Nrf2 (C-Term) Polyclonal Antibody
Nrf2 (C-Term) Polyclonal Antibody
Nuclear factor erythroid 2-related factor 2 (Nrf2) is a basic leucine zipper transcription factor encoded by NFE2L2 in humans that...
From €234.00 €198.90
Glucose regulated protein 94 (GRP94) is a constitutively expressed endoplasmic reticulum (ER) lumenal protein that is up-regulated in response to cellular stress such as heat shock, oxidative stress or glucose depletion. GRP94 is thought to play a role in protein translocation to the ER, in their subsequent folding and assembly, and in regulating protein secretion.{15669} GRP94 also plays a role in antigen presentation by accessing the endogenous pathway and eliciting specific cytotoxic T lymphocyte (CTL) responses to chaperone bound peptides via the major histocompatibility complex (MHC) class I pathway.{15670} GRP94 is a member of the Hsp90 family of stress proteins and shares sequence homology with its cytosolic equivalent, Hsp90.{15671} Both Hsp90 and GRP94 are calcium binding proteins.{15672} Despite sharing 50% sequence homology over its N domains and complete conservation in its ligand binding domains with Hsp90, GRP94, and Hsp90 differ in their interactions with regulatory ligands as GRP94 has weak ATP binding and hydrolysis activity.{15673} GRP94 exists as a homodimer and the two subunits interact at two distinct intermolecular sites, C-terminal dimerization domains and the N-terminal interacts with the middle domain of opposing subunits.{15674} GRP94 contains a carboxy terminal KDEL (Lys-Asp-Glu-Leu) sequence which is believed to aid in its retention in the ER.{15675}
Territorial Availability: Available through Bertin Technologies only in France
Size | 100 µg, 25 µg |
---|---|
Shipping | dry ice |
Molecular weight | 98 |
Antigen | Purified GRP94 isolated from chicken oviducts |
Host | Rat |
Clone | 9G10 |
Isotype | IgG2A |
Custom code | 3822.19 |
Application(s) | FC, ICC/IF, IP, WB |
Formulation | Protein G purified IgG2a at a concentration of 1 mg/ml |
UNSPSC code | 12352203 |
Cayman Chemical’s mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.
Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.
Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.
Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.
Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009
Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.
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