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Manufactured by BioVendor

Heat Shock 70kDa Protein 1A/1B Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Heat shock 70 kDa protein 1/2, HSP70-1/HSP70-2, HSP70.1/HSP70.2, HSPA1A, HSPA1, HSPA1B
  • Species:Human
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Cat. No. Size Price


RD172271100 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 650 AA. MW: 71.16 kDa (calculated). UniProtKB acc.no. P08107. N-Terminal His-tag (10 extra AA)

Amino Acid Sequence

MKHHHHHHASAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD

Source

E. coli

SDS-PAGE Gel

12% SDS-PAGE separation of Human HSP70
1. M.W. marker – 97, 66, 45, 31, 21, 14 kDa
2. reduced and boiled sample, 5μg/lane
3. non-reduced and non-boiled sample, 5μg/lane

Formulation

Filtered (0,4 μm) and lyophilized in 0.5 mg/mL in 0.05 M phosphate buffer, 0.075 M NaCl, pH 7.4

Reconstitution

Add deionized water to prepare a working stock solution of 0.5 mg/mL and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.

Applications

Western blotting, ELISA, Immunoassays

Shipping

On ice. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Summary

Research topic

Diabetology - Other Relevant Products, Others

Summary

The Heat shock protein 70(HSP70) family was found in many intracellular compartments. Members of this protein occur in chloroplasts, endoplasmic reticulum, mitochondria, and cytosol. These proteins are induced by a variety of biological stresses, including heat stress, in every organism. HSP70 serves a variety of roles: It acts as molecular chaperones facilitating the assembly of multi-protein complexes, It participates in the translocation of polypeptides across cell membranes and to the nucleus It aids in the proper folding of nascent polypeptide chains. HSP70 is mitochondrial import machinery and plays key roles in the cytosolic endoplasmic reticulum. Recently, extracellular localized HSP have been found to play key roles in the induction of a cellular immune response.

Summary References (9)

References to Heat Shock 70kDa Protein 1A/1B

  • Boorstein WR, Ziegelhoffer T, Craig EA. Molecular evolution of the HSP70 multigene family. J Mol Evol. 1994 Jan;38 (1):1-17
  • Bork P, Sander C, Valencia A. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci U S A. 1992 Aug 15;89 (16):7290-4
  • DeLuca-Flaherty C, McKay DB, Parham P, Hill BL. Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. Cell. 1990 Sep 7;62 (5):875-87
  • Fernandez-Funez P, Nino-Rosales ML, de Gouyon B, She WC, Luchak JM, Martinez P, Turiegano E, Benito J, Capovilla M, Skinner PJ, McCall A, Canal I, Orr HT, Zoghbi HY, Botas J. Identification of genes that modify ataxin-1-induced neurodegeneration. Nature. 2000 Nov 2;408 (6808):101-6
  • Fink AL. Chaperone-mediated protein folding. Physiol Rev. 1999 Apr;79 (2):425-49
  • Prapapanich V, Chen S, Toran EJ, Rimerman RA, Smith DF. Mutational analysis of the hsp70-interacting protein Hip. Mol Cell Biol. 1996 Nov;16 (11):6200-7
  • Rothman JE. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell. 1989 Nov 17;59 (4):591-601
  • Smith DF, Sullivan WP, Marion TN, Zaitsu K, Madden B, McCormick DJ, Toft DO. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol Cell Biol. 1993 Feb;13 (2):869-76
  • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell. 1998 Aug 21;94 (4):471-80
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