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折扣/货期| 货号：SMC-104B-RPE | 规格：200 µg | 目录价：￥5670 |
产品详情
产品名称:
HSP70/HSC70 Antibody: RPE
别名:
HSP70 1 Antibody, HSP70 2 Antibody, HSP70.1 Antibody, HSP72 Antibody, HSPA1 Antibody, HSPA1A Antibody, HSPA1B Antibody
产品描述:
Mouse Anti-Human HSP70/HSC70 Monoclonal IgG1
反应种属:
Human | Mouse | Rat | Bovine | Nematode (Caenorhabditis elegans) | Beluga | Dog | Chicken | Fruit Fly (Drosophila melanogaster) | Fish | Guinea Pig (Cavia porcellus) | Hamster | Monkey | Pig | Plant | Cucumber | Pea (Pisum sativum) | Rabbit | Sheep | African clawed frog (Xenopus laevis)
宿主来源:
Mouse
实验应用:
WB | IHC | ICC/IF | IP | FCM | IEM
靶标/特异性:
Detects ~72 (HSP) and ~73kDa (HSC).
同种型:
IgG1
免疫原:
Human Recombinant HSP70/HSC70
免疫原种属:
Human
克隆性:
Monoclonal
克隆号:
N27F3-4
纯化方式:
Protein G Purified
偶联:
RPE
产品浓度:
1 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 pH7.2, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
产地:
加拿大
功能与背景:
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 50% identity (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 locations, 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. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.
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