提醒:代购产品,无质量问题不接受退换货,下单前请仔细核对信息。下单后请及时联系客服 核对商品价格,订单生效后再付款。
StressMarq/Anti-HSP27 Antibody (pSer15)/SPC-1263D-APC/100-µl
价格:

自营商城

解放采购

正品保障

及时交付

厂家直采

一站服务

货号:
品牌:
会员服务:
尊享会员价
贵宾专线
运费优惠
闪电退款
福利优惠
上门换新
友情提示
以上价格仅为参考,请联系客服询价。
免费咨询热线
4000-520-616
产品说明
Overview: Product Name HSP27 Antibody (pSer15) DescriptionRabbit Anti-Human HSP27 (pSer15) Polyclonal Species Reactivity Human, Mouse, Rat Applications WB, IHC, ICC/IF Antibody Dilution WB (1:1000), IHC (1:100), ICC/IF (1:200); optimal dilutions for assays should be determined by the user. Host Species Rabbit Immunogen Species Human Immunogen Synthesized phosphopeptide derived from human HSP27 around the phosphorylation site of serine15 (G-P-SP-W-D). 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 HSP27only when phosphorylated at serine 15. Cite This Product StressMarq Biosciences Cat# SPC-1263, RRID: AB_2712539 Certificate of Analysis A 1:1000 dilution of SPC-1263 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 Immunohistochemistry analysis using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263). Tissue: Breast Carcinoma Tissue. Species: Human. Fixation: Formalin fixed paraffin-embedded. Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263) at 1:1000. The image on the right is treated with the synthesized peptide. Western blot analysis of Human HeLa cell lysates showing detection of ~27kDa Hsp27 protein using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263). Lane 1 and Lane 2: Human HeLa, Hsp27 Antibody (Ser15). Lane 3 and Lane 4: Human HeLa, Hsp27 Antibody (pSer15). Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263) at 1:1000. Predicted/Observed Size: ~27kDa. Product Citations (0) Currently there are no citations for this product.APC (Allophycocyanin)Overview:High quantum yieldLarge phycobiliprotein6 chromophores per moleculeIsolated from red algaeMolecular Weight: 105 kDaAPC Datasheet Optical Properties:λex = 650 nmλem = 660 nmεmax = 7.0×105Φf = 0.68Brightness = 476Laser = 594 or 633 nmFilter set = Cy®5 

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。

客服在线
service-logo
已有 人查看该问题
tel
全国免费服务热线
4000-520-616
微信公众号
关注我们
手机扫码,关注动态