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当前位置： 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP70 Antibody [7FB]/SMC-230D-A594/100-µg
商品详细StressMarq/Anti-HSP70 Antibody [7FB]/SMC-230D-A594/100-µg
StressMarq/Anti-HSP70 Antibody [7FB]/SMC-230D-A594/100-µg
StressMarq/Anti-HSP70 Antibody [7FB]/SMC-230D-A594/100-µg
商品编号： SMC-230D-A594
市场价： ¥6540.00
美元价： 3924.00
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 HSP70 Antibody
Description

Rat Anti-Drosophila HSP70 Monoclonal IgG2B

Species Reactivity Fruit Fly (Drosophila melanogaster)
Applications WB, ICC/IF, ELISA
Antibody Dilution WB (1:2000); optimal dilutions for assays should be determined by the user.
Host Species Rat
Immunogen Species Drosophila
Immunogen Prepared from Drosophila tissue culture cells heat shocked at 36.5◦C for 3 hours, and isolated using SDS PAGE.
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 pH7.4, 50% glycerol, 0.1% sodium azide
Storage Temperature -20ºC
Shipping Temperature Blue Ice or 4ºC
Purification Protein G Purified
Clonality Monoclonal
Clone Number 7FB
Isotype IgG2b
Specificity Detects ~70kDa (heat-inducible form).
Cite This Product StressMarq Biosciences Cat# SMC-230, RRID: AB_2699430
Certificate of Analysis 1 µg/ml of SMC-230 was sufficient for detection of Drosophila HSP70 using an indirect assay with rabbit anti-rat IgG and goat anti-rabbit IgG:HRP.

Biological Description

Alternative Names HSP70Bb Antibody, Heat Shock Protein 70Bb Antibody, dHSP70 Antibody, HSP70b Antibody, HSP70B Antibody, Dm-HSP70 Antibody
Research Areas Cancer, Heat Shock
Accession Number NP_524927.2
Gene ID 48582
Swiss Prot Q9BIS2
Scientific Background HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.
References 1. Welch W.J. and Suhan J.P. (1986) J Cell Biol. 103: 2035-2050.
2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J.Mol. Evol. 38(1): 1-17.
3. Rothman J. (1989) Cell 59: 591-601.
4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887.
5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294.
6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
7. Galan A., et al. (2000) J. Biol. Chem. 275: 11418-11424.
8. Kondo T., et al. (2000) J. Biol. Chem. 275: 8872-8879.
9. Misaki T., et al. (1994) Clin. Exp. Immun. 98: 234-239.
10. Pockley A.G., et al. (1998) Immunol. Invest. 27: 367-377.
11. Moon I.S., et al. (2001) Cereb Cortex 11(3): 238-248.
12. Dressel et al. (2000) J. Immunol. 164: 2362-2371.
13. Verma A.K., et al. (2007) Fish and Shellfish Immunology. 22(5): 547-555.
14. Banduseela V.C., et al. (2009) Physiol Genomics. 39(3): 141-159.

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Product Citations (1)

Western Blot

The heat shock response restricts virus infection in Drosophila.

Merkling, S.H. et al. (2015) Sci Rep. 5:12758.

PubMed ID: 26234525 Reactivity Drosophila Applications: Western Blot

 ATTO 594
Overview:

  • High fluorescence yield
  • High photostability
  • Very hydrophilic
  • Excellent solubility in water
  • Very little aggregation
  • New dye with net charge of -1
  • Molar Mass: 1137 g/mol

ATTO 594 Datasheet

 ATTO 594 Fluorophore Excitation and Emission SpectrumOptical Properties:

λex = 601 nm

λem = 627 nm

εmax = 1.2×105

Φf = 0.85

τfl = 3.5 ns

Brightness = 102

Laser = 594 nm

Filter set = Texas Red®

 

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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