. By producing GLO2 as a recombinant protein, researchers can investigate its biochemical properties, interactions with other cellular components, and its potential as a therapeutic target. This research not only elucidates the fundamental biology of GLO2 but also opens avenues for the development of novel strategies in disease treatment and prevention. As such, the study of GLO2 recombinant protein is essential for advancing our understanding of its functionality and implications in health and disease.
