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当前位置： 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP27 Antibody (Ser78)/SPC-1261D-A594/100-µl
商品详细StressMarq/Anti-HSP27 Antibody (Ser78)/SPC-1261D-A594/100-µl
StressMarq/Anti-HSP27 Antibody (Ser78)/SPC-1261D-A594/100-µl
StressMarq/Anti-HSP27 Antibody (Ser78)/SPC-1261D-A594/100-µl
商品编号： SPC-1261D-A594
市场价： ¥6040.00
美元价： 3624.00
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 (Ser78)
Description

Rabbit Anti-Human HSP27 (Ser78) Polyclonal

Species Reactivity Human
Applications WB, IHC
Antibody Dilution WB (1:1000), IHC (1:100); optimal dilutions for assays should be determined by the user.
Host Species Rabbit
Immunogen Species Human
Immunogen Synthesized unphosphorylated peptide derived from human HSP27 around the phosphorylation site of serine 78 (A-L-SP-R-Q).
Conjugates Alkaline Phosphatase, APC, ATTO 390, ATTO 488, ATTO 565, ATTO 594, ATTO 633, ATTO 655, ATTO 680, ATTO 700, Biotin, FITC, HRP, PE/ATTO 594, PerCP, RPE, Streptavidin, Unconjugated

Properties

Storage Buffer PBS pH 7.4, 50% glycerol, 150mM NaCl, 0.02% sodium azide
Storage Temperature -20ºC
Shipping Temperature Blue Ice or 4ºC
Purification Affinity Purified
Clonality Polyclonal
Isotype IgG
Specificity Detects endogenous levels of total HSP27 protein.
Cite This Product StressMarq Biosciences Cat# SPC-1261, RRID: AB_2712503
Certificate of Analysis A 1:1000 dilution of SPC-1261 was sufficient for detection of Hsp27 in 10 µg of HeLa cell lysates by ECL immunoblot analysis using Goat Anti-Rabbit IgG:HRP as the secondary antibody.

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, Atherosclerosis, Cardiovascular System, Chaperone Proteins, Chaperones, Heart, Protein Trafficking, Trafficking
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). Looking for more information on HSP27? Visit our new 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>Immunohistochemistry analysis using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1261). Tissue: Breast Carcinoma Tissue. Species: Human. Fixation: Formalin fixed paraffin-embedded. Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1261) at 1:1000. The image on the right is treated with the synthesized peptide.</p>

Immunohistochemistry analysis using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1261). Tissue: Breast Carcinoma Tissue. Species: Human. Fixation: Formalin fixed paraffin-embedded. Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1261) at 1:1000. The image on the right is treated with the synthesized peptide.

<p>Western blot analysis of Human HeLa cell lysates showing detection of ~27kDa Hsp27 protein using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1261). Lane 1 and Lane 2: Human HeLa, Hsp27 Antibody (Ser78). Lane 3 and Lane 4: Human HeLa, Hsp27 Antibody (pSer78). Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1261) at 1:1000. Predicted/Observed Size: ~27kDa.</p>

Western blot analysis of Human HeLa cell lysates showing detection of ~27kDa Hsp27 protein using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1261). Lane 1 and Lane 2: Human HeLa, Hsp27 Antibody (Ser78). Lane 3 and Lane 4: Human HeLa, Hsp27 Antibody (pSer78). Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1261) at 1:1000. Predicted/Observed Size: ~27kDa.

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 ATTO 594
Overview:

  • High fluorescence yield
  • High photostability
  • Very hydrophilic
  • Excellent solubility in water
  • Very little aggregation
  • New dye with net charge of -1
  • Molar Mass: 1137 g/mol

ATTO 594 Datasheet

 ATTO 594 Fluorophore Excitation and Emission SpectrumOptical Properties:

λex = 601 nm

λem = 627 nm

εmax = 1.2×105

Φf = 0.85

τfl = 3.5 ns

Brightness = 102

Laser = 594 nm

Filter set = Texas Red®

 

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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