B1174
BiP from calf liver
~96% (SDS-PAGE)
Synonym(s):
GRP78, Immunoglobulin-heavy-chain binding protein
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About This Item
MDL number:
UNSPSC Code:
12352204
assay
~96% (SDS-PAGE)
form
powder
mol wt
~78 kDa
solubility
H2O: 0.1 mg/mL, clear to hazy
storage temp.
−20°C
Biochem/physiol Actions
BiP is a member of the hsp70 family of chaperone proteins and is the major chaperone in endoplasmic reticulum (ER) lumen. It is involved in protein folding and translocation through the ER membranes. BiP displays a low basal level of ATPase activity that is stimulated by various peptides. It is activated by Ca2+ and also serves as a Ca2+ storage protein in the ER lumen.
Other Notes
Lyophilized powder containing 20 mM HEPES, pH 7.5, 25 mM KCl, 5 mM MgCl2, and 100 mg/ml trehalose.
Storage Class
13 - Non Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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S Blond-Elguindi et al.
The Journal of biological chemistry, 268(17), 12730-12735 (1993-06-15)
The molecular chaperone BiP purified from bovine liver (bBiP) exhibits a low basal level of ATPase activity that can be stimulated 3-6-fold by synthetic peptides (Flynn, G. C., Chappell, T. G., and Rothman, J. E. (1989) Science 245, 385-390). By
N Shirai et al.
Journal of biochemistry, 121(4), 787-797 (1997-04-01)
Polymerization caused by defective folding of heat-denatured ovalbumin was examined. A compactly misfolded ovalbumin that was produced by cooling heat-denatured protein rapidly tended to aggregate in the presence of salt. Two different forms of aggregates were observed as the concentration
J Wei et al.
The Journal of biological chemistry, 270(44), 26677-26682 (1995-11-03)
In the present study, we produced single point mutations in the ATP binding site of hamster BiP, isolated recombinant proteins, and characterized them in terms of their affinity for ATP and ADP, their ability to undergo a conformational change upon
J P Lièvremont et al.
The Journal of biological chemistry, 272(49), 30873-30879 (1998-01-10)
The activity of BiP, the major chaperone of the endoplasmic reticulum (ER) lumen, is known to be Ca2+-regulated; however, the participation of this protein in the ER storage of the cation has not yet been investigated. Here such a role
M J Gething et al.
Nature, 355(6355), 33-45 (1992-01-02)
In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the absence of other macromolecular cellular components, folding and
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