Recombinant Human Calreticulin His Protein

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SDS-Page: Recombinant Human Calreticulin Protein [NBP1-44499] - Calreticulin, 48.7 kDa (421aa), confirmed by MALDI-TOF with a purity of 85% by SDS - PAGE

Product Details

Summary
Reactivity HuSpecies Glossary
Applications PAGE
Concentration
1 mg/ml

Order Details

Recombinant Human Calreticulin His Protein Summary

Description
A recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 18-417 of Human Calreticulin

Source: E.coli

Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MEPAVYFKEQ FLDGDGWTSR WIESKHKSDF GKFVLSSGKF YGDEEKDKGL QTSQDARFYA LSASFEPFSN KGQTLVVQFT VKHEQNIDCG GGYVKLFPNS LDQTDMHGDS EYNIMFGPDI CGPGTKKVHV IFNYKGKNVL INKDIRCKDD EFTHLYTLIV RPDNTYEVKI DNSQVESGSL EDDWDFLPPK KIKDPDASKP EDWDERAKID DPTDSKPEDW DKPEHIPDPD AKKPEDWDEE MDGEWEPPVI QNPEYKGEWK PRQIDNPDYK GTWIHPEIDN PEYSPDPSIY AYDNFGVLGL DLWQVKSGTI FDNFLITNDE AYAEEFGNET WGVTKAAEKQ MKDKQDEEQR LKEEEEDKKR KEEEEAEDKE DDEDKDEDEE DEEDKEEDEE EDVPGQAKDE L

Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
CALR
Purity
>85%, by SDS-PAGE

Applications/Dilutions

Dilutions
  • SDS-Page
Theoretical MW
48.7 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publication using NBP1-44499.

Packaging, Storage & Formulations

Storage
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
20 mM Tris-HCl buffer (pH8.0), 1 mM DTT, 0.1 M Nacl, 10% glycerol
Preservative
No Preservative
Concentration
1 mg/ml
Purity
>85%, by SDS-PAGE

Alternate Names for Recombinant Human Calreticulin His Protein

  • Autoantigen Ro
  • CALR
  • Calregulin
  • Calreticulin
  • cC1qR
  • CRP55
  • CRT
  • Endoplasmic reticulum resident protein 60
  • epididymis secretory sperm binding protein Li 99n
  • ERp60
  • FLJ26680
  • grp60
  • HACBP
  • HEL-S-99n
  • RO
  • Sicca syndrome antigen A (autoantigen Ro; calreticulin)
  • SSA
  • Vasostatin

Background

Calreticulin, also called CALR, is an endoplasmic reticulum (ER) protein that functions as a calcium (Ca2+) buffering molecular chaperone (1-3). Together with calnexin and ERp57, calreticulin has a critical role in protein folding and quality control of newly synthesized glycoproteins (1-3). Calreticulin has many diverse functions beyond Ca2+ binding, including cell adhesion, lectin binding, apoptosis, nuclear transport, antigen presentation, and immune response (1-3). Specifically, calreticulin is part of the peptide-loading complex that resides on the ER membrane and is responsible for antigen loading onto MHC class I molecules (1-3). Calreticulin protein has a theoretical molecular weight of 46 kDa and is 417 amino acids (aa) in length (1-3). The protein has three main domains: the N-terminal lectin-like domain, the proline-rich P-domain, and the acidic C-domain which is followed by an ER-retention KDEL signal sequence (1-3).

Given its role in multiple biological processes, it makes sense that calreticulin is implicated in both healthy and disease states. Studies have found that calreticulin mutations were present in patients with myeloproliferative neoplasms (MFN) and essential thrombocythaemia (ET) (4). Calreticulin expression is typically upregulated in most cancer lines, however it is downregulated in some tissues including cervical carcinomas, prostate cancer, and human colon adenocarcinoma (3). High expression of calreticulin on cancer cells is related to tumor cell phagocytosis and is often correlated with, and counteracted by, elevated CD47 expression to prevent cancer cell phagocytosis (3). Calreticulin mutations can serve as a major diagnostic biomarker for MFN and ET and additionally the calreticulin gene may be a potential target for cancer therapeutics (3,4).

References

1. Michalak, M., Groenendyk, J., Szabo, E., Gold, L. I., & Opas, M. (2009). Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. The Biochemical Journal. https://doi.org/10.1042/BJ20081847

2. Fucikova, J., Spisek, R., Kroemer, G., & Galluzzi, L. (2021). Calreticulin and cancer. Cell Research. https://doi.org/10.1038/s41422-020-0383-9

3. Sun, J., Mu, H., Dai, K., & Yi, L. (2017). Calreticulin: a potential anti-cancer therapeutic target. Die Pharmazie. https://doi.org/10.1691/ph.2017.7031

4. Prins, D., Gonzalez Arias, C., Klampfl, T., Grinfeld, J., & Green, A. R. (2020). Mutant Calreticulin in the Myeloproliferative Neoplasms. HemaSphere. https://doi.org/10.1097/HS9.0000000000000333

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Publications for Calreticulin Recombinant Protein (NBP1-44499)(1)

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Blogs on Calreticulin.

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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Bioinformatics

Gene Symbol CALR