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Sino Biological Inc. liefert CALR / Calreticulin Protein mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.
Weitere Informationen über CALR / Calreticulin Protein lesen Sie bitte: http://www.sinobiological.com/CALR-Calreticulin-Protein-g-10313.html
| Synonym | CALR |
| Protein Construction | A DNA sequence encoding the human CALR(P27797)(Met1-Ala413) was expressed with the Fc region of human IgG1 at the C-terminus. |
| Source | Human |
| Expression Host | Human Cells |
| Purity | > (75.9+20.5)% as determined by SDS-PAGE | SDS-PAGE:![]() CALR protein |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method | |
| Stability | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal | Glu 18 | |
| Molecular Mass | The recombinant human CALR/Fc is a disulfide-linked homodimer. The reduced monomer comprises 637 amino acids and has a predicted molecular mass of 73 kDa. The apparent molecular mass of the protein is approximately 96 and 38 kDa in SDS-PAGE under reducing conditions. | |
| Formulation | Lyophilized from sterile PBS, pH 7.4.
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| Storage | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
As a multifunctional protein, calreticulin binds Ca2+ ions (a second messenger in signal transduction), rendering it inactive. It is a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin also binds to misfolded proteins and prevents them from being exported from the endoplasmic reticulum to the golgi apparatus. Calreticulin binds to antibodies in certain sera of systemic lupus and Sjogren patients that contain anti-Ro/SSA antibodies. Calreticulin binds to the synthetic peptide KLGFFKR, which is almost identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. 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 can inhibit the binding of androgen receptor to its hormone-responsive DNA element and can inhibit androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Thus, calreticulin can act as an important modulator of the regulation of gene transcription by nuclear hormone receptors.