Heat Shock Protein 70 (HSP70) (full length) (Active) 蛋白

ABIN1686685 产品详细信息, 供应商: Log in to see
蛋白名称
  • HSP70
  • HEAT SHOCK PROTEIN 70
  • HEAT SHOCK PROTEIN 70-7
  • HSC70-7
  • K9P8.5
  • K9P8_5
  • chloroplast heat shock protein 70-2
  • cpHsc70-2
  • F19K16.12
  • F19K16_12
  • LOC100305036
  • hsc70
  • CG31354
  • Hsp70Bb
  • hsp70B
  • hsp70Bb-prime
  • DmelCG5834
  • CG5834
  • APG-2
  • HS24/P52
  • HSPH2
  • RY
  • hsp70
  • hsp70RY
  • hsc71
  • Hsp70
  • Hsp70-1
  • Hsp70.1
  • hsp68
  • Hsp110
  • irp94
  • HSPA1
  • HSP70B'
  • HSPA6
  • ARABIDOPSIS HEAT SHOCK PROTEIN 70
  • ATHSP70
  • heat shock protein 70
  • hsp70-5
  • heat shock 70 kD protein cognate
  • heat shock protein 70-2
  • Heat shock protein 70
  • heat shock protein 70
  • CG5834 gene product from transcript CG5834-RA
  • heat shock 70kDa protein 1A
  • heat shock 70kDa protein 2
  • heat shock 70kDa protein 4
  • heat shock cognate protein 70a
  • heat shock protein 1B
  • heat shock protein 4
  • heat shock protein 70-4
  • heat shock protein1
  • Protein HSP-70
  • LOC692373
  • CPHSC70-2EAT SHOCK PROTEIN 70-2
  • AT1G79920
  • HSP70
  • PCC7424_2419
  • Isop_1041
  • CGB_C3390W
  • Bacsa_1698
  • dnaK-B
  • LOC100305036
  • Hsp70Bbb
  • HSPA1A
  • HSPA2
  • HSPA4
  • hsc70a
  • Hspa1b
  • Hspa4
  • hsp1
  • hsp-70
产品特性
full length
5
2
2
1
宿主

15
6
4
4
3
1
资源
大肠杆菌(E. Coli)
14
3
2
1
蛋白类型
Recombinant
生物活性
Active
应用范围
Activity Assay (AcA), ELISA, Functional Studies (Func), SDS-PAGE (SDS), Western Blotting (WB)
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序列 MAKAAAIGID 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 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
特异性 ~70 kDa
产品特性 The protein has ATPase activity at the time of manufacture of 3.0 µM phosphate liberated/hr/μg protein in a 200 µL reaction at 37 °C (pH 7.5) in the presence of 20 µL of 1 mM ATP using a Malachite Green assay.
纯化方法 Multi-Step Purified
纯度 >95%
ProductDetails: Biological Activity Comment ATPase active
背景 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.
分子量 approx. 70 kDa
基因ID 3303
NCBI登录号 NM_005345
UniProt P08107
研究领域 Heat Shock Proteins
说明

This product has been certified >95% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.0μM phosphate liberated/hr/μg protein in a 200μl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.

限制 仅限研究用
浓度 Lot specific
缓冲液 50 mM Tris/HCl pH 7.5, 2.5 mM Bme, 0.15M NaCl, 10 % glycerol
储存条件 -20 °C
背景 Ionescu-Zanetti, Khurana, Gillespie, Petrick, Trabachino, Minert, Carter, Fink: "Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, Issue 23, pp. 13175-9, 1999 (PubMed).

Fink: "Chaperone-mediated protein folding." in: Physiological reviews, Vol. 79, Issue 2, pp. 425-49, 1999 (PubMed).

Zou, Guo, Guettouche, Smith, Voellmy: "Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1." in: Cell, Vol. 94, Issue 4, pp. 471-80, 1998 (PubMed).

Boorstein, Ziegelhoffer, Craig: "Molecular evolution of the HSP70 multigene family." in: Journal of molecular evolution, Vol. 38, Issue 1, pp. 1-17, 1994 (PubMed).

Bork, Sander, Valencia: "An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 16, pp. 7290-4, 1992 (PubMed).

Rothman: "Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells." in: Cell, Vol. 59, Issue 4, pp. 591-601, 1990 (PubMed).

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