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当前位置: 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP90 (P. Falciparum) Antibody/SPC-187D-A488/100-µg
商品详细StressMarq/Anti-HSP90 (P. Falciparum) Antibody/SPC-187D-A488/100-µg
StressMarq/Anti-HSP90 (P. Falciparum) Antibody/SPC-187D-A488/100-µg
StressMarq/Anti-HSP90 (P. Falciparum) Antibody/SPC-187D-A488/100-µg
商品编号: SPC-187D-A488
市场价: ¥6820.00
美元价: 4092.00
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 (P. Falciparum) Antibody
Description

Rabbit Anti-P. Falciparum HSP90 (P. Falciparum) Polyclonal

Species Reactivity Plasmodium falciparum
Applications WB, ICC/IF, IP
Antibody Dilution WB (1:2000), ICC/IF (1:50); optimal dilutions for assays should be determined by the user.
Host Species Rabbit
Immunogen Species P. Falciparum
Immunogen Recombinant full length PfHSP90
Concentration 1.56 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 ~ 86kDa. Specific to P. Falciparum and does not cross-react to HSP90 from Human, yeast, and dictyostelium.
Cite This Product StressMarq Biosciences Cat# SPC-187, RRID: AB_1608357
Certificate of Analysis 0.7 µg/ml of SPC-187 was sufficient for detection of PfHSP90 in 20 µg of P. falciparum lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Biological Description

Alternative Names PF14_0417 HSP90 Antibody, Heat shock 86 kDa antibody, heat shock 90kDa protein 1 alpha antibody, Heat shock protein 90kDa alpha cytosolic class A member 1 antibody, Heat shock protein 90kDa alpha cytosolic class B member 1 antibody, Heat shock protein HSP 90 alpha antibody, Heat shock protein HSP 90 beta antibody, Heat shock protein HSP 90-alpha antibody, HSP 84 antibody, HSP 86 antibody, HSP 90 antibody, HSP90 Beta antibody, HSP90A antibody, HSP90AA1 antibody, HSP90AB1 antibody, HSP90B antibody, HSP90N antibody, HSPC1 antibody, HSPC2 antibody, HSPCA antibody, HSPCAL1 antibody, HSPCAL4 antibody, HSPCB antibody, HSPN antibody
Research Areas Cancer, Heat Shock
Cellular Localization Cytoplasm, Melanosome
Accession Number XP_001348591.1
Gene ID 811999
Swiss Prot Q8IL32
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 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 (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 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 (9). Recently, Prof. Tatu’s laboratory has shown the importance of HSP90 in parasite growth. They have shown that inhibition of P. falciparum HSP90 (PfHSP90), blocks the erythrocytic cycle by inhibiting stage transformation, leading to inhibition of parasite growth (10, 11). 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. Banumathy G., Singh V., Pavithra S.R., and Tatu U. (2003) J Biol Chem. 278(20): 18336-45.
11. Pavithra S.R, Banumathy G., Joy O., Singh V., and Tatu U. (2004) J Biol Chem. 279(45):46692-9.

Product Images

<p>Western blot analysis of Parasite Lysates showing detection of HSP90 protein using Rabbit Anti-HSP90 Polyclonal Antibody (SPC-187). Primary Antibody: Rabbit Anti-HSP90 Polyclonal Antibody (SPC-187) at 1:2000.</p>

Western blot analysis of Parasite Lysates showing detection of HSP90 protein using Rabbit Anti-HSP90 Polyclonal Antibody (SPC-187). Primary Antibody: Rabbit Anti-HSP90 Polyclonal Antibody (SPC-187) at 1:2000.

Product Citations (1)

Other Citations

A Purine Analog Synergizes with Chloroquine (CQ) by Targeting Plasmodium falciparum Hsp90 (PfHsp90).

Shahinas, D. et al. (2013) PLoS ONE. 8(9): e75446.

PubMed ID: 24098696 Reactivity W2 parasite Applications: Immunoprecipitation

  ATTO 488
Overview:

  • High fluorescence yield
  • High photostability
  • Very hydrophilic
  • Excellent solubility in water
  • Very little aggregation
  • New dye with net charge of -1
  • Molar Mass: 804 g/mol 

ATTO 488 Datasheet

  ATTO 488 Fluorophore Excitation and Emission SpectraOptical Properties:

λex = 501 nm

λem = 523 nm

εmax = 9.0×104

Φf = 0.80

τfl = 4.1 ns

Brightness = 72

Laser = 488 nm

Filter set = FITC

 

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。