Background:

Secretory and transmembrane proteins are synthesized on polysomes and translocated into the endoplasmic reticulum (ER). Inside the ER, these proteins are often modified by disulfide bond formation, amino-linked glycosylation and folding. To help proteins fold properly, the ER contains a pool of molecular chaperones including BiP. BiP was identified as an immunoglobulin heavy chain binding protein in pre-B cells. It was also found to be induced at the protein level by glucose starvation. When protein folding is disturbed inside ER, BiP synthesis is increased. Subsequently, BiP binds to misfolded proteins to prevent them from forming aggregates and assists in proper refolding.

Specificity:

Recognizes endogenous levels of GRP78 protein.

Alternative names:

GRP78; 78 kDa glucose-regulated protein; GRP-78; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein; BiP

Species reactivity:

Human, Rat

Host:

Mouse

Ig type:

Liquid in 0.42% Potassium phosphate, 0.87% Sodium chloride, pH 7.3, 30% glycerol, and 0.01% sodium azide.

Immunogen:

KLH-conjugated synthetic peptide encompassing a sequence of human GRP78. The exact sequence is proprietary.

Purification & Purity:

The antibody was affinity-purified from mouse antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

Molecular weight:

~ 78 kDa

Applications:

WB, IHC

Usage:

WB (1/1000 - 1/2000), IHC (1/100 - 1/200)

Storage:

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Precautions:

For research use only, not for use in diagnostic procedure.

More info:

Email: info@sobekbio.com

Orders:

Email: orders@sobekbio.com