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Recombinant HSP70 抗体 (C-Term)

The 兔 单克隆 anti-HSP70 antibody is suitable to detect HSP70 in samples from 小鼠. It has been validated for WB, IF, ICC, FACS, IHC (p) 和 IHC (fro).
产品编号 ABIN6943753
发货至: 中国
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中国
北京 101111
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Beijing Economic Technological Development Area
Room 801-803
4A Biotech Co.,Ltd.
Tel +86 (0512) 65829739 传真 +86 (010) 6788 5057

Quick Overview for Recombinant HSP70 抗体 (C-Term) (ABIN6943753)

抗原

See all HSP70 抗体
HSP70 (Heat Shock Protein 70 (HSP70))

抗体类型

Recombinant Antibody

适用

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小鼠

宿主

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克隆类型

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单克隆

标记

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This HSP70 antibody is un-conjugated

应用范围

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Western Blotting (WB), Immunofluorescence (IF), Immunocytochemistry (ICC), Flow Cytometry (FACS), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunohistochemistry (Frozen Sections) (IHC (fro))
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    C-Term

    原理

    Hsp70 Recombinant Antibody

    交叉反应

    人, 小鼠, 大鼠

    纯化方法

    Purified by Protein A.

    免疫原

    Recombinant Mouse Hsp70 from 400 amino acid to C-terminus

    亚型

    IgG
  • 应用备注

    WB(1:1000-2000), IHC-P(1:200-500), IHC-F(1:200-500), IF(1:200-500), Flow-Cyt(1 μg/Test), ICC/IF(1:50-200)

    限制

    仅限研究用
  • 状态

    Liquid

    浓度

    1 mg/mL

    缓冲液

    0.01M TBS ( pH 7.4), 1 % BSA, 0.02 % Proclin 300, and 50 % Glycerol

    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

    4 °C,-20 °C

    储存方法

    Shipped at 4C. Store at -20C for one year. Avoid repeated freeze/thaw cycles.

    有效期

    12 months
  • 抗原

    HSP70 (Heat Shock Protein 70 (HSP70))

    别名

    Hsp70

    背景

    Synonyms: Heat shock 70 kDa protein 1B, HSPA1B, Heat shock 70 kDa protein 1A, HSPA1A

    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). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401).

    UniProt

    P17879, Q61696
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