基本信息：

中文名称：

ActivAbTMHS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B 抗体封闭肽

英文名称：

ActivAbTMHS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B Antibody Blocking Peptide

别名：

HSP70-Hom,HSP70-1,HSP70.1,HSP72,HSPA1,HSX70,HSP70-2,HSP70.2,HSP72

外观(性状)：

Lyophilized powder

来源：

Synthetic

储存条件：

Store at -20°C. Avoid freeze / thaw cycles.

运输条件：

冷冻运输

规格：

500ug



生物活性：

应用：

Blocking Peptide of K109870P Antibody

纯化方法：

HPLC

背景说明：

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins.It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria.Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides,activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response.(Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation.(Microbial infection)In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.

生物活性：

Not tested

该产品为 HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B 抗体的抗原肽，在抗体检测、纯化时作为封闭肽使用，对应抗体货号为：K109870P。
抗体封闭肽是一类专门用于免疫学检测体系的功能性合成多肽，其核心作用是通过特异性结合干扰性抗体或非特异性结合位点，从而降低实验背景信号，提高检测结果的准确性和可靠性。它并不直接识别目标抗原，而是充当一种“分子屏蔽层”，封闭那些可能导致假阳性或假阴性结果的非特异性相互作用。
在功能层面，抗体封闭肽主要具备两大特性。一是高亲和力的特异性中和能力——其氨基酸序列与检测体系中可能引起交叉反应的抗体表位完全相同或高度同源，因此能够优先与这些干扰抗体结合，占据其活性位点。二是物理屏蔽作用，即在不干扰靶标抗原与检测抗体正常识别的前提下，封闭固相载体或捕获分子上的空缺结合区域，减少杂蛋白或杂抗体的非特异性吸附。
在应用层面，抗体封闭肽广泛应用于各类免疫分析技术中，包括酶联免疫吸附测定、蛋白质印迹、免疫组化以及免疫层析试纸条等。在自身抗体检测、生物制剂的免疫原性分析以及多重免疫检测方法开发中，它能够有效消除由异嗜性抗体、抗物种抗体或样本基质效应引起的背景干扰。此外，在基于标签融合蛋白的表达检测以及抗体亲和纯化流程中，封闭肽同样扮演着关键角色，可作为竞争性洗脱剂或信号校正控制组使用。
注意事项：
1.本产品仅供科研使用，请勿用于医药、临床治疗、食品及化收品等用途 。
2.为了您的安全和健康，请穿实验服，口罩，护目镜，并戴一次性手套操作。
3.实验结果可由多种因素影响，相关处理只限于产品本身，不涉及其他赔偿。
4.请勿存放于普通住宅区。

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