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 15 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 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 4 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
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 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
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
Chicken Polyclonal GRP78 Primary Antibody for FACS, ICC - ABIN446404
Rasche, Menoret, Dubljevic, Menu, Vanderkerken, Lapa, Steinbrunn, Chatterjee, Knop, Düll, Greenwood, Hensel, Rosenwald, Einsele, Brändlein: A GRP78-Directed Monoclonal Antibody Recaptures Response in Refractory Multiple Myeloma with Extramedullary Involvement. in Clinical cancer research : an official journal of the American Association for Cancer Research 2016
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
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.
The present study indicates that GRP78 is increased in BALF in cigarette smokers; that HAEC secrete GRP78; and that GRP78 secretion by HAEC is augmented by cigarette smoke particulates. Enhanced secretion of GRP78 by lung cells makes it a potential biomarker of cigarette smoke-induced lung injury.
P4HB (show P4HB Antibodies) promotes hepatocellular carcinoma progression by down-regulating GRP78 expression and subsequently promoting epithelial-to-mesenchymal transition.
analysis of the effects of triptolide on cell proliferation, cell cycle and the expression of GRP78 in nasopharyngeal carcinoma
Antibodies targeting GRP78 exhibited antitumor activity and enhanced the efficacy of radiation in Non-small cell lung cancer and glioblastoma multiforme both in vitro and in vivo GRP78 is a promising novel target, and anti-GRP78 antibodies could be used as an effective cancer therapy alone or in combination with ionizing radiation
These data reveal an essential role for the molecular chaperone (show HSP90AA1 Antibodies) GRP78 in IGF-IR signaling and implicate the use of GRP78 inhibitors in blocking IGF-IR signaling in hepatoma cells.
Novel finding of the current study is that the level of GRP78/BiP was greatly increased in the Parkinson's disease dementia and dementia with Lewy bodies patients compared with people with Alzheimer's disease in cingulate gyrus and parietal cortex.
Bisdemethoxycurcumin promotes apoptosis through a GRP78-dependent pathway and mitochondrial dysfunctions, and potentiates the antitumor effect of gemcitabine in human pancreatic cancer cells.
Results identified GRP78 and HSP90a (show HSP90AA1 Antibodies) as binding partners of PRDM14 (show PRDM14 Antibodies) in triple-negative breast cancer cells, and all participate in cancer regulation. The interactions were direct and required the C-terminal region including the zinc finger motifs of PRDM14 (show PRDM14 Antibodies).
GRP78 affects p53 (show TP53 Antibodies) localization which in turn regulates autophagy.
candidate genes that modulate Hspa5 expression in the retina, were examined.
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.
These results indicate that GRP78, but not nutritional status, is a potent up-regulator of hepatic PTC (show PTCH1 Antibodies)-mRNA levels during induction of ER stress in vivo.
Data suggest that activation of GRP78/Ire1 (show ERN1 Antibodies)/Xbp1 (show XBP1 Antibodies) pathway of ER stress-unfolded protein response is involved in mouse decidualization.
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.
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