protein

HSP70 (amino acids 1-641) Human, Recombinant, His- tag, E Coli

MBS203037

0.1 mg

255 USD

Recombinant Protein

HSP70 (amino acids 1-641) Human, Recombinant, His- tag, E Coli

HSP70

HSPA1A; HSPA1; HSPA1B; HSP70; HSP70.1; HSP70-1/HSP70-2; Heat shock 70 kDa protein 1; Heat shock 70 kDa protein 1; heat shock 70kDa protein 1A

heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1A/1B; heat shock 70 kDa protein 1A/1B; HSP70-1/HSP70-2; dnaK-type molecular chaperone HSP70-1; epididymis secretory protein Li 103; heat shock 70 kDa protein 1/2; heat shock 70kD protein 1A; heat shock-induced protein; heat shock 70kDa protein 1A; Heat shock 70 kDa protein 1/2; HSP70-1/HSP70-2; HSP70.1/HSP70.2

HSP70

HSPA1A; HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A; HEL-S-103; HSPA1; HSX70; HSP70-1/HSP70-2; HSP70.1/HSP70.2

HSP71_HUMAN

641

MGSSHHHHHH SSGLVPRGSH MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGD TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D

> 95% by SDS - PAGE

Liquid. 20mM Tris pH7.5, 2mM DTT

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

Hsp70 is a human heat shock protein. Hsp70 is an important part of the cell's machinery for protein folding, and help to protect cells from stress. In most species, there are many proteins that belong to the hsp70 family. Some of these are only expressed under stress conditions, while some are present in cells under normal growth conditions and are not heat-inducible. They can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc. ). Recombinant human Hsp70, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.

Gething M-J, et al. (1992). Nature. 355. 33-45. Lewis MJ, et al. EMBO J. (1985) 4:3137-3143.

194248072

NP_005336

NM_005345.5

72.2kDa (661aa), confirmed by MALDI-TOF.

AUF1 (hnRNP D0) Destabilizes MRNA Pathway (187212); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Apoptosis Modulation By HSP70 Pathway (198877); Attenuation Phase Pathway (1127556); Cellular Response To Heat Stress Pathway (1127553); Cellular Responses To Stress Pathway (645258); Direct P53 Effectors Pathway (137939); Disease Pathway (530764); Endocytosis Pathway (102279)

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]

HSP70: a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70. Protein type: Chaperone; Motility/polarity/chemotaxis; Heat shock protein. Chromosomal Location of Human Ortholog: 6p21.3. Cellular Component: signalosome; focal adhesion; mitochondrion; endoplasmic reticulum; inclusion body; ribonucleoprotein complex; cytosol; nucleoplasm; centriole; perinuclear region of cytoplasm; cytoplasm; nuclear speck; nucleus; vesicle; ubiquitin ligase complex. Molecular Function: viral receptor activity; protein binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; ubiquitin protein ligase binding; double-stranded RNA binding; unfolded protein binding; ATPase activity; protein N-terminus binding; ATPase activity, coupled; ATP binding. Biological Process: negative regulation of cell proliferation; entry of virus into host cell; protein stabilization; positive regulation of erythrocyte differentiation; mRNA catabolic process; negative regulation of protein ubiquitination; protein refolding; gene expression; negative regulation of cell growth; response to unfolded protein; negative regulation of apoptosis

0.1 mg

255 USD

0.5 mg

535