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当前位置： 首页 > 产品中心 > acid_base_buffer_solution > STRESTMARQ/HSP70蛋白质/SPR-115A/50-微克
商品详细STRESTMARQ/HSP70蛋白质/SPR-115A/50-微克
STRESTMARQ/HSP70蛋白质/SPR-115A/50-微克
STRESTMARQ/HSP70蛋白质/SPR-115A/50-微克
商品编号： SPR-115A
市场价： ¥5740.00
美元价： 3444.00
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 Protein
Description

Active Human Recombinant HSP70 Protein

Applications WB, SDS-PAGE, ATPase Activity Assay, Functional Assay, ELISA
Concentration Lot/batch specific. See included datasheet.
Conjugates His tag

Properties

Storage Buffer 20mM Tris, 150mM NaCl, 10% glycerol
Storage Temperature -20ºC
Shipping Temperature Blue Ice or 4ºC
Purification Affinity Purified, Endotoxin-free
Specificity ~70 kDa
Cite This Product Human Recombinant HSP70 Protein (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-115)
Certificate of Analysis This product has been certified >90% pure using SDS-PAGE analysis. The protein tested positive for ATPase activity using a Malachite Green assay.

Biological Description

Alternative Names HSP70 1 Protein, HSP70 2 Protein, HSP70.1 Protein, HSP72 Protein, HSP73 Protein, HSPA1 Protein, HSPA1A Protein, HSPA1B Protein
Research Areas Cancer, Heat Shock
Cellular Localization Cytoplasm
Accession Number NM_005345
Gene ID 3303
Swiss Prot P08107
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 44kDa 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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
References 1. Zho J. (1998) Cell. 94: 471-480.
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. Natl Acad. Sci. USA. 89: 7290-7294.
6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2): 869-876.
8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11): 6200-6207.
9. Fernandez-Funez et al., (2000) Nature. 408(6808): 101-106.

Product Images

<p>SDS-Page of endotoxin-free his-tagged 70kDa human Hsp70 protein (SPR-115).</p>

SDS-Page of endotoxin-free his-tagged 70kDa human Hsp70 protein (SPR-115).

Product Citations (3)

Western Blot

The Mesenchymal Precursor Cell Marker Antibody STRO-1 Binds to Cell Surface Heat Shock Cognate 70.

Fitter, S., Gronthos, S., Ooi, S.S. and Zannettino, A.C. (2016) Stem Cells. 35(4):940-951.

PubMed ID: 28026090 Applications: Western Blot

Other Citations

The heat shock response in congeneric land snails (Sphincterochila) from different habitats.

Mizrahi, T., Heller, J., Goldenberg, S. and Arad, Z. (2012) Cell Stress Chaperones. 17 (5): 639-645.

PubMed ID: 22535471 Applications: Western Blot Control

Heat shock proteins and resistance to desiccation in congeneric land snails.

Mizrahi, T., Heller, J., Goldenberg, S. and Arad, Z. (2010) Cell Stress Chaperones. 15 (4): 351-363.

PubMed ID: 19953352 Applications: Western Blot Control

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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