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Recombinant Human CALR/Calreticulin Protein (Fc Tag)
SKU: PKSH030607-50
Recombinant Human CALR/Calreticulin Protein (Fc Tag)
| SKU # | PKSH030607 |
| Expression Host | HEK293 Cells |
Description
| Synonyms | CRT, HEL-S-99n, RO, SSA, cC1qR |
| Species | Human |
| Expression Host | HEK293 Cells |
| Sequence | Met 1-Ala413 |
| Accession | P27797 |
| Calculated Molecular Weight | 73.0 kDa |
| Observed Molecular Weight | 96&38 kDa |
| Tag | C-hFc |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from sterile PBS, pH 7.4 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
Background
Calreticulin is a multifunctional protein. It acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin binds Ca2+ ions (a second messenger in signal transduction); rendering it inactive. The Ca2+ is bound with low affinity; but high capacity; and can be released on a signal. Located in storage compartments associated with the endoplasmic reticulum; calreticulin also binds to misfolded proteins and prevents them from being exported from the endoplasmic reticulum to the golgi apparatus. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo; as well as retinoic acid-induced neuronal differentiation. Therefore; calreticulin acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.