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当前位置: 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP27 Antibody/SPC-106B-A390/200-µg
商品详细StressMarq/Anti-HSP27 Antibody/SPC-106B-A390/200-µg
StressMarq/Anti-HSP27 Antibody/SPC-106B-A390/200-µg
StressMarq/Anti-HSP27 Antibody/SPC-106B-A390/200-µg
商品编号: SPC-106B-A390
市场价: ¥6720.00
美元价: 4032.00
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

Rabbit Anti-Human HSP27 Polyclonal

Species Reactivity Dog, Human, Mouse, Gummy Shark (Mustelus antarcticus), School Shark (Galeorhinus galeus), Shark
Applications WB, ICC/IF, FCM, FACS
Antibody Dilution WB (1:2000), ICC/IF (1:250); optimal dilutions for assays should be determined by the user.
Host Species Rabbit
Immunogen Species Human
Immunogen Human HSP27, His tagged
Concentration 1.38 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 A purified
Clonality Polyclonal
Specificity Detects ~27kDa.
Cite This Product StressMarq Biosciences Cat# SPC-106, RRID: AB_11229711
Certificate of Analysis A 1:2000 dilution of SPC-106 was sufficient for detection of HSP27 in 20 µg of HeLa cell lysate by ECL immunoblot 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). 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>Immunocytochemistry/Immunofluorescence analysis using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-106). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-106) at 1:250 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Rabbit (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Mitochondrion matrix. Magnification: 100x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp27 Antibody. (C) Composite. Heat Shocked at 42°C for 1h.</p>

Immunocytochemistry/Immunofluorescence analysis using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-106). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-106) at 1:250 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Rabbit (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Mitochondrion matrix. Magnification: 100x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp27 Antibody. (C) Composite. Heat Shocked at 42°C for 1h.

<p>Western blot analysis of Human HeLa cell lysates showing detection of HSP27 protein using Rabbit Anti-HSP27 Polyclonal Antibody (SPC-106). Load: 15 µg protein. Block: 1.5% BSA. Primary Antibody: Rabbit Anti-HSP27 Polyclonal Antibody (SPC-106) at 1:2000 for 2 hours at RT. Secondary Antibody: Donkey Anti-Rabbit IgG: HRP for 1 hour at RT.</p>

Western blot analysis of Human HeLa cell lysates showing detection of HSP27 protein using Rabbit Anti-HSP27 Polyclonal Antibody (SPC-106). Load: 15 µg protein. Block: 1.5% BSA. Primary Antibody: Rabbit Anti-HSP27 Polyclonal Antibody (SPC-106) at 1:2000 for 2 hours at RT. Secondary Antibody: Donkey Anti-Rabbit IgG: HRP for 1 hour at RT.

<p>Immunocytochemistry/Immunofluorescence analysis using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-106). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-106) at 1:250 for 12 hours at 4°C. Secondary Antibody: APC Goat Anti-Rabbit (red) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Mitochondrion matrix. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp27 Antibody. (C) Composite. Heat Shocked at 42°C for 1h.</p>

Immunocytochemistry/Immunofluorescence analysis using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-106). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-106) at 1:250 for 12 hours at 4°C. Secondary Antibody: APC Goat Anti-Rabbit (red) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Mitochondrion matrix. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-Hsp27 Antibody. (C) Composite. Heat Shocked at 42°C for 1h.

Product Citations (1)

Western Blot

Protective effect of a molecular chaperone inducer, paeoniflorin, on the HCl- and ethanol-triggered gastric mucosal injury.

Asai, M. et al. (2011) Life Sci. 88 (7-8): 350-357.

PubMed ID: 21167840 Reactivity Mouse Applications: Western Blot

  ATTO 390
Overview:

  • High fluorescence yield
  • Large Stokes-shift (89 nm)
  • Good photostability
  • Moderately hydrophilic
  • Good solubility in polar solvents
  • Coumarin derivate, uncharged
  • Low molar mass: 343.42 g/mol 

ATTO 390 Datasheet

ATTO 390 Fluorescent Dye Excitation and Emission SpectraOptical Properties:

λex = 390 nm

λem = 479 nm

εmax = 2.4×104

Φf = 0.90

τfl = 5.0 ns

Brightness = 21.6

Laser = 365 or 405 nm

 

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。