Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human GRP78 Antibodies:
anti-Mouse (Murine) GRP78 Antibodies:
anti-Rat (Rattus) GRP78 Antibodies:
Go to our pre-filtered search.
Chicken Polyclonal GRP78 Primary Antibody for FACS, ICC - ABIN446401
Pepping, Freeman, Gupta, Keller, Bruce-Keller: NOX2 deficiency attenuates markers of adiposopathy and brain injury induced by high-fat diet. in American journal of physiology. Endocrinology and metabolism 2013
Show all 14 Pubmed References
Human Polyclonal GRP78 Primary Antibody for ICC, IF - ABIN152679
Shin, Feltri, Wrabetz: Altered Trafficking and Processing of GALC Mutants Correlates with Globoid Cell Leukodystrophy Severity. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2016
Show all 4 Pubmed References
Human Polyclonal GRP78 Primary Antibody for ICC, IF - ABIN4316288
Sharma, Masri, Jo, Bernath, Martin, Funk, Gera: Protein kinase C regulates internal initiation of translation of the GATA-4 mRNA following vasopressin-induced hypertrophy of cardiac myocytes. in The Journal of biological chemistry 2007
Show all 3 Pubmed References
Human Polyclonal GRP78 Primary Antibody for IF (cc), IF (p) - ABIN673554
Du, Zhou, Jia, Huang: SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis. in Archives of biochemistry and biophysics 2010
Show all 3 Pubmed References
Human Monoclonal GRP78 Primary Antibody for IHC, ELISA - ABIN969204
Honda, Horie, Daito, Ikuta, Tomonaga: Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface. in Journal of virology 2009
Show all 4 Pubmed References
Dog (Canine) Polyclonal GRP78 Primary Antibody for ICC, IF - ABIN863190
Cho, Park, Kim, Kim, Kim, Jang: BiP internal ribosomal entry site activity is controlled by heat-induced interaction of NSAP1. in Molecular and cellular biology 2006
Show all 9 Pubmed References
Human Polyclonal GRP78 Primary Antibody for ELISA, WB - ABIN561386
Lindenmeyer, Rastaldi, Ikehata, Neusser, Kretzler, Cohen, Schlöndorff: Proteinuria and hyperglycemia induce endoplasmic reticulum stress. in Journal of the American Society of Nephrology : JASN 2008
Show all 2 Pubmed References
Cow (Bovine) Polyclonal GRP78 Primary Antibody for ICC, IF - ABIN361825
Luo, Mao, Lee, Lee: GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. in Molecular and cellular biology 2006
Show all 10 Pubmed References
Human Polyclonal GRP78 Primary Antibody for WB - ABIN2801942
Ting, Lee: Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. in DNA (Mary Ann Liebert, Inc.) 1988
Dog (Canine) Polyclonal GRP78 Primary Antibody for ICC, IF - ABIN2723101
Barel, Harduin-Lepers, Portier, Slomianny, Charbit: Host glycosylation pathways and the unfolded protein response contribute to the infection by Francisella. in Cellular microbiology 2016
In amphibians, the association of BiP with unfolded protein and its possible role in aggresome function may be vital in the maintenance of cellular proteostasis.
Hspa5 is essential for pronephros formation by mediating retinoic acid signaling.
Endoplasmic reticulum resident chaperone GRP78, mitochondrial protein (show COX6B2 Antibodies) Prohibitin (show PHB Antibodies) and heterogeneous nuclear ribonucleoprotein (show PCBP2 Antibodies) hnRNPC (show HNRNPC Antibodies) (C1/C2) have been shown to interact with viral RNA. Hence it is proposed that these are the principle candidates governing endoplasmic reticulum stress-induced apoptosis in JEV infection.
We revealed that a small amount of GRP78 effectively inhibited fibrillation of Abeta (show APP Antibodies) fragments. Intriguingly, the fibrillation inhibition by GRP78 was confirmed in the absence of ATP, suggesting GRP78 exhibited ATP-independent interaction with Abeta (show APP Antibodies) fragments.
Testosterone exposure could deregulate glucose availability by reducing GRP78 protein levels in endometrial stromal cells
Low GRP78 expression is associated with cancer.
These results highlight a functional role for CRIPTO (show TDGF1 Antibodies) and GRP78 in prostate cancer metastasis and suggest that targeting CRIPTO (show TDGF1 Antibodies)/GRP78 signaling may have significant therapeutic potential.
High GRP78 expression is associated with resistance to sorafeinib in liver cancer.
Results show that GRP78 was up-regulated in human prostate cancer and inversely correlated with PCA3 expression.
Inhibition of 17beta-HSD (show HSD17B3 Antibodies) 7 modulates breast cancer protein profile and enhances apoptosis by down-regulating GRP78.
GALNT6 (show GALNT6 Antibodies)-induced O-glycosylation is critical for the stability, subcellular localization, and anti-apoptotic function of GRP78 protein in cancer cells. We also suggest that GRP78 might enhance the activity of GALNT6 (show GALNT6 Antibodies) in carcinogenesis through driving Golgi-to-ER relocation of GALNT6 (show GALNT6 Antibodies).
BiP (show GDF10 Antibodies) binds to the unfolded state of MJ0366 and prevents its refolding, and that this effect is dependent on both the type and concentration of nucleotides.
This paper reports the localization of both GRP78 and HSP60 (show HSPD1 Antibodies) on the luminal/apical surface of oviduct epithelial cells, their binding to spermatozoa, and the presence of endogenous HSP60 (show HSPD1 Antibodies) in the sperm midpiece.
BiP is a master regulator of endoplasmic reticulum function, and its cleavage by subtilase cytotoxin represents a previously unknown trigger for cell death
Over-expression of GRP78 enhances replication of Porcine Circovirus 2.
Upregulating HSF1 (show HSF1 Antibodies) relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP (show DDIT3 Antibodies) and increasing HSP70 (show HSP70 Antibodies) a5 (BiP/GRP78). Our work reveals how the bidirectional crosstalk between the two stress response systems promotes early tau pathology and identifies HSF1 (show HSF1 Antibodies) being one likely key player in both systems.
These results demonstrate a key role for GRP78 in alveolar epithelial cell survival.
These results indicate that GRP78, an endoplasmic reticulum chaperon of the HSP70 (show HSP70 Antibodies) family, is a novel host factor involved at multiple steps of the Japanese encephalitis virus life cycle and could be a potential therapeutic target.
Genetic or pharmacologic inhibition of the HSPA5-GPX4 pathway enhanced gemcitabine sensitivity by disinhibiting ferroptosis in vitro and in both subcutaneous and orthotopic animal models of PDAC.
The data presented indicate that the unfolded protein response is activated in fibrotic lung tissue and strongly localized to macrophages. GRP78- and CHOP (show DDIT3 Antibodies)-mediated macrophage apoptosis was found to protect against bleomycin-induced fibrosis.
Endoplasmic reticulum stress gene GRP78 is involved in signaling pathway during hepatitis B virus-mediated hepatocarcinogenesis.
data show that Med inhibits ER stress-induced apoptosis and promotes osteoblast cell survival by targeting GRP78.
These results suggested the important roles of endoplasmic reticulum-related chaperons, Bip and SIL1 (show SIL1 Antibodies), in Alzheimer's disease-like tau hyperphosphorylation.
We show that chronic VPA treatment did not modify the ATXN3 (show ATXN3 Antibodies) inclusion load and astrogliosis in affected brain regions However, VPA chronic treatment was able to increase GRP78 protein levels at 30 weeks of age, one of its known neuroprotective effects
these findings reveal a novel critical role of GRP78 in regulating ER stress-mediated apoptosis in cartilage development and the molecular mechanisms involved.
Phosphatidylinositol deficient zebrafish have elevated hspa5 expression in the liver and hepatic lipid accumulation due to endoplasmic reticulum stress response.
The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.
78 kDa glucose-regulated protein
, heat shock 70 kDa protein 5
, Protein 1603
, 78 kDa glucose-regulated protein homolog
, luminal-binding protein
, glucose-regulated protein 78
, glucose-regulated protein 78kDa
, heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
, GRP 78
, heavy-chain binding protein BiP
, immunoglobulin heavy chain-binding protein
, endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
, glucose-regulated protein, 78kDa
, XAP-1 antigen
, glucose regulated protein, 78 kDa
, heat shock 70kD protein 5 (glucose-regulated protein, 78kD)
, heat shock 70kD protein 5
, heat shock 70kDa protein 5 (glucose-regulated protein)
, steroidogenesis-activator polypeptide