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GRP78 抗体

HSPA5 适用: 人 WB, ELISA, IHC 宿主: 小鼠 Monoclonal 4E3 unconjugated
产品编号 ABIN969204
发货至: 中国
  • 抗原 See all GRP78 (HSPA5) 抗体
    GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))
    适用
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    小鼠
    克隆类型
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    单克隆
    标记
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    This GRP78 antibody is un-conjugated
    应用范围
    • 214
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    Western Blotting (WB), ELISA, Immunohistochemistry (IHC)
    原理
    HSPA5 Antibody
    纯化方法
    Ascitic fluid
    免疫原
    Purified recombinant fragment of human HSPA5 expressed in E. Coli.
    克隆位点
    4E3
    亚型
    IgG1
    Top Product
    Discover our top product HSPA5 Primary Antibody
  • 应用备注
    ELISA: 1/10000
    限制
    仅限研究用
  • 状态
    Liquid
    缓冲液
    Ascitic fluid containing 0.03 % sodium azide.
    储存液
    Sodium azide
    注意事项
    This product contains Sodium azide: 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
    Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
  • Tanimoto, Sakaguchi, Abarzua, Kataoka, Kurose, Murata, Nasu, Kumon, Huh: "Down-regulation of BiP/GRP78 sensitizes resistant prostate cancer cells to gene-therapeutic overexpression of REIC/Dkk-3." in: International journal of cancer. Journal international du cancer, Vol. 126, Issue 7, pp. 1562-9, (2010) (PubMed).

    Zhuang, Scolyer, Murali, McCarthy, Zhang, Thompson, Hersey: "Lactate dehydrogenase 5 expression in melanoma increases with disease progression and is associated with expression of Bcl-XL and Mcl-1, but not Bcl-2 proteins." in: Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc, Vol. 23, Issue 1, pp. 45-53, (2010) (PubMed).

    Honda, Horie, Daito, Ikuta, Tomonaga: "Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface." in: Journal of virology, Vol. 83, Issue 23, pp. 12622-5, (2009) (PubMed).

  • 抗原
    GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))
    别名
    HSPA5 (HSPA5 产品)
    背景

    Description: When Chinese hamster K12 cells are starved of glucose, the synthesis of several proteins, called glucose-regulated proteins (GRPs), is markedly increased. Hendershot et al. (1994) (PubMed 8020977) pointed out that one of these, GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), is a member of the heat-shock protein-70 (HSP70) family and is involved in the folding and assembly of proteins in the endoplasmic reticulum (ER). Because so many ER proteins interact transiently with GRP78, it may play a key role in monitoring protein transport through the cell.Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.The HSP70 proteins are ubiquitous molecular chaparones that are found in all organisms and tissue types. Like other members of the HSP70 family, BiP is a peptide-binding ATPase that is able to differentiate native proteins from unfolded polypeptides. BiP does not bind to fully folded and assembled proteins, except in the presence of other co-chaparones. BiP is involved in a number of key mechanisms and pathways including polypeptide translocation across the endoplasmic reticulum, folding, assembly, transport of secreted or membrane proteins, and the regulation of calcium homeostasis. Although BiP is relatively abundant, marked increases in BiP occur where there is an accumulation of unfolded polypeptides. For this reason, BiP has been identified as a marker for various disease states that are associated with secretory and transmembrane protein misfolding.

    Aliases: BIP, MIF2, GRP78, FLJ26106, HSPA5

    分子量
    78kDa
    基因ID
    3309
    HGNC
    3309
    UniProt
    P11021
    途径
    Thyroid Hormone Synthesis, ER-Nucleus Signaling
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