StressMarq/Anti-HSP70 Antibody [7FB]/SMC-230D-BI/100-µg-免疫在线蚂蚁淘旗下平台

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商品详细StressMarq/Anti-HSP70 Antibody [7FB]/SMC-230D-BI/100-µg

StressMarq/Anti-HSP70 Antibody [7FB]/SMC-230D-BI/100-µg

商品编号： SMC-230D-BI

品牌： StressMarq Biosciences

市场价： ¥6460.00

美元价： 3876.00

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

Biotin

Properties:

Binds tetrameric avidin proteins including Streptavidin and neuravidin with very high affinity
Molar mass: 244.31 g/mol
Formula: C₁₀H₁₆N₂O₃S
Applications: Western blot, immunohistochemistry, and ELISA

Biotin Datasheet

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。

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