HSP70 Protein (full length)

Catalog No. ABIN1686694

Product Details

Target: HSP70 (Heat Shock Protein 70 (HSP70))

Protein Type: Recombinant

Protein Characteristics: full length

Origin: Human

Source: Baculovirus infected Insect Cells

Application: SDS-PAGE (SDS), Western Blotting (WB), Functional Studies (Func), Activity Assay (AcA), ELISA

Sequence: MAKAAAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTGA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVG YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSCIPPAPGV PQIEVTFDID ANGILNVTAT KDSTGKANKI TITNDKGRLS KEEIERMVQE AEKYKAEDEV QRERVSAKNA LESYAFNMKS AVEDEGLKGK ISEADKKKVL DKCQEVISWL DANTLAEKDE FEHKRKELEQ VCNPIISGLY QGAGGPGPGG FGAQGPKGGS GSGPTIEEVD

Specificity: ~70 kDa

Characteristics: The protein tested positive for ATPase activity using a Malachite Green assay.

Purification: Multi-Step Purified | Endotoxin-free

Purity: >90%

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

This product has been certified >90% pure using SDS-PAGE analysis. The protein tested positive for ATPase activity using a Malachite Green assay.

Restrictions: For Research Use only

Handling

Concentration: Lot specific

Buffer: 50 mM Tris/HCl pH 7.5, 0.3M NaCl, 10 % glycerol, 0.1 mM EDTA

Storage: -20 °C

Target Details

Target: HSP70 (Heat Shock Protein 70 (HSP70))

Alternative Name: Hsp70 (HSP70 Products)

Synonyms: APG-2 Protein, HS24/P52 Protein, HSPH2 Protein, RY Protein, hsp70 Protein, hsp70RY Protein, CG31354 Protein, HSP70 Protein, Hsp70Bb Protein, hsp70B Protein, hsp70Bb-prime Protein, DmelCG5834 Protein, CG5834 Protein, HSPA1 Protein, HSP70B' Protein, HSPA6 Protein, ARABIDOPSIS HEAT SHOCK PROTEIN 70 Protein, ATHSP70 Protein, heat shock protein 70 Protein, LOC100305036 Protein, hsc70 Protein, Hsp70 Protein, Hsp70-1 Protein, Hsp70.1 Protein, hsp68 Protein, Hsp110 Protein, irp94 Protein, HSP70-2 Protein, HSPA1B Protein, HSPA2 Protein, hsp70-5 Protein, HSP70-1 Protein, HSP70.1 Protein, HSP70.2 Protein, heat shock protein family A (Hsp70) member 4 Protein, CG5834 gene product from transcript CG5834-RA Protein, heat shock protein 70 Protein, heat shock protein family A (Hsp70) member 6 Protein, heat shock 70kDa protein 2 Protein, heat shock 70 kD protein cognate Protein, Hsp70 family chaperone Protein, Heat shock protein 70 Protein, Heat shock protein 70, putative Protein, heat shock protein 1B Protein, heat shock protein family A member 4 Protein, heat shock 70kDa protein 1A Protein, heat shock protein 1 Protein, Heat Shock Protein Protein, heat shock cognate 70-kd protein Protein, Heat shock 70 kDa protein 1A Protein, HSPA4 Protein, Hsp70Bbb Protein, HSP70 Protein, HSPA6 Protein, HSPA2 Protein, PCC7424_2419 Protein, Isop_1041 Protein, CGB_C3390W Protein, Bacsa_1698 Protein, dnaK-B Protein, LOC100305036 Protein, Hspa1b Protein, Hspa4 Protein, HSPA1A Protein, hsp1 Protein, hsp-70 Protein, hsp70 Protein, LOC108348108 Protein

Background: HSP70 genes encode abundant heat-inducible 70- kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50 % identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.

Molecular Weight: approx. 70 kDa

Gene ID: 3303