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Hsc70 抗体

This 大鼠 单克隆 antibody specifically detects Hsc70 in WB, IHC, IP 和 ICC. It exhibits reactivity toward Hamster.
产品编号 ABIN190358
发货至: 中国
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Quick Overview for Hsc70 抗体 (ABIN190358)

抗原

See all Hsc70 (HSPA8) 抗体
Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))

适用

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Hamster

宿主

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大鼠

克隆类型

  • 82
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单克隆

标记

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This Hsc70 antibody is un-conjugated

应用范围

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Western Blotting (WB), Immunohistochemistry (IHC), Immunoprecipitation (IP), Immunocytochemistry (ICC)

克隆位点

1B5
  • 原理

    Anti-Hsc70 (Hsp73) Antibody Rat Monoclonal Antibody

    交叉反应

    小鸡, Cow, 犬, 豚鼠, Hamster, 人, 猴, 小鼠, Pig, 兔, 大鼠, 绵羊

    免疫原

    Hsc70 purified from sodium arsenite treated heat-resistant variants of Chinese hamster cells.

    亚型

    IgG2a
  • 应用备注

    Western Blot: 0.1 μg/mL
    Immunoprecipitation: 5 μg/mL
    Immunohistochemistry: 5 μg/mL
    Immunocytochemistry: 5 μg/mL

    限制

    仅限研究用
  • 状态

    Liquid

    溶解方式

    Dilute in PBS or medium which is identical to that used in the assay system.

    浓度

    Lot specific

    缓冲液

    Phosphate buffered saline, pH 7.2, 0.1 mM PMSF in 50 % glycerol

    储存条件

    4 °C,-20 °C

    储存方法

    Store frozen product at or below -20°C. Thawed product may be stored for 2-4 weeks at 4°C. For optimal storage, aliquot and store at -20°C.
  • 抗原

    Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))

    别名

    HSPA8 / HSC70

    背景

    Heat shock cognate 71 kDa protein,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 (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792). The affinity of HSP70 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. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones 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:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). Interacts with VGF-derived peptide TLQP-21 (PubMed:28934328). {PubMed:10722728, PubMed:11276205, PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:23990462, PubMed:24318877, PubMed:24732912, PubMed:27474739, PubMed:27916661, PubMed:28934328, PubMed:24121476, PubMed:26865365}.,Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.

    基因ID

    600816

    UniProt

    P11142
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