HSP27 Protein (full length)
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- 抗原 See all HSP27 (HSPB1) 蛋白
- HSP27 (HSPB1) (Heat Shock 27kDa Protein 1 (HSPB1))
- 蛋白类型
- Recombinant
- 产品特性
- full length
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宿主
- 人
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资源
- 大肠杆菌（E. Coli）
- 应用范围
- Western Blotting (WB), ELISA, SDS-PAGE (SDS), Functional Studies (Func)
- 序列
- MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD ETAAK
- 特异性
- ~27 kDa
- 纯化方法
- Affinity Purified
- 纯度
- >90%
- Top Product
- Discover our top product HSPB1 蛋白
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Heat Shock 27kDa Protein 1 (HSPB1) (AA 1-205) protein (GST tag)
HSPB1 宿主: 人 宿主: 小麦胚 Recombinant WB, ELISA, AP, AA
Heat Shock 27kDa Protein 1 (HSPB1) (AA 1-205) protein (His-IF2DI Tag)HSPB1 宿主: 人 宿主: 大肠杆菌（E. Coli） Recombinant Greater than 95 % by SDS-PAGE gel analyses WB, ELISA
Heat Shock 27kDa Protein 1 (HSPB1) (AA 96-205) protein (GST tag)HSPB1 宿主: 人 宿主: 小麦胚 Recombinant WB, ELISA, AP, AA
Heat Shock 27kDa Protein 1 (HSPB1) (AA 1-205) protein (His tag)Crystallography grade HSPB1 宿主: 人 宿主: Insect Cells Recombinant >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. WB, ELISA, SDS, Crys
Heat Shock 27kDa Protein 1 (HSPB1) (AA 1-209) protein (His tag)Crystallography grade HSPB1 宿主: 小鼠 宿主: Insect Cells Recombinant >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. WB, ELISA, SDS, Crys
Heat Shock 27kDa Protein 1 (HSPB1) proteinHSPB1 宿主: 小鼠 宿主: 大肠杆菌（E. Coli） Recombinant > 95 % WB, ELISA, SDS, IP
Heat Shock 27kDa Protein 1 (HSPB1) protein (Myc-DYKDDDDK Tag)HSPB1 宿主: 人 宿主: HEK-293 Cells Recombinant > 80 % as determined by SDS-PAGE and Coomassie blue staining AbP, STD
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- 应用备注
- Optimal working dilution should be determined by the investigator.
- 说明
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This product has been certified >90% pure using SDS-PAGE analysis.
- 限制
- 仅限研究用
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- 浓度
- Lot specific
- 缓冲液
- 20 mM Tris/HCl pH 7.5, 0.45M NaCl, 10 % glycerol, 5 mM DTT
- 储存条件
- -20 °C
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- 抗原
- HSP27 (HSPB1) (Heat Shock 27kDa Protein 1 (HSPB1))
- 别名
- Hsp27 (HSPB1 产品)
- 背景
- HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an α-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
- 分子量
- approx. 27 kDa
- 基因ID
- 3315
- UniProt
- P04792
- 途径
- MAPK Pathway, Regulation of Actin Filament Polymerization, Signaling Events mediated by VEGFR1 and VEGFR2, Negative Regulation of intrinsic apoptotic Signaling, VEGF Signaling
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