Rabbit anti-Human HSPA5 Polyclonal Antibody | anti-HSPA5 antibody
HSPA5, CT (HSPA5, GRP78, 78kD glucose-regulated protein, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70kD protein 5, Immunoglobulin heavy chain-binding protein)
Purified by Protein A affinity chromatography.
Purified by Protein A affinity chromatography.
Dilution: ELISA: 1:1,000
Western Blot: 1:100-500
Immunohistochemistry: 1:50-100
Flow Cytometry: 1:10-50
Western Blot (WB)
(Western Blot analysis in A375, A2058, Hela cell line lysates (35ug/lane) using MBS645158. This demonstrates that MBS645158 detected the HSPA5 protein (arrow).)
Immunohistochemistry (IHC)
(Immunohistochemistry analysis in formalin fixed and paraffin embedded human colon carcinoma using MBS645158 followed by peroxidase conjugation of the secondary antibody and DAB staining. This data demonstrates the use of MBS645158 for immunohistochemistry.)
NCBI and Uniprot Product Information
NCBI Description
The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.[provided by RefSeq, Sep 2010]
Uniprot Description
GRP78: a member of the HSP family of molecular chaperones required for endoplasmic reticulum integrity and stress-induced autophagy. Plays a central role in regulating the unfolded protein response (UPR), and is an obligatory component of autophagy in mammalian cells. May play an important role in cellular adaptation and oncogenic survival. One of the client proteins of GRP78 is protein double-stranded RNA-activated protein-like endoplasmic reticulum kinase (PERK). Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.
Protein type: Heat shock protein; Chaperone
Chromosomal Location of Human Ortholog: 9q33.3
Cellular Component: signalosome; endoplasmic reticulum membrane; cell surface; focal adhesion; smooth endoplasmic reticulum; mitochondrion; endoplasmic reticulum; endoplasmic reticulum lumen; ER-Golgi intermediate compartment; membrane; plasma membrane; melanosome; integral to endoplasmic reticulum membrane; midbody; nucleus
Molecular Function: protein domain specific binding; protein binding; enzyme binding; chaperone binding; ubiquitin protein ligase binding; unfolded protein binding; ATPase activity; ribosome binding; misfolded protein binding; calcium ion binding; glycoprotein binding; ATP binding
Biological Process: platelet activation; ER-associated protein catabolic process; cerebellum structural organization; unfolded protein response; cerebellar Purkinje cell layer development; cellular response to glucose starvation; cellular protein metabolic process; platelet degranulation; substantia nigra development; unfolded protein response, activation of signaling protein activity; positive regulation of protein ubiquitination; negative regulation of transforming growth factor beta receptor signaling pathway; blood coagulation; ER overload response; positive regulation of cell migration; negative regulation of apoptosis