Reactivity | HuSpecies Glossary |
Applications | WB, IHC |
Clone | 681207 |
Clonality | Monoclonal |
Host | Mouse |
Conjugate | Unconjugated |
Immunogen | E. coli-derived recombinant human Calreticulin Glu18-Leu417 Accession # P27797 |
Specificity | Detects human Calreticulin in direct ELISAs. In direct ELISAs, no cross-reactivity with human Vasostatin is observed. |
Source | N/A |
Isotype | IgG1 |
Clonality | Monoclonal |
Host | Mouse |
Purity Statement | Protein A or G purified from hybridoma culture supernatant |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Reconstitution Instructions | Reconstitute at 0.5 mg/mL in sterile PBS. |
Secondary Antibodies |
Isotype Controls |
Calreticulin - ER chaperone involved in calcium homeostasis and protein quality control Calreticulin is a calcium-dependent ER chaperone, involved in protein folding, maturation, and cellular localization. Calreticulin is a highly conserved 48 kDa protein encoded by the CALR gene. Calreticulin and its homolog calnexin regulate the fo... Read full blog post. |
Calnexin - an ER chaperone that folds the cell's glycoproteins Calnexin is an abundant 90kDa chaperone protein that resides in the membrane of the endoplasmic reticulum. Calnexin and the related calreticulin protein function together to ensure the proper folding of glycoproteins. By binding to partially folded... Read full blog post. |
Calreticulin: a Multiprocess Calcium Buffering Chaperone Calreticulin is a Calcium binding chaperone that has multiple functions both inside and outside the endoplasmic reticulum. Calreticulin is involved in the quality control of newly synthesized proteins and glycoproteins, interacting with various other ... Read full blog post. |
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Uniprot |
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