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Merck
CN

C4714

Sigma-Aldrich

Calreticulin from bovine liver

≥90% (SDS-PAGE), lyophilized powder

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352200
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Assay

≥90% (SDS-PAGE)

form

lyophilized powder

mol wt

~60 kDa

impurities

salt, essentially free

UniProt accession no.

storage temp.

−20°C

Gene Information

cow ... CALR(281036)

Biochem/physiol Actions

A high-affinity calcium binding protein which plays a dynamic role in calcium homeostasis. In addition, calreticulin binds directly to the DNA domain of hormone receptors as well as to the regulatory cytoplasmic domain of proteins of the integrin family. Calreticulin has also been shown to possess a chaperone function.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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I Wada et al.
The Journal of biological chemistry, 270(35), 20298-20304 (1995-09-01)
A unique type of chaperone that requires glucose trimming of the target proteins has been shown to be important for their maturation in the endoplasmic reticulum (ER). Calnexin, an ER membrane chaperone, is the first example of such a class.
Novel functions for calreticulin: interaction with integrins and modulation of gene expression?
S Dedhar
Trends in biochemical sciences, 19(7), 269-271 (1994-07-01)
L Mery et al.
The Journal of biological chemistry, 271(16), 9332-9339 (1996-04-19)
The widely distributed and highly conserved Ca(2+)-binding protein calreticulin has been suggested to play a role as a Ca2+ storage protein of intracellular Ca+ stores. To test this hypothesis, we have generated a mouse L fibroblast cell line stably transfected
K Burns et al.
Nature, 367(6462), 476-480 (1994-02-03)
Calreticulin is a multifunctional protein that acts as a major Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. It is also found in the nucleus, suggesting that it may have a role in transcription regulation. Calreticulin has been

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