HSP70 Protein, Chicken, Recombinant (His)

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.

Pack Size	Availability	Price/USD
20 μg	20 days	$ 360.00
100 μg	20 days	$ 678.00
1 mg	20 days	$ 2,300.00

Pack Size

Availability

Price/USD

Quantity

20 μg

20 days

$ 360.00

100 μg

20 days

$ 678.00

1 mg

20 days

$ 2,300.00

Description

Species	Chicken
Expression System	E. coli
Tag	N-terminal 6xHis-tagged
Accession Number	P08106
Amino Acid	GKGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKYDDPTVQSDMKHWPFRVVNEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGKKVETAVITVPAYFNDSQRQATKDAGTITGLNVMRIINEPTAAAIAYGLDKKGTRAGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNRFVEEFKGKHKRDNAGNKRAVRRLRTACERARRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILMGDKSE Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Construction	3-389 aa
Protein Purity	> 85% as determined by SDS-PAGE.
Molecular Weight	48.6 kDa as predicted

Formulation	If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	A hardcopy of COA with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage	Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shipping	In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background	Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.

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HSP70 Protein, Chicken, Recombinant (His)

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