protein

BIP, 20-650aa, Human, His-tag, Recombinant, E Coli

MBS203186

0.1 mg

375 USD

Recombinant Protein

BIP, 20-650aa, Human, His-tag, Recombinant, E Coli

BIP

HSPA5; heat shock 70kDa protein 5; GRP78; glucose-regulated protein 78kD; MIF2; Binding immunoglobulin protein; BIP; Binding immunoglobulin protein 78 kDa glucose regulated protein; Endoplasmic reticulum lumenal Ca2+ binding protein grp78; FLJ26106; Glucose Regulated Protein 78kDa; GRP 78; GRP78; Heat Shock 70kDa Protein 5; HSPA 5; Immunoglobulin Heavy Chain Binding Protein.

78 kDa glucose-regulated protein; 78 kDa glucose-regulated protein; 78 kDa glucose-regulated protein; endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; epididymis secretory sperm binding protein Li 89n; immunoglobulin heavy chain-binding protein; heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein; BiP

BIP

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

GRP78_HUMAN

654

MEEDKKEDVG TVVGIDLGTT YSCVGVFKNG RVEIIANDQG NRITPSYVAF TPEGERLIGD AAKNQLTSNP ENTVFDAKRL IGRTWNDPSV QQDIKFLPFK VVEKKTKPYI QVDIGGGQTK TFAPEEISAM VLTKMKETAE AYLGKKVTHA VVTVPAYFND AQRQATKDAG TIAGLNVMRI INEPTAAAIA YGLDKREGEK NILVFDLGGG TFDVSLLTID NGVFEVVATN GDTHLGGEDF DQRVMEHFIK LYKKKTGKDV RKDNRAVQKL RREVEKAKRA LSSQHQARIE IESFYEGEDF SETLTRAKFE ELNMDLFRST MKPVQKVLED SDLKKSDIDE IVLVGGSTRI PKIQQLVKEF FNGKEPSRGI NPDEAVAYGA AVQAGVLSGD QDTGDLVLLD VCPLTLGIET VGGVMTKLIP RNTVVPTKKS QIFSTASDNQ PTVTIKVYEG ERPLTKDNHL LGTFDLTGIP PAPRGVPQIE VTFEIDVNGI LRVTAEDKGT GNKNKITITN DQNRLTPEEI ERMVNDAEKF AEEDKKLKER IDTRNELESY AYSLKNQIGD KEKLGGKLSS EDKETMEKAV EEKIEWLESH QDADIEDFKA KKKELEEIVQ PIISKLYGSA GPPPTGEEDT AELEHHHHHH

> 90% by SDS - PAGE

Liquid in 20mM Tris pH 8.0, 10% glycerol

1 mg/ml (determined by Bradford assay)

Can be stored at 4 degree C short term (1-2 weeks). For long term storage, aliquot and store at -20 degree C or -70 degree C. Avoid repeated freezing and thawing cycles.

SDS-PAGE

Antigen Species: Human. Tag: His-tag

Expression System: E Coli

Heat Shock Proteins

Binding immunoglobulin protein (BiP) belongs to the family of ~70 kDa heat shock proteins (HSP 70). It is a stress response protein which is induced by agents or conditions that adversely affect endoplasmic reticulum (ER) function. This protein is essential for the proper glycosylation, folding as well as for the maintenance of cell homeostasis and the prevention of apoptosis. Recombinant human BIP protein, fused to His-tag at C-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.

Lee LC., et al. (2009) Clin Chim Acta. 400(1-2):56-62. Racek T., et al. (2008) J Biol Chem. 283(49):34305-14.

16507237

NP_005338.1

NM_005347.4

71 kDa (640 aa)

ATF6-alpha Activates Chaperone Genes Pathway (530770); ATF6-alpha Activates Chaperones Pathway (105905); Adaptive Immune System Pathway (366160); Antigen Presentation: Folding, Assembly And Peptide Loading Of Class I MHC Pathway (366163); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Class I MHC Mediated Antigen Processing Presentation Pathway (366161); Hemostasis Pathway (106028); IRE1alpha Activates Chaperones Pathway (105906); Immune System Pathway (106386)

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]

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; focal adhesion; cell surface; mitochondrion; endoplasmic reticulum lumen; endoplasmic reticulum; 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; calcium ion binding; misfolded protein 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; platelet degranulation; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; substantia nigra development; positive regulation of protein ubiquitination; negative regulation of transforming growth factor beta receptor signaling pathway; blood coagulation; ER overload response; negative regulation of apoptosis; positive regulation of cell migration

0.1 mg

375 USD

0.5 mg

925