78 kDa glucose-regulated Recombinant Protein | GRP78 recombinant protein

Recombinant Human 78 kDa glucose-regulated protein

Cat. Num. AAA1265212

• Gene Names: HSPA5; BIP; MIF2; GRP78; HEL-S-89n
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: 78 kDa glucose-regulated; Recombinant Human 78 kDa glucose-regulated protein; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein; BiP; GRP78 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 25-293aa; Partial
• Sequence: EDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVE
• Sequence Length: 654

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for GRP78 recombinant protein

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.

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 and Uniprot Product Information

• NCBI GI #: 16507237
• NCBI GeneID: 3309
• NCBI Accession #: NP_005338.1
• NCBI GenBank Nucleotide #: NM_005347.4
• UniProt Accession #: P11021; Q2EF78; Q9NPF1; Q9UK02; B0QZ61
• Molecular Weight: 33.6 kDa
• NCBI Official Full Name: 78 kDa glucose-regulated protein
• NCBI Official Synonym Full Names: heat shock protein family A (Hsp70) member 5
• NCBI Official Symbol: HSPA5
• NCBI Official Synonym Symbols: BIP; MIF2; GRP78; HEL-S-89n
• NCBI Protein Information: 78 kDa glucose-regulated protein
• 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: 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