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HSPA1B 抗体 (AA 418-641)

This anti-HSPA1B antibody is a 兔 多克隆 antibody detecting HSPA1B in WB, ELISA 和 IF. Suitable for 人.
产品编号 ABIN7154871
发货至: 中国

Quick Overview for HSPA1B 抗体 (AA 418-641) (ABIN7154871)

抗原

See all HSPA1B 抗体
HSPA1B (Heat Shock 70kDa Protein 1B (HSPA1B))

适用

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宿主

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克隆类型

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多克隆

标记

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This HSPA1B antibody is un-conjugated

应用范围

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Western Blotting (WB), ELISA, Immunofluorescence (IF)
  • 抗原表位

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    AA 418-641

    交叉反应

    纯化方法

    >95%, Protein G purified

    免疫原

    Recombinant Human Heat shock 70 kDa protein 1B protein (418-641AA)

    亚型

    IgG
  • 应用备注

    Recommended dilution: WB:1:1000-1:5000, IF:1:50-1:200,

    限制

    仅限研究用
  • 状态

    Liquid

    缓冲液

    Preservative: 0.03 % Proclin 300
    Constituents: 50 % Glycerol, 0.01M PBS, pH 7.4

    储存液

    ProClin

    注意事项

    This product contains ProClin: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

    储存条件

    -20 °C,-80 °C

    储存方法

    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 抗原

    HSPA1B (Heat Shock 70kDa Protein 1B (HSPA1B))

    别名

    HSPA1B

    背景

    Background: 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 (PubMed:24012426, PubMed:26865365, PubMed:24318877). 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 (PubMed:27708256). 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 (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).

    Aliases: HSPA1B antibody, HSP72 antibody, Heat shock 70 kDa protein 1B antibody, Heat shock 70 kDa protein 2 antibody, HSP70-2 antibody, HSP70.2 antibody

    UniProt

    P0DMV9
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