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当前位置： 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP90 (Salmon) Antibody/SPC-316D/100-µl
商品详细StressMarq/Anti-HSP90 (Salmon) Antibody/SPC-316D/100-µl
StressMarq/Anti-HSP90 (Salmon) Antibody/SPC-316D/100-µl
StressMarq/Anti-HSP90 (Salmon) Antibody/SPC-316D/100-µl
商品编号： SPC-316D
市场价： ¥6160.00
美元价： 3696.00
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 HSP90 (Salmon) Antibody
Description

Rabbit Anti-Salmon HSP90 (Salmon) Polyclonal

Species Reactivity Human, Fish, Salmon
Applications WB
Antibody Dilution WB (1:5000); optimal dilutions for assays should be determined by the user.
Host Species Rabbit
Immunogen Species Salmon
Immunogen KLH-conjugated synthetic peptide chosen from a highly conserved region of HSP90 found in both the alpha and beta form. The taget peptide is perfectly conserved in animals.
Conjugates Unconjugated

Properties

Storage Buffer Lyophilized rabbit Antiserum. For reconstitution add 100 µl of sterile water.
Storage Temperature -20ºC
Shipping Temperature Blue Ice or 4ºC
Purification Rabbit antiserum
Clonality Polyclonal
Specificity Detects ~90kDa. In salmonid fish a cross-reactive band at 40kDa is observed. Antibody will also detect a Human recombinant HSP90 protein.
Cite This Product StressMarq Biosciences Cat# SPC-316, RRID: AB_2264396
Certificate of Analysis 0.2 µl/ml of SPC-316 was sufficient for detection of HSP90 in 10 µg Heat shocked (25°C) rainbow trout nuclear fraction lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Biological Description

Alternative Names HSP84 Antibody, HSP86 Antibody, HSP90A Antibody, HSP90AA1 Antibody, HSP90AB1 Antibody, HSP90B Antibody, HSPC1 Antibody, HSPC2 Antibody, HSPCAL1 Antibody, HSPCAL4 Antibody, HSP90N Antibody
Research Areas Cancer, Heat Shock
Cellular Localization Cytoplasm, Melanosome
Accession Number NP_001117004.1
Gene ID 100136360
Swiss Prot Q9W6K6
Scientific Background HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology. The two isoforms of HSP90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer.(2) From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite it’s 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. (7-8). The number of proteins now know 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.5 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 immunoadsorption 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 (9). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
References 1. Nemoto T., et al. (1997) J.Biol Chem. 272: 26179-26187.
2. Minami Y., et al. (1991), J.Biol Chem. 266: 10099-10103.
3. Arlander S.J.H., et al. (2003) J Biol Chem 278: 52572-52577.
4. Pearl H., et al. (2001) Adv Protein Chem 59:157-186.
5. Neckers L., et al. (2002) Trends Mol Med 8:S55-S61.
6. Pratt W., Toft D. (2003) Exp Biol Med 228:111-133.
7. Pratt W., Toft D. (1997) Endocr Rev 18:306–360.
8. Pratt W.B. (1998) Proc Soc Exptl Biol Med 217: 420–434.
9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328.
10. Barent R. L. (1998) Mol. Endocrinol. 12: 342-354
11. Lo. M.A. (1998) EMBO J. 17: 6879-6887.

Product Images

<p>Western blot analysis of Rainbow trout Nuclear Fraction showing detection of HSP90 protein using Rabbit Anti-HSP90 Polyclonal Antibody (SPC-316). Lane 1: HSP90 protein standard. Lane 2: Control (13?C) rainbow trout nuclear fraction. Lane 3: Heat Shocked (25?C) rainbow trout nuclear fraction. Lane 4: 24h post heat shock rainbow trout nuclear fraction. Primary Antibody: Rabbit Anti-HSP90 Polyclonal Antibody (SPC-316) at 1:5000.</p>

Western blot analysis of Rainbow trout Nuclear Fraction showing detection of HSP90 protein using Rabbit Anti-HSP90 Polyclonal Antibody (SPC-316). Lane 1: HSP90 protein standard. Lane 2: Control (13?C) rainbow trout nuclear fraction. Lane 3: Heat Shocked (25?C) rainbow trout nuclear fraction. Lane 4: 24h post heat shock rainbow trout nuclear fraction. Primary Antibody: Rabbit Anti-HSP90 Polyclonal Antibody (SPC-316) at 1:5000.

Product Citations (4)

Western Blot

Temporal changes in stress and tissue-specific metabolic responses to municipal wastewater effluent exposure in rainbow trout.

Ings, J.S., Oakes, K.D., Vijayan, M.M., and Servos, M.R. (2012) Comp Biochem Physiol C Toxicol Pharmacol. 156 (2): 67-74.

PubMed ID: 22579662 Reactivity Trout Applications: Western Blot

Differential expression of heat-shock proteins in F2 offspring from F1 hybrids produced between thermally selected and normal rainbow trout strains.

Ojima, N. et al. (2012) Fish Sci. 78 (5): 1051-1057.

PubMed ID: N/A Reactivity Rainbow Trout Applications: Western Blot

Hepatic transcriptomics and protein expression in rainbow trout exposed to municipal wastewater effluent.

Ings, J.S., Servos, M.R. and Vijayan, M.M. (2011) Environ Sci Technol. 45 (6): 2368-2376.

PubMed ID: 21322548 Reactivity Trout Applications: Western Blot

Regulation of Heat Shock Protein 70 Levels in Red Blood Cells of Rainbow Trout.

Henrickson, L. (2010) University of Waterloo Dissertation

PubMed ID: N/A Reactivity Rainbow Trout Applications: Western Blot

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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