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当前位置: 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP90 Antibody [D7A]/SMC-137D-RPE/100-µg
商品详细StressMarq/Anti-HSP90 Antibody [D7A]/SMC-137D-RPE/100-µg
StressMarq/Anti-HSP90 Antibody [D7A]/SMC-137D-RPE/100-µg
StressMarq/Anti-HSP90 Antibody [D7A]/SMC-137D-RPE/100-µg
商品编号: SMC-137D-RPE
市场价: ¥7040.00
美元价: 4224.00
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 HSP90 Antibody
Description

Mouse Anti-Chicken HSP90 Monoclonal IgG

Species Reactivity Human, Mouse, Rat, Bovine, Chicken, Pig, Rabbit
Applications WB, IHC, IP, ELISA, AM
Antibody Dilution WB (1:500), IP (5µg) ; optimal dilutions for assays should be determined by the user.
Host Species Mouse
Immunogen Species Chicken
Immunogen Full length protein HSP90 purified from chicken brain
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 pH7.2, 50% glycerol, 0.09% sodium azide
Storage Temperature -20ºC
Shipping Temperature Blue Ice or 4ºC
Purification Protein G Purified
Clonality Monoclonal
Clone Number D7A
Isotype IgG
Specificity Recognizes 90kDa. Can isolate complexes of HSP90, Src kinase and cec37.
Cite This Product StressMarq Biosciences Cat# SMC-137, RRID: AB_2121062
Certificate of Analysis 2 µg/ml was sufficient for detection of HSP90α in 20 µg of heat shocked HeLa cell lysate as well as in 100 ng of human HSP90α protein by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

Biological Description

Alternative Names HSP86 Antibody, HSP89A Antibody, HSP90A Antibody, HSP90AA1 Antibody, HSPC1 Antibody, HSPCA Antibody, HsoCAL3 Antibody
Research Areas Cancer, Heat Shock
Cellular Localization Cytoplasm, Melanosome
Accession Number NP_001103255.1
Gene ID 9031
Swiss Prot P11501
Scientific Background HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (4-7). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90- regulated proteins that have been discovered to date are involved in cell signaling (8-9). The number of proteins now known to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase(6). When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immune-adsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (10). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.
References 1. Schuh S. et al. (1985) J Biol Chem. 260 (26): 14292-14296.
2. Lipsich L.A., Cutt J.R. and Brugge J.S. (1982) Mol. Cell Biol. 2(7): 875-880.
3. Brugge J.S., Yonemoto W., and Darrow D. (1983) Mol. Cell. Biol. 3(1): 9-19.
4. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577.
5. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186.
6. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61.
7. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133.
8. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360.
9. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434.
10. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324– 8328.

Product Images

<p>Immunohistochemistry analysis using Mouse Anti-Hsp90 Monoclonal Antibody, Clone D7alpha (SMC-137). Tissue: colon carcinoma. Species: Human. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp90 Monoclonal Antibody (SMC-137) at 1:100000 for 12 hours at 4°C. Secondary Antibody: Biotin Goat Anti-Mouse at 1:2000 for 1 hour at RT. Counterstain: Mayer Hematoxylin (purple/blue) nuclear stain at 200 µl for 2 minutes at RT. Magnification: 40x.</p>

Immunohistochemistry analysis using Mouse Anti-Hsp90 Monoclonal Antibody, Clone D7alpha (SMC-137). Tissue: colon carcinoma. Species: Human. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp90 Monoclonal Antibody (SMC-137) at 1:100000 for 12 hours at 4°C. Secondary Antibody: Biotin Goat Anti-Mouse at 1:2000 for 1 hour at RT. Counterstain: Mayer Hematoxylin (purple/blue) nuclear stain at 200 µl for 2 minutes at RT. Magnification: 40x.

<p>Immunohistochemistry analysis using Mouse Anti-Hsp90 Monoclonal Antibody, Clone D7alpha (SMC-137). Tissue: inflamed colon. Species: Mouse. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp90 Monoclonal Antibody (SMC-137) at 1:100000 for 12 hours at 4°C. Secondary Antibody: Biotin Goat Anti-Mouse at 1:2000 for 1 hour at RT. Counterstain: Mayer Hematoxylin (purple/blue) nuclear stain at 200 µl for 2 minutes at RT. Localization: Inflammatory cells. Magnification: 40x.</p>

Immunohistochemistry analysis using Mouse Anti-Hsp90 Monoclonal Antibody, Clone D7alpha (SMC-137). Tissue: inflamed colon. Species: Mouse. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp90 Monoclonal Antibody (SMC-137) at 1:100000 for 12 hours at 4°C. Secondary Antibody: Biotin Goat Anti-Mouse at 1:2000 for 1 hour at RT. Counterstain: Mayer Hematoxylin (purple/blue) nuclear stain at 200 µl for 2 minutes at RT. Localization: Inflammatory cells. Magnification: 40x.

<p>Western Blot analysis of Rat cell lysates showing detection of Hsp90 protein using Mouse Anti-Hsp90 Monoclonal Antibody, Clone D7Alpha (SMC-137). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp90 Monoclonal Antibody (SMC-137) 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 Rat cell lysates showing detection of Hsp90 protein using Mouse Anti-Hsp90 Monoclonal Antibody, Clone D7Alpha (SMC-137). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp90 Monoclonal Antibody (SMC-137) at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.

Product Citations (3)

Western Blot

Masseter muscle myofibrillar protein synthesis and degradation in an experimental critical illness myopathy model.

Akkad, H., Corpeno, R., Larsson L. (2014) PLoS One. 9(4): e92622.

PubMed ID: 24705179 Reactivity Rat Applications: Western Blot

Other Citations

Biomarker Analysis with Grating Coupled Surface Plasmon Coupled Fluorescence.

Mendoza, A., Dias, J.A., Zeltner, T. and Lawrence, D.A. (2014) J Adv Bio & Biotech. 1(1): 1-22.

PubMed ID: N/A Reactivity Human Applications: Antibody Microarray

Biomarker Analysis with Grating Coupled Surface Plasmon Coupled Fluorescence.

Mendoza, A., Dias, J.A., Zeltner, T. and Lawrence, D.A. (2014) J Adv Bio & Biotech. 1(1): 1-22.

PubMed ID: N/A Reactivity Mouse Applications: Antibody Microarray

  R-PE (R-Phycoerythrin)
Overview:

  • Broad excitation spectrum
  • High quantum yield
  • Photostable
  • Member of the phycobiliprotein family
  • Isolated from red algae
  • Excellent solubility in water
  • Molecular Weight: 250 kDa

R-PE Datasheet

 R-PE Fluorophore Excitation and Emission SpectraOptical Properties:

λex = 565 nm

λem = 575 nm

εmax = 2.0×106

Φf = 0.84

Brightness = 1.68 x 103

Laser = 488 to 561 nm

Filter set = TRITC

 

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。