G4420
Anti-GRP94 (C-terminal) antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous solution
别名:
Anti-Endoplasmin precursor, Anti-Glucose Regulated Protein 94, Anti-Tumor Rejection Antigen 1, Anti-gp96
生物来源
rabbit
偶联物
unconjugated
抗体形式
affinity isolated antibody
抗体产品类型
primary antibodies
克隆
polyclonal
表单
buffered aqueous solution
分子量
antigen 94 kDa
种属反应性
canine, human, mouse
浓度
~1 mg/mL
技术
immunocytochemistry: suitable
immunoprecipitation (IP): 10-20 μg using MDCK whole cell lysate
indirect immunofluorescence: 2-4 μg/mL using HeLa cells
microarray: suitable
western blot: 0.5-1 μg/mL using whole cell extracts of HeLa, MDCK, and NIH3T3 cells
UniProt登记号
运输
dry ice
储存温度
−20°C
靶向翻译后修饰
unmodified
基因信息
human ... HSP90B1(7184)
mouse ... Hsp90b1(22027)
rat ... Tra1(298957)
免疫原
synthetic peptide corresponding to amino acids 733-750 located near the C-terminus of human GRP94. This sequence is identical in mouse, rat, dog, porcine, and bovine GRP94 and highly conserved (1 amino acid substitutuion) in chicken.
应用
Anti-GRP94 (C-terminal) antibody produced in rabbit has been used in immunocytochemistry.
Anti-GRP94 (C-terminal) antibody produced in rabbit is suitable for immunoblotting at a working concentration of 0.5-1μg/mL using whole cell extracts of the human epitheloid carcinoma HeLa cells, Madin Darby canine kidney (MDCK) cells, and mouse fibroblast NIH3T3 cells. It is also suitable for immunoprecipitation of GRP94 protein from a MDCK whole cell lysate at 10-20μg concentration.
生化/生理作用
GRP94 (glucose-regulated protein 94) is involved in protein folding, sorting and secretion, and binding of immunogenic peptides. GRP94 has a role in peptide antigen presentation to major histocompatibility complex class I molecules of antigen presenting cells (APCs). It binds specifically to CD91 (α2-macroglobulin receptor), and possibly to the Toll-like receptors (TLRs) on the surface of APCs. Overexpression of GRP94 has been associated with cellular transformation and tumorigenesis.
GRPs are unresponsive to heat stress and are induced by stress related to glucose starvation or defects in glycoprotein processing, depletion of Ca2+ stores, acidosis, and hypoxia conditions that are also common in poorly vascularized tumor tissues.
The GRP94 (glucose-regulated protein 94) is a 94 kDa Ca2+- binding glycoprotein that belongs to a subfamily of the heat shock proteins Hsp90. It is a chaperone protein constitutively localized to the endoplasmic reticulum (ER) of mammalian cells.
外形
0.01M 磷酸缓冲盐溶液，pH 7.4，含 15mM 叠氮化钠。
免责声明
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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储存分类代码
10 - Combustible liquids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
Y Argon et al.
Seminars in cell & developmental biology, 10(5), 495-505 (1999-12-22)
GRP94 is the ER representative of the HSP90 family of stress-induced proteins. It binds to a limited number of proteins in the secretory pathway, apparently by recognizing advanced folding intermediates or incompletely assembled proteins, GRP94 also binds peptides and can
P K Srivastava et al.
Current opinion in immunology, 6(5), 728-732 (1994-10-01)
Heat shock proteins (HSPs) are associated with a broad spectrum of peptides derived from the cells from which they are isolated. Vaccination with such HSP-peptide complexes elicits protective immunity against tumors or other cells used as the source of HSPs.
A Ménoret et al.
International journal of cancer, 56(3), 400-405 (1994-02-01)
Resistance to glucose starvation and expression of glucose-regulated proteins (grp) were studied in a model of rat colon carcinoma. In this model, various clones originating from the same parental tumor showed distinct tumorigenic potential in syngeneic hosts. Some clones were
Ramachandra K Reddy et al.
Cancer research, 62(24), 7207-7212 (2002-12-25)
A major challenge in treating cancer is the difficulty of bringing therapy to poorly perfused areas of solid tumors, which are often most resistant to chemotherapy and radiation. GRP94 is a chaperone protein localized in the endoplasmic reticulum with antiapoptotic
Zihai Li et al.
Frontiers in bioscience : a journal and virtual library, 7, d731-d751 (2002-02-28)
Heat shock protein (HSP) gp96, or grp94 is an endoplasmic reticular (ER) paralog of the cytosolic HSP90. Being abundant and non-polymorphic, gp96 plays significant roles in maintaining protein homeostasis in the secretory pathway. This "house-keeping" role of gp96 has now
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