Analytical Data
-
Gene name
CALY
- Application
-
Alternative Names
CALY；DRD1IP；Neuron-specific vesicular Protein calcyon
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NYX4
-
Expression Region
1-217aa
-
AA Sequence
MVKLGCSFSGKPGKDPGDQDGAAMDSVPLISPLDISQLQPPLPDQVVIKTQTEYQLSSPDQQNFPDLEGQRLNCSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPTQAGAAAAATEPPGKPSAKAEKEAARKAAGSAAPPPAQ
-
Molecular Weight
23.4 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
CALY, or Calreticulin, is a ubiquitous calcium-binding chaperone protein found in the endoplasmic reticulum, playing a pivotal role in various cellular processes, including protein folding, assembly, and quality control. Its significance extends to immune response regulation, influencing T-cell activation and the presentation of antigens. Recent research has focused on the implications of CALY in different diseases, particularly in cancer, where its aberrant expression has been linked to tumor progression and immune evasion. The recombinant production of CALY has gained attention as it enables the detailed study of its structure, function, and potential therapeutic applications. By expressing CALY in a controlled environment, researchers can investigate its properties, interactions with other proteins, and its role in pathophysiological conditions. Understanding CALY through recombinant techniques may lead to novel insights into its function in immune modulation and inform the development of targeted therapies, enhancing our strategies against various diseases, particularly tumors that exploit CALY's mechanisms for immune evasion.
