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当前位置: 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP60 (P. Falciparum) Antibody/SPC-185C/25-µg
商品详细StressMarq/Anti-HSP60 (P. Falciparum) Antibody/SPC-185C/25-µg
StressMarq/Anti-HSP60 (P. Falciparum) Antibody/SPC-185C/25-µg
StressMarq/Anti-HSP60 (P. Falciparum) Antibody/SPC-185C/25-µg
商品编号: SPC-185C
市场价: ¥2980.00
美元价: 1788.00
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 HSP60 (P. Falciparum) Antibody
Description

Rabbit Anti-P. Falciparum HSP60 (P. Falciparum) Polyclonal

Species Reactivity Bacteria, E. coli (Escherichia coli), Plasmodium falciparum
Applications WB, ICC/IF
Antibody Dilution WB (1:2000); optimal dilutions for assays should be determined by the user.
Host Species Rabbit
Immunogen Species P. Falciparum
Immunogen Recombinant full length PfHSP60
Concentration 1.83 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 ~ 60kDa. Cross-reacts with E.coli HSP60, GroEl.
Cite This Product StressMarq Biosciences Cat# SPC-185, RRID: AB_1608348
Certificate of Analysis 0.9 µg/ml of SPC-185 was sufficient for detection of PfHSP60 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 CH60_PLAFG Antibody, Chaperonin CPN60 Antibody, mitochondrial Antibody
Research Areas Cancer, Heat Shock
Cellular Localization Mitochondrion, Mitochondrion Matrix
Accession Number XM_001347402.1
Swiss Prot P34940
Scientific Background In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. HSP60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian HSP60 (1-3). Whereas mammalian HSP60 is localized within the mitochondria, plant HSP60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that HSP60 is present in so many different species. The common characteristics of the HSP60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, HSP60 with its co-chaperonin, HSP10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of HSP60-HSP10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of HSP60 and HSP10 is their protective functions against infection and cellular stress. HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
References 1. Hartl F.U. (1996) Nature 381: 571-579.
2. Bukau B., and Horwich A.L. (1998) Cell 92: 351-366.
3. Hartl F.U and Hayer-Hartl M. (2002) Science 295: 1852-1858.
4. Jindal S., et al. (1989) Molecular and Cellular Biology 9: 2279-2283.
5. La Verda D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64-71.
6. Itoh H., et al. (2002) Eur. J. Biochem. 269: 5931-5938.
7. Gupta S. and Knowlton A.A. J. Cell Mol Med. 9: 51-58.
8. Deocaris C.C., et al. (2006) Cell Stress Chaperones 11: 116-128.
9. Lai H.C., et al. (2007) Am. J. Physiol. Endocrinol. Metab 292: E292-E297.

Product Images

<p>Western blot analysis of Parasite Lysates showing detection of HSP60 protein using Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185). Primary Antibody: Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185) at 1:1000.</p>

Western blot analysis of Parasite Lysates showing detection of HSP60 protein using Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185). Primary Antibody: Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185) at 1:1000.

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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。