Anti-GRP78 Antibody__Rabbit Anti-Rat GRP78 Polyclonal CCT241533 (hydrochloride)
Storage Buffer
PBS pH7.4, 50% glycerol, 0.09% sodium azide
Storage Temperature
-20ºC
Shipping Temperature
Blue Ice or 4ºC
Purification
Protein A purified
Clonality
Polyclonal
Specificity
Detects ~78kDa. Weak detection in human tissues.
Cite This Product
Rabbit Anti-Rat GRP78 Polyclonal (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPC-167)
Certificate of Analysis
1 µg/ml of SPC-167 was sufficient for detection of Grp78 in 10 µg of rat brain cell lysate by colorimetric immunoblot analysis using Goat anti -rabbit IgG:HRP as the secondary antibody.
References PubMed ID::http://www.ncbi.nlm.nih.gov/pubmed/19126857
Alternative Names
BIP Antibody, Grp78 Antibody, HSPA5 Antibody, MIF2 Antibody, immunoglobulin heavy chain binding protein Antibody
Research Areas
Cancer, Heat Shock, Cell Signaling, Chaperones, Organelle Markers, Trafficking
Cellular Localization
Endoplasmic Reticulum, Endoplasmic reticulum membrane, Melanosome
Accession Number
NP_037215.1
Gene ID
25617
Swiss Prot
P06761.1
Scientific Background
GRP78 is a ubiquitously expressed, 78-kDa glucose-regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' nontranslated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia, to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer’s patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti¬tumor drugs (6, 7).
References
1. Cho S., et al. (2007). Mol Cell Biol 27(1): 368-83.
2. Yang Y., et al. (1998) J Biol Chem 273: 25552-25555.
3. Luo S., et al (2006) 26 (15): 5688-97.
4. Yu Z., et al. (1999) Exp Neurol. 15: 302-314.
5. Koomagi R., et al. (1999) Anticancer Res. 19:4333- 4336.
6. Laquerre S., et al. (1998) J. Virology 72: 4940-4949.
7. Dong D., et al. (2005) Cancer Res 65(13): 5785-91.
2. Yang Y., et al. (1998) J Biol Chem 273: 25552-25555.
3. Luo S., et al (2006) 26 (15): 5688-97.
4. Yu Z., et al. (1999) Exp Neurol. 15: 302-314.
5. Koomagi R., et al. (1999) Anticancer Res. 19:4333- 4336.
6. Laquerre S., et al. (1998) J. Virology 72: 4940-4949.
7. Dong D., et al. (2005) Cancer Res 65(13): 5785-91.













