Recombinant Mouse Calreticulin (CALR) Protein (SKIK&His)

Name: Recombinant Mouse Calreticulin (CALR) Protein (SKIK&His)
Brand: Beta LifeScience
SKU: BLC-07706P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Calreticulin (CALR) Protein (SKIK&His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P14211
Target Symbol	CALR
Synonyms	CRP55Calregulin;Endoplasmic reticulum resident protein 60 ;ERp60HACBP
Species	Mus musculus (Mouse)
Expression System	Yeast
Tag	N-SKIK&C-6His
Target Protein Sequence	DPAIYFKEQFLDGDAWTNRWVESKHKSDFGKFVLSSGKFYGDLEKDKGLQTSQDARFYALSAKFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPSGLDQKDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAAKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDANIYAYDSFAVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDDDRDEDEDEEDEKEEDEEESPGQAKDEL
Expression Range	18-416aa
Protein Length	Full Length of Mature Protein
Mol. Weight	48.3 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy.
Subcellular Location	Endoplasmic reticulum lumen. Cytoplasm, cytosol. Cytolytic granule. Secreted, extracellular space, extracellular matrix. Cell surface. Sarcoplasmic reticulum lumen. Cytoplasmic vesicle, secretory vesicle, Cortical granule.
Protein Families	Calreticulin family
Database References	KEGG: mmu:12317 STRING: 10090.ENSMUSP00000003912 UniGene: Mm.1971

Gene Functions References

Calreticulin is required for TGF-beta mediated epithelial-mesenchymal transition and cardiomyogenesis from mESCs. PMID: 28434939
CALR mutation analysis can thus be a useful additional diagnostic tool to achieve an accurate diagnosis for patients with ET who lack JAK2V617F and MPLW515 mutations PMID: 26343915
CRT inhibition significantly blunted APN's anti-oxidative action (evidenced by gp91(phox) expression and superoxide generation). However, CRT inhibition did not attenuate AMPK phosphorylation by APN administration in NCM. Therefore, these novel findings strongly indicate that APN exerts cardioprotective effects against I/R injury partially via CRT mediated anti-apoptotic and anti-oxidative actions. PMID: 27757734
we show that the homologous mouse CALR del52, ins5 and del61 mutants also activate thrombopoietin receptor signaling via JAK-STAT pathway PMID: 26987905
study provides a model showing that the C-terminal of mutant CALR activated JAK-STAT signaling specifically downstream of MPL and may have a central role in CALR-induced myeloproliferative neoplasms PMID: 27807369
the results of this investigation provide the first molecular insights into the phospholipid binding site of calreticulin as a key anchor point for the cell surface expression of calreticulin on apoptotic cells PMID: 27036911
a profound impairment in calreticulin function when its lectin site was inactivated. Remarkably, inactivation of the polypeptide binding site had little impact. These findings indicate that the lectin-based mode of client interaction is the predominant contributor to the chaperone functions of calreticulin within the endoplasmic reticulum. PMID: 27413183
This essential role of calreticulin in nucleocytoplasmic communication competency ties its regulatory action with proficiency of cardiac myofibrillogenesis essential for proper cardiac development. PMID: 26826378
Study provides evidence that chronic stress activates calreticulin and might be one of the pathological mechanisms underlying the motor coordination and motor learning dysfunctions seen in social defeat mice. PMID: 26815100
This study for the first time revealed that increased CRT inhibited Fas/FasL-mediated neuronal cell apoptosis during the early stage of ischemic stroke, suggesting it to be a potential protector activated soon after ischemia-reperfusion injury PMID: 26583143
The findings highlight the importance of CALR in female reproduction and demonstrate that compromised CALR function leads to ovarian insufficiency and female infertility. PMID: 26388295
Calreticulin mediates vascular smooth muscle cell responses to injury through the regulation of collagen deposition and neointima formation. PMID: 26910059
CALR mutants are sufficient to induce thrombocytosis through MPL activation. PMID: 26608331
Thrombopoietin receptor activation by myeloproliferative neoplasm associated calreticulin mutants. PMID: 26668133
These studies reveal central roles for ATP and calcium binding as regulators of calreticulin-substrate interactions and as key determinants of PLC dynamics. PMID: 26420867
study demonstrates for the first time that LRH-1 has a CRT-dependent NES which is not only required for cytoplasmic trafficking, but also essential for correct protein folding to avoid misfolding-induced aggregation. PMID: 26268559
Arginylated CRT has a longer half-life than non-arginylated CRT and displays different ubiquitin dependence. PMID: 25969538
Data suggest that oligomerization of calreticulin (CRT) may occur under certain pathophysiological conditions (42 degrees C/pH 6.5) and the resultant oligomers may exhibit exaggerated immunostimulating activities. PMID: 25171171
In calreticulin-deficient embryonic stem (ES) cells WNT and miR-302 dependent maintenance of the naive ES cell state and the transition to primed pluripotency are lost. PMID: 24415131
Calreticulin expression was also found to have a dramatic effect on the phosphorylation state of serine 636 of IRS-1, such that phosphorylation of IRS-1 on serine 636 increased radically in the absence of calreticulin. PMID: 24470116
CRT is critically involved in the molecular mechanisms that drive renal fibrosis progression. PMID: 24035512
The recruitment of monoglucosylated proteins to calreticulin is kinetically driven, whereas the P-domain and co-chaperone contribute to stable substrate binding. PMID: 24100026
CRT-regulated Ca(2+)-dependent pathways are a critical molecular link between ER stress and TGF-beta fibrotic signaling PMID: 23564462
The experimental autommune encephalomyelitis-modulating effect of recombinant CRT/39-272 is attributed to activation/expansion of CD1d(hi)CD5+ IL-10-secreting B cells rather than induction of CRT-specific antibodies PMID: 23523122
data revealed a novel regulatory role for Bruton's tyrosine kinase in mediating apoptotic cell clearance, with calreticulin identified as the critical component of the CRT/CD91/C1q system targeted by Btk PMID: 23596312
Citrullinated CRT is overabundant in the rheumatoid arthritis synovium and potentiates shared epitope-activated signaling in vitro. PMID: 23233327
roles for calreticulin in cross-presentation of ovalbumin PMID: 22848581
Calreticulin appears on the surface of murine T cells soon after activation and remains detectable (at relatively low level) by flow cytometry for approximately 5 days in vitro. PMID: 22685035
post-translational arginylation of CRT can regulate its intracellular localization, cell function, and survival PMID: 22577148
ATF6-mediated down-regulation of miR-455 augments calreticulin expression, which may contribute to the protective effects of ATF6 in the heart. PMID: 22326432
enolase 1 and calreticulin are important proteins in regulating the differentiation and functions of bone marrow mast cells PMID: 21803152
Calreticulin chaperones regulate functional expression of vomeronasal type 2 pheromone receptors. PMID: 21933956
the expression of calreticulin and high-mobility group box-1 protein following Photofrin-photodynamic therapy (PDT) of Lewis lung carcinoma cells uncovers important mechanistic insights into the development of host response induced by PDT PMID: 21644033
Surface expression of CRT in viable, thapsigargin-treated fibroblasts correlates with their enhanced phagocytic uptake by bone marrow-derived dendritic cells. PMID: 21670312
Calreticulin is a thermostable protein with distinct structural responses to different divalent cation environments. PMID: 21177861
The polypeptide binding conformation of calreticulin facilitates its cell-surface expression under conditions of endoplasmic reticulum stress PMID: 21075854
Calreticulin controls the rate of assembly of CD1d molecules in the endoplasmic reticulum. PMID: 20861015
Structural basis of carbohydrate recognition by calreticulin. PMID: 20880849
magnetic resonance imaging and histopathology detected a ventricular septal defect, revealing organogenic manifestation of calreticulin deletion. PMID: 20506533
We argue that calreticulin is a potent stimulatory molecule to B cells and macrophages via the TLR-4/CD14 pathway and plays important roles in the pathogenesis of autoimmune diseases. PMID: 20855873
Study demonstrated involvement of residues Glu(217) and Glu(223)--and to a lesser extent residue Asp(220)--in binding with rheumatoid arthritis shared epitope. PMID: 20661469
Calreticulin and glycoprotein 96 chaperone the majority of antigenic peptides in the endoplasmic reticulum before exiting in association with class I histocompatibility antigen heavy chains and beta 2-microglobulin as a trimolecular complex. PMID: 20410492
Post-translational arginylation of retrotranslocated CRT, together with the decrease in intracellular calcium ions, promotes the association of CRT to stress granules. PMID: 20423325
calreticulin may have a protective effect on the heart in the face of cardiac hypertrophy. PMID: 20110410
Data show that interactions with the thiol oxidoreductase ERp57 and substrate glycans are important for the recruitment of calreticulin into the peptide loading complex and for its functional activities in MHC class I assembly. PMID: 19959473
These data identify calreticulin (CRT) as an important regulator of collagen and suggest that intracellular CRT signaling plays an important role in tissue remodeling and fibrosis. PMID: 20044481
Calreticulin reveals a critical Ca(2+) checkpoint in cardiac myofibrillogenesis PMID: 12105184
Removal of Ca2+ from calreticulin inhibits its capacity to stimulate the nuclear export of GR and the inhibition is due to the failure of Ca2+-free calreticulin to bind the DNA-binding domain of the GR. PMID: 12167720
calreticulin and calcineurin play fundamental roles in Ca(2+)-dependent pathways essential for normal cardiac development and explain the molecular basis for the rescue of calreticulin-deficient phenotype PMID: 12377773
Data show that in calreticulin-deficient cells, calnexin-substrate association is severely reduced, leading to accumulation of unfolded proteins and a triggering of the unfolded protein response. PMID: 12727205

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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