Recombinant Human 78 kDa glucose-regulated protein | MyBioSource MBS1265212 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human 78 kDa glucose-regulated protein

catalog :

MBS1265212

quantity :

0.05 mg (E-Coli)

price :

165 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS1265212

products type :

Recombinant Protein

products full name :

Recombinant Human 78 kDa glucose-regulated protein

products short name :

78 kDa glucose-regulated

products name syn :

Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; 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; heat shock protein family A (Hsp70) member 5; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein; BiP

products gene name :

GRP78

other gene names :

HSPA5; HSPA5; BIP; MIF2; GRP78; HEL-S-89n; GRP78; GRP-78; BiP

uniprot entry name :

GRP78_HUMAN

host :

E Coli

sequence positions :

25-293

sequence length :

654

sequence :

EDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITP
SYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRT
WNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFA
PEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQ
RQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKN
ILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDF
DQRVMEHFIKLYKKKTGKDVR

purity :

Greater than 90% as determined by SDS-PAGE.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

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.

products references :

Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene structure, conservation, and regulation.Ting J., Lee A.S.DNA 7:275-286(1988) Chao C.C.K. Grp78 is involved in the quality control of the LDL-receptor.Hansen J.J., Nielsen M.N., Jorgensen M.M., Gregersen N., Bolund L. Sequence differences between human grp78/BiP isolated from HeLa cells and previously reported human sequences.Bermudez-Fajardo A., Llewellyn D.H., Campbell A.K., Errington R.R.NIEHS SNPs programDNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004)

ncbi gi num :

16507237

ncbi acc num :

NP_005338.1

ncbi gb acc num :

NM_005347.4

uniprot acc num :

P11021

ncbi mol weight :

33.7kD

ncbi pathways :

ATF6-alpha Activates Chaperone Genes Pathway (1268758); ATF6-alpha Activates Chaperones Pathway (1268757); Adaptive Immune System Pathway (1269171); Antigen Presentation: Folding, Assembly And Peptide Loading Of Class I MHC Pathway (1269194); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Cellular Response To Heat Stress Pathway (1270421); Cellular Responses To Stress Pathway (1270414); Class I MHC Mediated Antigen Processing Presentation Pathway (1269192); Hemostasis Pathway (1269340)

ncbi summary :

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 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. Chromosomal Location of Human Ortholog: 9q33.3. Cellular Component: cell surface; endoplasmic reticulum; endoplasmic reticulum lumen; endoplasmic reticulum membrane; ER-Golgi intermediate compartment; focal adhesion; integral to endoplasmic reticulum membrane; melanosome; membrane; midbody; mitochondrion; myelin sheath; nucleus; plasma membrane; signalosome; smooth endoplasmic reticulum. Molecular Function: ATP binding; ATPase activity; calcium ion binding; chaperone binding; enzyme binding; glycoprotein binding; misfolded protein binding; protein binding; protein domain specific binding; ribosome binding; ubiquitin protein ligase binding; unfolded protein binding. Biological Process: blood coagulation; cellular protein metabolic process; cellular response to glucose starvation; cerebellar Purkinje cell layer development; cerebellum structural organization; ER overload response; ER-associated protein catabolic process; negative regulation of apoptosis; negative regulation of transforming growth factor beta receptor signaling pathway; platelet activation; platelet degranulation; positive regulation of cell migration; positive regulation of protein ubiquitination; substantia nigra development; unfolded protein response; unfolded protein response, activation of signaling protein activity

size1 :

0.05 mg (E-Coli)

price1 :

165 USD

size2 :

0.2 mg (E-Coli)

price2 :

275

size3 :

0.5 mg (E-Coli)

price3 :

515

size4 :

1 mg (E-Coli)

price4 :

755

more info or order :

MyBioSource product webpage