protein

Recombinant Mouse Calreticulin

MBS957196

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Mouse Calreticulin

Calreticulin

CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP

calreticulin; Calreticulin; calreticulin; calreticulin; CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP

Calr

Calr; Calr; CRT; Calregulin; ERp60

CALR_MOUSE

E Coli or Yeast or Baculovirus or Mammalian Cell

18-416

416

DPAIYFKEQFLDGDAWTNRWVESKHKSDFGKFVLSSGKF
YGDLEKDKGLQTSQDARFYALSAKFEPFSNKGQTLVVQF
TVKHEQNIDCGGGYVKLFPSGLDQKDMHGDSEYNIMFGP
DICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYT
LIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPD
AAKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPE
DWDEEMDGEWEPPVIQNPEYK

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

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.

Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP) , a major calcium binding ER/SR protein.Smith M.J., Koch G.L.E.EMBO J. 8:3581-3586(1989) Determination of the sequence of an expressible cDNA clone encoding ERp60/calregulin by the use of a novel nested set method.Mazzarella R.A., Gold P., Cunningham M., Green M.Gene 120:217-225(1992) Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis.Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.Electrophoresis 15:735-745(1994) Lubec G., Kang S.U., Sunyer B., Chen W.-Q.Submitted (JAN-2009) to UniProtKB The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes.Dupuis M., Schaerer E., Krause K.-H., Tschopp J.J. Exp. Med. 177:1-7(1993) Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver.Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.J. Biol. Chem. 281:32806-32819(2006) Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.J. Biol. Chem. 285:35551-35557(2010) A mouse protein that localizes to acrosome and sperm tail is regulated by Y-chromosome.Bhattacharya R., Devi M.S., Dhople V.M., Jesudasan R.A.BMC Cell Biol. 14:50-50(2013) SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.Mol. Cell 50:919-930(2013) Structural basis of carbohydrate recognition by calreticulin.Kozlov G., Pocanschi C.L., Rosenauer A., Bastos-Aristizabal S., Gorelik A., Williams D.B., Gehring K.J. Biol. Chem. 285:38612-38620(2010) Structural and functional relationships between the lectin and arm domains of calreticulin.Pocanschi C.L., Kozlov G., Brockmeier U., Brockmeier A., Williams D.B., Gehring K.J. Biol. Chem. 286:27266-27277(2011)

6680836

NP_031617.1

NM_007591.3

P14211

73.7kD

Calreticulin: 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. Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57. Interacts with NR3C1 and TRIM21. Interacts with GABARAP. Belongs to the calreticulin family. Protein type: Motility/polarity/chemotaxis; Calcium-binding; Secreted; Nuclear receptor co-regulator; Secreted, signal peptide. Cellular Component: acrosome; cell surface; cytoplasm; cytosol; endoplasmic reticulum; endoplasmic reticulum lumen; external side of plasma membrane; extracellular matrix; extracellular space; focal adhesion; Golgi apparatus; intracellular membrane-bound organelle; membrane; nucleus; perinuclear region of cytoplasm; polysome; protein complex; sarcoplasmic reticulum; smooth endoplasmic reticulum. Molecular Function: androgen receptor binding; calcium ion binding; carbohydrate binding; glycoprotein binding; hormone binding; integrin binding; iron ion binding; metal ion binding; mRNA binding; peptide binding; protein binding; ubiquitin protein ligase binding; unfolded protein binding. Biological Process: cell cycle arrest; cortical actin cytoskeleton organization and biogenesis; negative regulation of neuron differentiation; negative regulation of retinoic acid receptor signaling pathway; negative regulation of steroid hormone receptor signaling pathway; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of translation; peptide antigen assembly with MHC class I protein complex; positive regulation of cell cycle; positive regulation of cell proliferation; positive regulation of DNA replication; positive regulation of phagocytosis; protein export from nucleus; protein folding; protein stabilization; regulation of meiosis

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750