HSP60 (P. falciparum) Antibody: RPE-多抗-深圳欣博盛生物科技有限公司

首页产品中心多抗

HSP60 (P. falciparum) Antibody: RPE

品牌：Stressmarq

官网链接

说明书

折扣/货期

货号：SPC-185D-RPE

规格：100 µg

目录价：￥4888.8

产品详情

* 以下信息仅供参考，详情请以原厂网站为准

产品名称:

HSP60 (P. falciparum) Antibody: RPE

别名:

CH60_PLAFG Antibody, Chaperonin CPN60 Antibody, mitochondrial Antibody

产品描述:

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

反应种属:

Plasmodium falciparum | Bacteria | E. coli (Escherichia coli) | Bacteria

宿主来源:

Rabbit

实验应用:

WB | ICC/IF | IHC

靶标/特异性:

Detects ~ 60kDa. Cross-reacts with E.coli HSP60, GroEl.

推荐稀释度:

WB (1:2000); optimal dilutions for assays should be determined by the user.

免疫原:

Recombinant full length PfHSP60

免疫原种属:

P. falciparum

克隆性:

Polyclonal

纯化方式:

Protein A Purified

偶联:

RPE

产品浓度:

1.83 mg/ml

保存温度:

Conjugated antibodies should be stored according to the product label

运输温度:

Blue Ice or 4ºC

存储溶液:

PBS pH7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated

产地:

加拿大

功能与背景:

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).

Accession #:

XM_001347402.1