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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃.
- 保质期:
Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
- 英文名:
Recombinant Human Heat shock protein HSP 90-beta (HSP90AB1)
- 库存:
200
- 供应商:
武汉华美生物工程有限公司
- 规格:
20μg
英文名称:
Recombinant Human Heat shock protein HSP 90-beta (HSP90AB1)品名简称:
Recombinant Human HSP90AB1 protein货号:
CSB-BP010808HU规格:
20μg价格:
3168LC-MS/Western Blot:
/SDS-PAGE:
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.纯度:
Greater than 85% as determined by SDS-PAGE.内毒素:
Not test生物活性:
/基因名:
HSP90AB1Uniprot No.:
P08238别名:
HSP 90;Heat shock 84 kDa;HSP 84;HSP84种属:
Homo sapiens (Human)蛋白长度:
Full Length of Mature Protein来源:
Baculovirus分子量:
84.0 kDa表达区域:
2-724aa氨基酸序列:
PEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRMEEVD蛋白标签:
C-terminal 6xHis-tagged产品提供形式:
Liquid or Lyophilized powder缓冲液:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.储存条件:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.保质期:
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.货期:
28-38 business days注意事项:
Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.功能1:
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10. ; (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes. Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable).功能2:
/文献:
/研究领域:
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文献和实验Isolation of Heat Shock Protein Complexes
Heat shock proteins (Hsp) are molecular chaperones with the capability to interact with a wide range of other proteins and are thus often found coupled with other heat shock and non-heat shock proteins. This can be an advantage to study
Purification of the Eucaryotic Heat-Shock Proteins Hsp70 and gp96
Heat-shock proteins (HSPs), highly conserved across species, are generally considered as intracellular proteins that have protective functions in situations of cellular stress. A wide variety of stressful stimuli like heat shock, ultraviolet
Investigating Receptors for Extracellular Heat Shock Proteins
Extracellular heat shock proteins (HSP) play important roles in cell signaling and immunity. Many of these effects are mediated by cell surface receptors expressed on a wide range of cell types. We have investigated the nature
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