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当前位置： 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP27 Antibody: FITC [5D12-A12]/SMC-186A/50-µg
商品详细StressMarq/Anti-HSP27 Antibody: FITC [5D12-A12]/SMC-186A/50-µg
StressMarq/Anti-HSP27 Antibody: FITC [5D12-A12]/SMC-186A/50-µg
StressMarq/Anti-HSP27 Antibody: FITC [5D12-A12]/SMC-186A/50-µg
商品编号： SMC-186A
市场价： ¥3500.00
美元价： 2100.00
产地： 美国(厂家直采)
公司：
产品分类： 酸碱缓冲液
公司分类： acid_base_buffer_solution
联系Q Q： 3392242852
电话号码： 4000-520-616
电子邮箱： info@ebiomall.com
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商品介绍

Overview:

Product Name HSP27 Antibody: FITC
Description

Mouse Anti-Human HSP27 Monoclonal IgG2b Kappa

Species Reactivity Human
Applications FCM, FACS
Antibody Dilution FACS (1:50); optimal dilutions for assays should be determined by the user.
Host Species Mouse
Immunogen Species Human
Immunogen Human HSP27
Concentration 0.27 mg/ml
Conjugates FITC

Properties

Storage Buffer PBS pH7.4, 50% glycerol, 0.09% sodium azide
Storage Temperature -20ºC
Shipping Temperature Blue Ice or 4ºC
Purification Protein G Purified
Clonality Monoclonal
Clone Number 5D12-A12
Isotype IgG2b Kappa
Specificity Detects ~27kDa. No cross-reactivity to alphaB Crystallin.
Cite This Product StressMarq Biosciences Cat# SMC-186, RRID: AB_10643261
Certificate of Analysis 20 µg/ml of SMC-186 was sufficient for detection of HSP27 in human Jurkat cells by FACS analysis.

Biological Description

Alternative Names 28kDa heat shock protein Antibody, CMT2F Antibody, HSP25 Antibody, HSP27 Antibody, HSP28 Antibody, HSPB1 Antibody, SRP27 Antibody
Research Areas Cancer, Heat Shock
Cellular Localization Cytoplasm, Nucleus
Accession Number NP_001531.1
Gene ID 3315
Swiss Prot P04792
Scientific Background 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.
References 1. Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599.
2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56.
3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229.
4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70.
5. Sarto C., Binnz P.A., and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26.
6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.

Product Images

<p>Fluorescence Activated Cell Sorting analysis using Mouse Anti-Hsp27: FITC Monoclonal Antibody, Clone 5D12-A12 (SMC-186). Tissue: Heat Shocked CD3+ CD8+ T cells . Species: Mouse. Primary Antibody: Mouse Anti-Hsp27: FITC Monoclonal Antibody (SMC-186) at 1:1000. Courtesy of: Cheryl Cameron, Vaccine and Gene Therapy Instit. Florida.</p>

Fluorescence Activated Cell Sorting analysis using Mouse Anti-Hsp27: FITC Monoclonal Antibody, Clone 5D12-A12 (SMC-186). Tissue: Heat Shocked CD3+ CD8+ T cells . Species: Mouse. Primary Antibody: Mouse Anti-Hsp27: FITC Monoclonal Antibody (SMC-186) at 1:1000. Courtesy of: Cheryl Cameron, Vaccine and Gene Therapy Instit. Florida.

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  FITC (Fluorescein)
Overview:

  • Excellent fluorescence quantum yield
  • High rate of photobleaching
  • Good solubility in water
  • Broad emission spectrum
  • pH dependent spectra
  • Molecular formula: C20H12O5
  • Molar mass: 332.3 g/mol

FITC-Fluorescent-conjugate

FITC Fluorescein Fluorophore Excitation and Emission SpectraOptical Properties:

λex = 494 nm

λem = 520 nm

εmax = 7.3×104

Φf = 0.92

τfl = 5.0 ns

Brightness = 67.2

Laser = 488 nm

Filter set = FITC

 

品牌介绍
StressMarq Biosciences公司的核心技术领域为细胞应激与离子通道以及载体研究，同时在其他领域也取得了一定成就，包括翻译后修饰，提供甲基化与乙酰基化抗体。其中，细胞应激领域主要包括热休克蛋白（HSP）领域。我们公司不仅在热休克蛋白领域领先全球，而且在氧化应激领域也卓有成就。StressMarq的优势在于提供四种独立的产品系列，分别涉及抗体、蛋白、酶联免疫吸附试验（ELISA）试剂盒及小分子领域。
公司介绍
StressMarq Biosciences公司的核心技术领域为细胞应激与离子通道以及载体研究，同时在其他领域也取得了一定成就，包括翻译后修饰，提供甲基化与乙酰基化抗体。其中，细胞应激领域主要包括热休克蛋白（HSP）领域。我们公司不仅在热休克蛋白领域领先全球，而且在氧化应激领域也卓有成就。StressMarq的优势在于提供四种独立的产品系列，分别涉及抗体、蛋白、酶联免疫吸附试验（ELISA）试剂盒
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