HSP27 Antibody: ATTO 390-单抗-深圳欣博盛生物科技有限公司

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HSP27 Antibody: ATTO 390

品牌：Stressmarq

官网链接

说明书

折扣/货期

货号：SMC-161B-A390

规格：200 µg

目录价：￥4863.6

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:

HSP27 Antibody: ATTO 390

别名:

28kDa heat shock protein Antibody, CMT2F Antibody, HSP25 Antibody, HSP27 Antibody, HSP28 Antibody, HSPB1 Antibody, SRP27 Antibody

产品描述:

Mouse Anti-Human HSP27 Monoclonal IgG2b Kappa

反应种属:

Human

宿主来源:

Mouse

实验应用:

WB | IHC | ICC/IF | IP | ELISA | FCM

靶标/特异性:

Detects ~27kDa. Has no cross-reactivity to Alpha B crystallin. Very limited cross-reactivity to other species.

同种型:

IgG2b Kappa

推荐稀释度:

WB (1:2000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

免疫原:

Full length human HSP27

免疫原种属:

Human

克隆性:

Monoclonal

克隆号:

5D12-A12

纯化方式:

Protein G Purified

偶联:

ATTO 390

产品浓度:

1 mg/ml

保存温度:

Conjugated antibodies should be stored according to the product label

运输温度:

Blue Ice or 4ºC

存储溶液:

PBS pH7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated

产地:

加拿大

功能与背景:

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). For more information visit our HSP27 Scientific Resource Guide at http://www.HSP27.com.

Accession #:

NP_001531.1