Analytical Data
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Gene name
CALR
- Application
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Alternative Names
CRT; RO; SSA; CC1qR; ERp60; HACBP; grp60; CRTC; CRP55; Calregulin; Sicca Syndrome Antigen A; Autoantigen Ro; Endoplasmic reticulum resident protein 60
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Species
Human
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Source
HEK293
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P27797
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Expression Region
Glu18~Leu417
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Molecular Weight
60kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
Calreticulin (CALR) is a multi-functional protein that plays a crucial role in calcium homeostasis, protein folding, and quality control within the endoplasmic reticulum (ER). Recent studies have highlighted its significant involvement in various hematological malignancies, particularly those associated with mutations in the CALR gene, which have been identified as a key driver of myeloproliferative neoplasms (MPNs). These mutations typically lead to a gain-of-function effect, altering the protein's interaction with calcium and the ER stress response, thus promoting abnormal cell proliferation. The search for CALR's specific contributions to oncogenesis has driven researchers to investigate recombinant CALR proteins, employing techniques such as expression cloning and yeast or bacterial systems to purify these variants. Such studies aim to elucidate the structural and functional characteristics of wild-type and mutant CALR proteins, as well as their potential as therapeutic targets. Additionally, the recombinant CALR provides a valuable tool for developing cellular and animal models to better understand its role in disease mechanisms. As therapeutic approaches evolve, understanding CALR's molecular pathways may identify new strategies for targeted treatment and improve prognosis for patients with CALR-associated myeloproliferative disorders. Therefore, research on recombinant CALR is critical for advancing our knowledge of its biological functions and implications in cancer biology, particularly within the context of MPNs.
