Porcine Glucose Regulated Protein 78 ELISA Kit | GRP78 elisa kit

Porcine Glucose Regulated Protein 78 ELISA Kit

Cat. Num. AAA14385

• Gene Names: HSPA5; BIP; MIF2; GRP78
• Reactivity: Porcine
• Synonyms: Glucose Regulated Protein 78; Porcine Glucose Regulated Protein 78 ELISA Kit; GRP78 elisa kit

• Reactivity: Porcine
• Specificity: No significant cross-reactivity or interference between this analyte and analogues is observed.

• Samples: Serum, Plasma and Tissue Homogenate
• Detection Range: 31.2 mug/ml - 1000 mug/ml.
• Sensitivity: 5.0 mug/ml.
• Assay Type: Sandwich
• Intra-assay Precision: Intra-assay CV (%) is less than 15%.
• Inter-assay Precision: Inter-assay CV (%) is less than 15%. [CV(%) = SD/mean ×100].
• Preparation and Storage: Store all reagents at 2-8 degree C

Related Product Information for GRP78 elisa kit

Background/Introduction: This Quantitative Sandwich ELISA kit is only for in vitro research use only! This kit is intended to be used for determination the level of GRP78 (hereafter termed this analyte) in undiluted original Porcine serum, plasma and tissue homogenate samples.

NCBI and Uniprot Product Information

• NCBI GI #: 386758
• NCBI GeneID: 3309
• UniProt Accession #: P11021; Q2EF78; Q9NPF1; Q9UK02; B0QZ61
• Molecular Weight: 72,333 Da
• NCBI Official Full Name: GRP78, partial
• NCBI Official Synonym Full Names: heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
• NCBI Official Symbol: HSPA5
• NCBI Official Synonym Symbols: BIP; MIF2; GRP78
• NCBI Protein Information: 78 kDa glucose-regulated protein; immunoglobulin heavy chain-binding protein; endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
• UniProt Protein Name: 78 kDa glucose-regulated protein
• Protein Family: 78 kDa glucose-regulated protein
• UniProt Gene Name: HSPA5
• UniProt Synonym Gene Names: GRP78; GRP-78; BiP
• UniProt Entry Name: GRP78_HUMAN

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; smooth endoplasmic reticulum; cell surface; focal adhesion; 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; ubiquitin protein ligase binding; chaperone 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; unfolded protein response, activation of signaling protein activity; platelet degranulation; cellular protein metabolic process; substantia nigra development; 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