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GRP78 anticorps

Cet anticorps anti-GRP78 est un anticorps Souris Monoclonal détectant GRP78 dans WB, ELISA et IHC. Adapté pour Humain. Ce Primary Antibody a été cité dans 3+ publications.
N° du produit ABIN969204

Aperçu rapide pour GRP78 anticorps (ABIN969204)

Antigène

Voir toutes GRP78 (HSPA5) Anticorps
GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))

Reactivité

  • 198
  • 129
  • 115
  • 36
  • 35
  • 35
  • 32
  • 30
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  • 20
  • 15
  • 5
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  • 4
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  • 2
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
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  • 1
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Humain

Hôte

  • 141
  • 99
  • 8
  • 3
  • 1
  • 1
Souris

Clonalité

  • 141
  • 113
Monoclonal

Conjugué

  • 109
  • 20
  • 16
  • 12
  • 12
  • 12
  • 9
  • 8
  • 8
  • 8
  • 3
  • 3
  • 3
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  • 3
  • 2
  • 2
  • 2
  • 2
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  • 2
Cet anticorp GRP78 est non-conjugé

Application

  • 221
  • 98
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  • 86
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  • 34
  • 32
  • 27
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Western Blotting (WB), ELISA, Immunohistochemistry (IHC)

Clone

4E3
  • Fonction

    HSPA5 Antibody

    Purification

    Ascitic fluid

    Immunogène

    Purified recombinant fragment of human HSPA5 expressed in E. Coli.

    Isotype

    IgG1
  • Indications d'application

    ELISA: 1/10000

    Restrictions

    For Research Use only
  • Format

    Liquid

    Buffer

    Ascitic fluid containing 0.03 % sodium azide.

    Agent conservateur

    Sodium azide

    Précaution d'utilisation

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

    Stock

    4 °C,-20 °C

    Stockage commentaire

    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." dans: 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." dans: 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." dans: Journal of virology, Vol. 83, Issue 23, pp. 12622-5, (2009) (PubMed).

  • Antigène

    GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))

    Autre désignation

    HSPA5

    Sujet

    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.

    Poids moléculaire

    78 kDa

    UniProt

    P11021

    Pathways

    Thyroid Hormone Synthesis, ER-Nucleus Signaling
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