• 概述

• 产品描述 The HSP/Chaperone Kit provides an economical means to investigate protein folding within the cell. The kit contains enough primary and secondary antibodies to perform three Western blot experiments with each antibody.

• 产品

• 产品包括	数量	应用	反应性	MW(kDa)
  HSPA14[ET1612-93]	30μl	WB,IF-Cell,IF-Tissue,IHC-P,IP	Human,Mouse,Rat	Predicted band size: 55 kDa
  Hsp70[ET1601-11]	30μl	WB,IF-Cell,IF-Tissue,IHC-P,FC	Human,Mouse,Rat	Predicted band size: 70 kDa
  GRP78[ER1706-50]	30μl	WB,IF-Cell,IHC-P,FC	Human,Mouse,Rat	Predicted band size: 72 kDa
  HSP40[EM2001-05]	30μl	WB	Human,Mouse,Rat	38 KDa
  Hsp90 beta[ET1605-56]	30μl	WB,IF-Cell,IF-Tissue,IHC-P,IP,FC	Human,Mouse,Rat	83 kDa
  Hsp90 alpha[ET1605-57]	30μl	WB,IF-Cell,IF-Tissue,IHC-P	Human,Mouse,Monkey,Rat	85 kDa
  Calmegin[ET7111-36]	30μl	WB,IHC-P,FC	Human,Mouse,Rat	70 kDa
  P4HB[ET7110-92]	30μl	WB,IF-Cell,IHC-P,FC	Human,Mouse,Rat	57 kDa
  HRP Conjugated Alpaca anti-Rabbit IgG FC, Recombinant VHH[HA1031]	100μl	IP,ELISA,IHC-P,WB	Rabbit	15 kDa
  HRP Conjugated Goat anti-Mouse IgG[HA1006]	100μl	WB,ELISA,IHC-P	Mouse

• 性能

• 数据库链接

• 背景介绍

• HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress. HSP70 and HSP90 interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP-dependent manner . HSP40 family proteins bind unfolded proteins and prevent their aggregation, and deliver unfolded protiens to HSP70 . HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria. HSP60 is also present in the cytosol of many cells and is induced by stress, inflammatory and immune responses, autoantibodies correlated with Alzheimer's, coronary artery diseases, MS, and diabetes. Secretory and transmembrane proteins are synthesized on polysomes and translocate into the endoplasmic reticulum (ER) where they are often modified by the formation of disulfide bonds, amino-linked glycosylation and folding. The ER contains a pool of molecular chaperones including calnexin, BiP and protein disulfide isomerase (PDI). Calenxin is a calcium-binding protein embedded in the ER membrane that retains newly synthesized glycoproteins inside the ER to ensure proper folding and quality control. When protein folding is disturbed inside the ER, Bip synthesis is increased. Subsequently, BiP binds to misfolded proteins to prevent them from forming aggregates and assists them to refold properly . PDI catalyzes the formation and isomerization of disulfide bonds required to reach a proteins native state . Heat shock gene transcription is regulated by a familly of heat shock factors (HSFs), transcriptional activators that bind to heat shock response elements (HSEs) located upstream of all heat shock genes. During attenuation from the heat shock response, HSF1 is repressed by direct binding of HSP70, HSP40/Hdj-1 and HSF binding protein 1 (HSBP1).

• 背景文献

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Specific Protocols

To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.