GRP78 anticorps

N° du produit ABIN969204

Détail du produit anti-GRP78 anticorps

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

Reactivité: Humain

Hôte: Souris

Clonalité: Monoclonal

Conjugué: Cet anticorp GRP78 est non-conjugé

Application: Western Blotting (WB), ELISA, Immunohistochemistry (IHC)

Purification: purified

Immunogène: Purified recombinant fragment of human HSPA5 expressed in E. coli.

Clone: 4-00E-03

Isotype: IgG1

Information d'application

Indications d'application: ELISA: 1:10000, WB: 1:500 - 1:2000, IHC: 1:200 - 1:1000

Restrictions: For Research Use only

Stockage

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: 4°C, -20°C for long term storage

Références pour anticorps anti-GRP78 (ABIN969204)

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).

Détails sur GRP78

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

Autre désignation: HSPA5 (HSPA5 Produits)

Synonymes: anticorps GRP78, anticorps BiP, anticorps GRP-78, anticorps grp78, anticorps hspa5a, anticorps BIP, anticorps MIF2, anticorps AL022860, anticorps AU019543, anticorps Bip, anticorps D2Wsu141e, anticorps D2Wsu17e, anticorps Grp78, anticorps Hsce70, anticorps SEZ-7, anticorps Sez7, anticorps baffled, anticorps mBiP, anticorps cb865, anticorps fb60h09, anticorps fi36d04, anticorps wu:fb60h09, anticorps wu:fi36d04, anticorps zgc:55994, anticorps zgc:77606, anticorps 78 kDa glucose-regulated protein, anticorps heat shock protein family A (Hsp70) member 5, anticorps BiP/GRP78, anticorps glucose-regulated protein 78, anticorps putative glucose-regulated protein 78, anticorps Hsp70 family ATPase KAR2, anticorps heat shock protein family A (Hsp70) member 5 S homeolog, anticorps heat shock 70 kDa protein 5a, anticorps heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa), anticorps heat shock protein 5, anticorps heat shock protein family A member 5, anticorps CpipJ_CPIJ003550, anticorps HSPA5, anticorps grp78, anticorps LOC100533358, anticorps BiP/grp78, anticorps Tc00.1047053506585.40, anticorps Tb11.02.5450, anticorps Tb11.02.5500, anticorps LMJF_28_1200, anticorps KAR2, anticorps LOC100135840, anticorps hspa5.S, anticorps hspa5, anticorps Hspa5

Sujet:

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

Poids moléculaire: 78 kDa

ID gène: 3309

HGNC: 3309

Pathways: Thyroid Hormone Synthesis, ER-Nucleus Signaling