catalog number :
MBS718537
products type :
Recombinant Protein
products full name :
Recombinant Mouse 78 kDa glucose-regulated protein (Hspa5)
products short name :
78 kDa glucose-regulated protein (Hspa5)
products name syn :
78 kDa glucose-regulated protein; GRP-78; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein; BiP
other names :
78 kDa glucose-regulated protein; 78 kDa glucose-regulated protein; 78 kDa glucose-regulated protein; GRP-78; XAP-1 antigen; heat shock 70 kDa protein 5; glucose regulated protein, 78 kDa; immunoglobulin heavy chain-binding protein; heat shock 70kD protein 5 (glucose-regulated protein, 78kD); heat shock protein 5; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein; BiP
products gene name :
Hspa5
products gene name syn :
Hspa5; Grp78
other gene names :
Hspa5; Hspa5; Bip; Sez7; mBiP; Grp78; SEZ-7; Hsce70; baffled; AL022860; AU019543; D2Wsu17e; D2Wsu141e; Grp78; GRP-78; BiP
uniprot entry name :
GRP78_MOUSE
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
20-655; Mature full length protein;
sequence :
EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQ
GNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAK
RLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGG
QTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPA
YFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDK
REGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTH
LGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRRE
VEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEEL
NMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIP
KIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGD
QDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKK
SQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTG
IPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKIT
ITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNE
LESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIE
WLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPP
TGEEDTSEKDEL
form :
Liquid containing glycerol; lyophilization may be available upon request.
storage stability :
Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.
other info1 :
Species: Mus musculus (Mouse)
products description :
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (By similarity).
ncbi acc num :
NP_001156906.1
ncbi gb acc num :
NM_001163434.1
ncbi pathways :
ATF6-alpha Activates Chaperone Genes Pathway (1000425); ATF6-alpha Activates Chaperones Pathway (1000424); Antigen Processing And Presentation Pathway (83271); Antigen Processing And Presentation Pathway (485); Hemostasis Pathway (1001295); MAPK Signaling Pathway (198294); Metabolism Of Proteins Pathway (970583); Platelet Activation, Signaling And Aggregation Pathway (1001305); Platelet Degranulation Pathway (1001317); Prion Diseases Pathway (101157)
uniprot summary :
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. Cellular Component: signalosome; endoplasmic reticulum membrane; smooth endoplasmic reticulum; cell surface; focal adhesion; mitochondrion; endoplasmic reticulum; endoplasmic reticulum lumen; ER-Golgi intermediate compartment; membrane; cytoplasm; plasma membrane; integral to endoplasmic reticulum membrane; midbody; nucleus; myelin sheath. Molecular Function: protein domain specific binding; protein binding; enzyme binding; ubiquitin protein ligase binding; unfolded protein binding; nucleotide binding; ribosome binding; misfolded protein binding; glycoprotein binding; ATP binding. Biological Process: cellular response to glucose starvation; positive regulation of embryonic development; unfolded protein response, activation of signaling protein activity; cerebellum structural organization; proteolysis involved in cellular protein catabolic process; positive regulation of protein ubiquitination; cerebellar Purkinje cell layer development; negative regulation of transforming growth factor beta receptor signaling pathway; ER overload response; negative regulation of apoptosis; positive regulation of cell migration
size5 :
0.05 mg (Baculovirus)