HSP70 抗体样品

小鼠抗人HSP70单克隆IgG1

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 5O% identity (1). 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 (2). 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 (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). 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 (5). 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. Balashova N. et al. (2005) J Biol Chem 280:2186-96. 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. Nat Acad. Sci. USA 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.

StressMarq Biosciences Inc.位于加拿大维多利亚，是一家生物科技公司，专门从事试剂与试剂盒研究。我们有强大的国际经销商网络，主要为私人和公众客户提供经我们多次试验成功 的试剂，服务范围遍及全球40多个国家。 我们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。 通过定位好以上四个领域，研究人员能够运用研究相关的整套试剂工具，将研究产品重点放在热休克蛋白70和90（HSP70和HSP90）两个核心领域。产 品主要包括ELISA试剂盒、抑制剂、蛋白质（包括无内毒素制剂，而非低内毒素制剂）以及经过高级验证的抗体，产品在全球范围内均有销售。 StressMarq因其试剂验证质量过硬，跻身为高端公司。研究人员能放心使用抗体产品，因为本产品将具有免疫印迹（WB）、免疫沉淀、组织染色技术的 功能，如免疫组织化学（IHC）和免疫细胞化学（ICC）。 本公司提供氧化应激产品，如8OHdG（DNA受损）ELISA试剂盒，同时还提供专门的抗体，适用于非定量技术，如免疫组化。在免疫组化中，组织的目标 可视化更为重要。除了提供用于进一步研究的相关工具外，StressMarq还提供新的尖端研究工具，用于开发新的生物项目，包括全球独一无二的α B晶体蛋白ELISA试剂盒（现在是公认的乳腺癌标志物）以及热休克同源蛋白70（Hsc70）ELISA试剂盒。本公司已将专业技术扩展到抗体、小分子 离子通道与载体等更新领域，前者包括当前热门的核心领域：Nav、Cav、TRP、Kv、KCNQ、HCN，后者包括当前热门的核心领域：ENaC、 NCC和NKCC2以及主要水通道蛋白载体。