추천 제품
생물학적 소스
rabbit
결합
unconjugated
항체 형태
affinity isolated antibody
항체 생산 유형
primary antibodies
클론
polyclonal
형태
buffered aqueous solution
분자량
antigen 94 kDa
종 반응성
canine, human, mouse
농도
~1 mg/mL
기술
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 수납 번호
배송 상태
dry ice
저장 온도
−20°C
타겟 번역 후 변형
unmodified
유전자 정보
human ... HSP90B1(7184)
mouse ... Hsp90b1(22027)
rat ... Tra1(298957)
관련 카테고리
면역원
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.
애플리케이션
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.
생화학적/생리학적 작용
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.
물리적 형태
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
면책조항
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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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
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
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.
R J Binder et al.
Nature immunology, 1(2), 151-155 (2001-03-15)
Antigen presenting cells (APCs) can take up exogenous antigenic peptides chaperoned by heat shock protein gp96 and re-present them through the endogenous pathway on their major histocompatibility class I molecules. The high efficiency of this process has been attributed previously
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
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