Analytical Data
-
Gene name
C22orf31
- Application
-
Alternative Names
C22orf31Uncharacterized Protein C22orf31
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O95567
-
Expression Region
1-290aa
-
AA Sequence
MHPINVRRDPSIPIYGLRQSILLNTRLQDCYVDSPALTNIWMARTCAKQNINAPAPATTSSWEVVRNPLIASSFSLVKLVLRRQLKNKCCPPPCKFGEGKLSKRLKHKDDSVMKATQQARKRNFISSKSKQPAGHRRPAGGIRESKESSKEKKLTVRQDLEDRYAEHVAATQALPQDSGTAAWKGRVLLPETQKRQQLSEDTLTIHGLPTEGYQALYHAVVEPMLWNPSGTPKRYSLELGKAIKQKLWEALCSQGAISEGAQRDRFPGRKQPGVHEEPVLKKWPKLKSKK
-
Molecular Weight
59.1 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
C22orf31, a protein encoded by the C22orf31 gene, has garnered attention in recent studies related to its potential roles in cellular processes and human diseases. This protein's exact biological function remains largely unexplored, but preliminary research suggests it may be involved in critical cellular pathways, including those related to cell proliferation and apoptosis. Mutations or dysregulation of C22orf31 have been implicated in certain genetic conditions, prompting further investigation into its structure and function. The recombinant expression of C22orf31 provides a valuable tool for elucidating its function and interactions within the cell. By producing and purifying this protein, researchers aim to characterize its biochemical properties, assess its role in various cellular contexts, and explore its potential as a biomarker or therapeutic target. The ongoing research into C22orf31 is vital not only for understanding fundamental biological processes but also for advancing the knowledge of its implications in human health and disease. Researchers are employing techniques such as crystallography and mass spectrometry to gain insights into the protein's structure and interactions, which may ultimately lead to the identification of novel therapeutic strategies for conditions associated with C22orf31 dysfunction. Overall, the investigation of C22orf31 as a recombinant protein represents a promising frontier in molecular biology and genetics, with implications for both basic science and translational medicine.











