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折扣/货期| 货号：GTX13492 | 规格：100μg | 目录价：￥6300 |
产品详情
* 以下信息仅供参考，详情请以原厂网站为准
产品名称:
Hsp90 antibody [AC88]
别名:
FLJ31884 heat shock 90kDa protein 1 alpha Heat shock protein HSP 90 alpha HSP86 Hsp89 HSP90A HSPC1 HSPCAL1 HSPN LAP2 Lipopolysaccharide associated protein2 LPS associated protein 2
反应种属:
Bovine, Carp, Dog, Fish, Guinea pig, Hamster, Human, Monkey, Mouse, Pig, Rabbit, Rainbow trout, Rat, Sheep
宿主来源:
Mouse
实验应用:
FCM, ICC/IF, IHC-P, IP, WB
靶标/特异性:
GTX13492 recognises both Hsp90 alpha and beta. It reacts with the rodent glucocorticoid receptor and with proliferation potential proteins (P2PS) with apparent molecular masses of 30-40 kDa, which are associated with the 30-40S substructures of nuclear hnRNP complexes and share an epitope in common with Hsp90.
同种型:
IgG1
免疫原:
Achlya ambisexualis (water mold) Hsp90.
克隆性:
Monoclonal
克隆号:
AC88
纯化方式:
Protein G purified
偶联:
Unconjugated
产品浓度:
1 mg/ml (Please refer to the vial label for the specific concentration.)
保存温度:
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
运输温度:
4°C
产品形式:
Liquid
存储溶液:
PBS, 50% Glycerol, 0.1mM PMSF, no preservatives.
生产商:
GeneTex
功能与背景:
The 90kDa molecular chaperone family comprises several proteins including the 90kDa heat shock protein, Hsp90 and the 94kDa glucose regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90a and hsp90s which are encoded by separate genes. The amino acid sequence of human and yeast Hsp90a is 85% and 90% homologous to that of Hsp90s respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N terminal and C terminal regions which have been shown to contain independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 is part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by nonphysiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signaling and cell cycle control. In this context several key regulatory proteins such as steriod receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90. It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways.
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