G4420
Anti-GRP94 (C-terminal) antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous solution
동의어(들):
Anti-Endoplasmin precursor, Anti-Glucose Regulated Protein 94, Anti-Tumor Rejection Antigen 1, Anti-gp96
조직 및 계약 가격을 보려면 로그인를 클릭합니다.
크기 선택
제품정보 (DICE 배송 시 비용 별도)
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ARR, ICC, IF, IP, WB
Citations:
15
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 94 kDa
species reactivity
canine, human, mouse
concentration
~1 mg/mL
technique(s)
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 accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... HSP90B1(7184)
mouse ... Hsp90b1(22027)
rat ... Tra1(298957)
관련 카테고리
Immunogen
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.
Application
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.
Biochem/physiol Actions
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
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.
적합한 제품을 찾을 수 없으신가요?
당사의 제품 선택기 도구.을(를) 시도해 보세요.
저장 등급
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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
Z Muresan et al.
The Journal of biological chemistry, 272(42), 26095-26102 (1997-10-23)
GRP94 serves as a molecular chaperone in the endoplasmic reticulum (ER). In normal thyrocytes, GRP94 interacts transiently with thyroglobulin (Tg), and in thyrocytes of animals suffering from congenital hypothyroid goiter with defective thyroglobulin, GRP94 and thyroglobulin associate in a protracted
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
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.
H Singh-Jasuja et al.
Cell stress & chaperones, 5(5), 462-470 (2001-02-24)
Heat shock proteins like gp96 (grp94) are able to induce specific cytotoxic T-cell (CTL) responses against cells from which they originate and are currently studied in clinical trials for use in immunotherapy of tumors. We have recently demonstrated that gp96
관련 콘텐츠
자사의 과학자팀은 생명 과학, 재료 과학, 화학 합성, 크로마토그래피, 분석 및 기타 많은 영역을 포함한 모든 과학 분야에 경험이 있습니다..
고객지원팀으로 연락바랍니다.