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GRP78 Mouse anti-Human, Clone: C38, eBioscience™

Mouse Monoclonal Antibody

$143.55 - $361.05

Specifications

Antigen GRP78
Clone C38
Host Species Mouse
Gene Alias BiP
Species Reactivity Human
View More Specs

 Disclaimers

For Research Use Only.

Products
Catalog Number Mfr. No. Quantity Price Quantity    

501122847

 
affymetrix
14976880
25μg Each for $143.55

501122848

 
affymetrix
14976882
100μg Each for $361.05
Description & Specifications

Specifications

Antigen GRP78
Clone C38
Host Species Mouse
Gene Alias BiP
Species Reactivity Human
Applications Enzyme Linked Immunosorbent Assay
Applications Flow Cytometry
Applications Immunocytochemistry
Applications Immunohistochemistry
Applications Immunohistochemistry (Formalin/Paraffin)
Applications Microscopy
Regulatory Status RUO
Conjugate Unlabeled
Format Purified
Storage Requirements Store at 2-8°C.
Primary or Secondary Primary
Monoclonal or Polyclonal Monoclonal
Formulation aqueous buffer, 0.09% sodium azide, may contain carrier protein/stabilizer
Concentration 0.5mg/mL

The monoclonal antibody C38 recognizes human glucose-related protein 78 (GRP78). The GRP78 is encoded by the HSPA5 gene and functions as an endoplasmic reticulum (ER) chaperone protein and is a member of the heat shock protein 70 family. GRP78 functions within the ER lumen to facilitate proper protein folding, to prevent intermediates from aggregating, to target misfolded proteins for degradation, and as a calcium binding protein capable of recognizing ER stress and inducing the Unfolded Protein Response (UPR). During normal cellular function, GRP78 is bound to the transmembrane sensor proteins PERK, IRE1, and ATF6, keeping them in an inactive state. During ER stress, GRP78 binds to the hydrophobic residues of unfolded proteins within the ER and releases the sensor proteins, allowing signaling to the nucleus and the initiation of the UPR. During the UPR, protein synthesis is slowed and the transcription of ER chaperones is upregulated, increasing the capacity of the ER.

GRP78 is normally expressed at basal levels in all adult organs and is required for the proliferation and survival of embryonic stem cells. GRP78 expression is upregulated in cancer cells due to the increased numbers of underglycosylated and misfolded proteins responsible for triggering the UPR. In addition to being expressed in the ER, GRP78 is also expressed on the surface of cancer cells. Evidence also suggests that GRP78 plays a role in promoting tumor growth and metastasis by inhibiting apoptosis. GRP78 overexpression confers drug-resistance to chemotherapeutic agents and the level of expression can be correlated with pathologic grade and survival in breast, liver, prostate, colon and gastric cancers.