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当前位置: 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP27 Antibody [5D12-A12]/SMC-161B-HRP/200-µg
商品详细StressMarq/Anti-HSP27 Antibody [5D12-A12]/SMC-161B-HRP/200-µg
StressMarq/Anti-HSP27 Antibody [5D12-A12]/SMC-161B-HRP/200-µg
StressMarq/Anti-HSP27 Antibody [5D12-A12]/SMC-161B-HRP/200-µg
商品编号: SMC-161B-HRP
市场价: ¥6240.00
美元价: 3744.00
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
商品介绍

Overview:

Product Name HSP27 Antibody
Description

Mouse Anti-Human HSP27 Monoclonal IgG2b Kappa

Species Reactivity Human
Applications WB, IHC, ICC/IF, IP, ELISA
Antibody Dilution WB (1:2000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.
Host Species Mouse
Immunogen Species Human
Immunogen Human HSP27
Concentration 1 mg/ml
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 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. Has no cross-reactivity to Alpha B crystallin. Very limited cross-reactivity to other species.
Cite This Product StressMarq Biosciences Cat# SMC-161, RRID: AB_2248586
Certificate of Analysis 0.5 µg/ml of SMC-161 was sufficient for detection of HSP27 in 10 µg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse 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
Cellular Localization Cytoplasm, Cytoskeleton, Nucleus, Spindle
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>Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 5D12-A3 (SMC-161). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody (SMC-161) at 1:100 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Nucleus. Magnification: 100x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp27 Antibody. (C) Composite.</p>

Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 5D12-A3 (SMC-161). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody (SMC-161) at 1:100 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Nucleus. Magnification: 100x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp27 Antibody. (C) Composite.

<p>Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 5D12-A3 (SMC-161). Tissue: HaCaT cells. Species: Human. Fixation: Cold 100% methanol for 10 minutes at -20°C. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody (SMC-161) at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Dull heterogeneous staining, some perinuclear, some nuclear and some cytoplasmic staining .</p>

Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 5D12-A3 (SMC-161). Tissue: HaCaT cells. Species: Human. Fixation: Cold 100% methanol for 10 minutes at -20°C. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody (SMC-161) at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Dull heterogeneous staining, some perinuclear, some nuclear and some cytoplasmic staining .

<p>Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 5D12-A3 (SMC-161). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody (SMC-161) at 1:100 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Nucleus. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp27 Antibody. (C) Composite.</p>

Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 5D12-A3 (SMC-161). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody (SMC-161) at 1:100 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Nucleus. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp27 Antibody. (C) Composite.

<p>Western Blot analysis of Human Cell lysates showing detection of Hsp27 protein using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 5D12-A3 (SMC-161). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody (SMC-161) at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.</p>

Western Blot analysis of Human Cell lysates showing detection of Hsp27 protein using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 5D12-A3 (SMC-161). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody (SMC-161) at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.

Product Citations (4)

Western Blot

Re-examining HSPC1 inhibitors.

Lee, S.L. et al. (2017) Cell Stress Chaperones. 22(2):293-306.

PubMed ID: 28255900 Reactivity Human Applications: Western Blot

The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins.

Mymrikov, E.V., Daake, M., Richter, B., Haslbeck, M. and Buchner, J. (2016) J Biol Chem. 292(2):672-684.

PubMed ID: 27909051 Reactivity Human Applications: Western Blot

Compositions and Methods for Inhibiting HSP90/HSP70 Machinery.

Chadli, A. and Patwardhan, C.A. (2015) United States Patent Application 20150025052.

PubMed ID: N/A Reactivity Human Applications: Western Blot

Immunohistochemistry

Human myocytes are protected from titin aggregation-induced stiffening by small heat shock proteins.

Kötter, S. et al. (2014) J Cell Biol. 204(2):187-202.

PubMed ID: 24421331 Reactivity Human Applications: Immunohistochemistry

HRP (Horseradish peroxidase)

Properties:

  • Enzymatic activity is used to amplify weak signals and increase visibility of a target
  • Readily combines with hydrogen peroxide (H2O2) to form HRP-H2O2 complex which can oxidize various hydrogen donors
  • Catalyzes the conversion of:
    • Chromogenic substrates (e.g. TMB, DAB, ABTS) into coloured products
    • Chemiluminescent substrates (e.g. luminol and isoluminol) into light emitting products via enhanced chemiluminescence (ECL)
    • Fluorogenic substrates (e.g. tyramine, homovanillic acid, and 4-hydroxyphenyl acetic acid) into fluorescent products
  • High turnover rate enables rapid generation of a strong signal
  • 44 kDa glycoprotein
  • Extinction coefficient: 100 (403 nm)
  • Applications: Western blot, immunohistochemistry, and ELISA

HRP Datasheet

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。