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当前位置: 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP70 (P. Falciparum) Antibody/SPC-186D-A390/100-µg
商品详细StressMarq/Anti-HSP70 (P. Falciparum) Antibody/SPC-186D-A390/100-µg
StressMarq/Anti-HSP70 (P. Falciparum) Antibody/SPC-186D-A390/100-µg
StressMarq/Anti-HSP70 (P. Falciparum) Antibody/SPC-186D-A390/100-µg
商品编号: SPC-186D-A390
市场价: ¥6840.00
美元价: 4104.00
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 (P. Falciparum) Antibody
Description

Rabbit Anti-P. Falciparum HSP70 (P. Falciparum) Polyclonal

Species Reactivity Plasmodium falciparum
Applications WB, ICC/IF
Antibody Dilution WB (1:2000), ICC/IF (1:50); optimal dilutions for assays should be determined by the user.
Host Species Rabbit
Immunogen Species P. Falciparum
Immunogen His-tagged and purified PfHSP70, C-terminus (AA 365-681)
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, 0.09% sodium azide
Storage Temperature -20ºC
Shipping Temperature Blue Ice or 4ºC
Purification Protein A purified
Clonality Polyclonal
Specificity Detects ~ 70kDa. Specific to P. Falciparum and does not cross-react to any protein from Human erythrocytes.
Cite This Product StressMarq Biosciences Cat# SPC-186, RRID: AB_1608355
Certificate of Analysis 0.15 µg/ml of SPC-186 was sufficient for detection of PfHSP70 in 20 µg of P. falciparum lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Biological Description

Alternative Names HSP70_PLAFA Antibody, Cytoplasmic antigen 74.3 kDa protein Antibody
Research Areas Cancer, Heat Shock
Cellular Localization Cytoplasm
Accession Number M19753
Swiss Prot P11144
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. PfHSP70-I (PF08_0054) is the major cytosolic HSP70 in Plasmodium falciparum. It is abundantly expressed in the blood stages of the parasite and is thought to constitute 1-2% of total parasite protein. It is induced upon heat shock. It is present in the parasite in different complexes with PfHSP90 and some PfHSP40 (6, 7). Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
References 1. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol.38 (1) 1-17.
2. Rothman J. (1989) Cell 59: 591 -601.
3. DeLuca-Flaherty, et al. (1990) Cell. 62: 875-887.
4. Bork P., Sander C. & Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294.
5. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
6. Pesce E.R., et al. (2008) Int J Biochem Cell Biol. 40(12): 2914-26.
7. Pavithra S.R, Banumathy G., Joy O., Singh V., Tatu U. (2004) J Biol Chem. 279(45): 46692-9.

Product Images

<p>Western blot analysis of Parasite Lysates showing detection of HSP70 protein using Rabbit Anti-HSP70 Polyclonal Antibody (SPC-186). Primary Antibody: Rabbit Anti-HSP70 Polyclonal Antibody (SPC-186) at 1:2000.</p>

Western blot analysis of Parasite Lysates showing detection of HSP70 protein using Rabbit Anti-HSP70 Polyclonal Antibody (SPC-186). Primary Antibody: Rabbit Anti-HSP70 Polyclonal Antibody (SPC-186) at 1:2000.

Product Citations (3)

Western Blot

RIFINs are adhesins implicated in severe Plasmodium falciparum malaria.

Geol, S. et al. (2015) Nat Med. 21(4):314-7.

PubMed ID: 25751816 Reactivity P. falciparum Applications: Western Blot

Immunocytochemistry/Immunofluorescence

Analysis of a Multi-component Multi-stage Malaria Vaccine Candidate—Tackling the Cocktail Challenge.

Boes, A. et al. (2015) PLoS ONE. 10(7):e0131456.

PubMed ID: 26147206 Reactivity P. falciparum Applications: Immunocytochemistry/Immunofluorescence

Biosynthesis of GDP-fucose and Other Sugar Nucleotides in the Blood Stages of Plasmodium falciparum.

Sanz, S. et al. (2013) J Biol Chem. 288, 16506-16517.

PubMed ID: 23615908 Reactivity P. falciparum Applications: Immunocytochemistry/Immunofluorescence

  ATTO 390
Overview:

  • High fluorescence yield
  • Large Stokes-shift (89 nm)
  • Good photostability
  • Moderately hydrophilic
  • Good solubility in polar solvents
  • Coumarin derivate, uncharged
  • Low molar mass: 343.42 g/mol 

ATTO 390 Datasheet

ATTO 390 Fluorescent Dye Excitation and Emission SpectraOptical Properties:

λex = 390 nm

λem = 479 nm

εmax = 2.4×104

Φf = 0.90

τfl = 5.0 ns

Brightness = 21.6

Laser = 365 or 405 nm

 

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。