HSP/Chaperone Antibody Sampler Kit

• 产品编号：CST-9965S      品牌：Cell Signaling Technology       原厂货号：9965S
• 产品分类：抗体 > 一抗 > 复合抗体试剂盒
• 应用分类：

其它组分：

描述：

HSP40 (C64B4) Rabbit mAb兔单抗识别内源性的HSP40总蛋白。HSP60 (D307) Antibody识别内源性的HSP60总蛋白。HSP70 Antibody识别内源性的HSP70K2总蛋白（HSP70-Hom, HSP70-1）。HSP90 (C45G5) Rabbit mAb识别内源性的HSP90总蛋白。HSF1 Antibody识别内源性的HSF1总蛋白。Calnexin (C5C9) Rabbit mAb兔单抗识别内源性的calnexin总蛋白。PDI (C81H6) Rabbit mAb兔单抗识别内源性的PDI总蛋白。BiP (C50B12) Rabbit mAb兔单抗识别内源性的BiP总蛋白。每个抗体都只识别其特异靶标。该多克隆抗体用与人类HSP60中Asp307位点，人类HSP70，或人类HSF1羧基末端附近的氨基酸序列对应的人工合成肽段免疫动物而制成。该抗体使用蛋白A和蛋白亲和层析纯化而得。兔单克隆抗体用与人类BiP中Gly584位点周围、HSP900中Asn300位点周围、HSP40/Hdj1中Glu223位点周围氨基酸序列对应的，或对应于人calnexin和PDI序列的人工合成肽段免疫动物而制成。HSP/Chaperone Sampler Kit提供了一个经济的方式来研究细胞内蛋白质折叠。该工具包包含足够每个一抗完成四次Western blots的一抗和二抗。HSP70和HSP90是正常情况下组成性表达的分子伴侣，能够保持蛋白稳态，并且在环境压力下被诱导（1）。HSP70和HSP90与未折叠蛋白发生相互作用，防止其不可逆聚集，并且以ATP依赖的方式催化其底物的重新折叠（1）。HSP40家族的蛋白质可以与未折叠蛋白质结合，防止其聚集，并将未折叠蛋白质输送至HSP70（2）。HSP60主要被认为是线粒体蛋白，对关键蛋白质转入线粒体后的正确折叠很重要（3）。HSP60也在很多细胞质中出现，可被压力、炎症、免疫反应、与阿茨海默症有关的自身免疫抗体、冠状动脉粥样硬化、多发性硬化和糖尿病诱导（4-7）。分泌型和跨膜型蛋白以多核糖体形式合成，然后转移到内质网中进行常见的二硫键形成、氨基糖基化和折叠。内质网包含很多分子伴侣，包括calnexin、BiP和蛋白质二硫键异构酶 (PDI)。Calenxin是嵌入内质网膜的钙结合蛋白，可以将新合成的糖蛋白保留在内质网内，确保其正确折叠和进行质量控制（8,9）。如果内质网内蛋白折叠被扰乱，Bip合成会增加。接下来，BiP结合到错误的蛋白质上，防止其形成聚集物，并帮助其重新正确折叠（10）。PDI催化蛋白质天然活性形成所需的二硫键形成和异构变化（11）。热休克基因转录被热休克因子（HSF）家族和转录激活因子调节，它们可以结合到所有热休克基因上游的热反应元件（HSE）（12）。在热休克反应衰减时，HSF1被HSP70、HSP40/Hdj-1和HSF结合蛋白1（HSBP1）直接结合抑制（13）。

原厂资料：

Specificity / Sensitivity

HSP40 (C64B4) Rabbit mAb detects endogenous levels of total HSP40 protein. HSP60 (D307) Antibody detects endogenous levels of total HSP60 protein. HSP70 Antibody detects endogenous levels of total HSP70 protein (HSP70-Hom, HSP70-1). HSP90 (C45G5) Rabbit mAb detects endogenous levels of total HSP90 protein. HSF1 Antibody detects endogenous levels of total HSF1 protein. Calnexin (C5C9) Rabbit mAb detects endogenous levels of total calnexin protein. PDI (C81H6) Rabbit mAb detects endogenous levels of total PDI protein. BiP (C50B12) Rabbit mAb detects endogenous levels of total BiP protein. Each of these antibodies recognizes only its specific target.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to Asp307 of human HSP60, corresponding to human HSP70, and corresponding to residues at the carboxy-terminus of human HSF1 protein. Polyclonal antibodies are purified by protein A and peptide affinity chromatography. Rabbit monclonal antibodies are produced by immunizing rabbits with a synthetic peptide corresponding to residues surrounding Gly584 of human BiP, surrounding Asn300 of HSP90, corresponding to Glu223 of human HSP40/Hdj1, corresponding to the sequence of human calnexin, and corresponding to the sequence of human PDI.

Description

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

Background

HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). HSP70 and HSP90 interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP-dependent manner (1). HSP40 family proteins bind unfolded proteins and prevent their aggregation, and deliver unfolded protiens to HSP70 (2). HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria (3). 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 (4-7). 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 (8,9). 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 (10). PDI catalyzes the formation and isomerization of disulfide bonds required to reach a proteins native state (11). 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 (12). During attenuation from the heat shock response, HSF1 is repressed by direct binding of HSP70, HSP40/Hdj-1 and HSF binding protein 1 (HSBP1) (13).

注意事项：

For Research Use Only. Not For Use In Diagnostic Procedures.

Storage: Supplied in 10 mM sodium HEPES (pH 7.5),
150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at
–20°C. Do not aliquot the antibodies