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当前位置: 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP70 Antibody/SPC-318D-A565/100-µg
商品详细StressMarq/Anti-HSP70 Antibody/SPC-318D-A565/100-µg
StressMarq/Anti-HSP70 Antibody/SPC-318D-A565/100-µg
StressMarq/Anti-HSP70 Antibody/SPC-318D-A565/100-µg
商品编号: SPC-318D-A565
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 HSP70 Antibody
Description

Rabbit Anti-Crab HSP70 Polyclonal

Species Reactivity Crab
Applications WB
Antibody Dilution WB (1:1000); optimal dilutions for assays should be determined by the user.
Host Species Rabbit
Immunogen Species Crab
Immunogen Crab protein peptide: NDQGNRTTPSYVA, 100% identical to a wide variety of species including Mouse, Rat, Drosophilia, Rice, Arabidopsis, Bovine, Nematode, Bonobos.
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 1X 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 ~70kDa.
Cite This Product StressMarq Biosciences Cat# SPC-318, RRID: AB_2704470
Certificate of Analysis 1 µg/ml of SPC-318 was sufficient for detection of HSP70 in 20 µg of crab muscle lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Biological Description

Alternative Names HSP70 1 Antibody, HSP70 2 Antibody, HSP70.1 Antibody, HSP72 Antibody, HSPA1 Antibody, HSPA1A Antibody, HSPA1B Antibody
Research Areas Cancer, Heat Shock
Cellular Localization Cytoplasm
Accession Number AFX62578
Gene ID JX913782
Swiss Prot B3VKG9
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, 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. Looking for more information on HSP70? Visit our new 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. Hung T.H., et al. (2001) Am J Pathol. 159: 1031-1043.
8. Locke M. (2000) Cell Stress & Chaperones 5: 45-51.
9. Ianaro A., et al. (2001) FEBS Lett. 508: 61-66.
10. Trentin G.A. et al. (2001) J Biol Chem. 276: 13087-13095.

Product Images

<p>Western blot analysis of Crab Cell Lysate showing detection of HSP70 protein using Rabbit Anti-HSP70 Polyclonal Antibody (SPC-318). Primary Antibody: Rabbit Anti-HSP70 Polyclonal Antibody (SPC-318) at 1:1000.</p>

Western blot analysis of Crab Cell Lysate showing detection of HSP70 protein using Rabbit Anti-HSP70 Polyclonal Antibody (SPC-318). Primary Antibody: Rabbit Anti-HSP70 Polyclonal Antibody (SPC-318) at 1:1000.

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 ATTO 565
Overview:

  • High fluorescence yield
  • High thermal and photostability
  • Good solubility in polar solvents
  • Excellent solubility in water
  • Very little aggregation
  • Rhodamine dye derivative
  • Molar Mass: 611 g/mol

ATTO 565 Datasheet

 ATTO 565 Fluorophore Excitation and Emission SpectraOptical Properties:

λex = 563 nm

λem = 592 nm

εmax = 1.2×105

Φf = 0.9

τfl = 3.4 n

Brightness = 10

Laser = 532 nm

Filter set = TRITC

 

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。