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Human HSPA1A Protein (Recombinant His) - LS-G18318

Catalog Size Price
LS-G18318-10 10 µg Unavailable
LS-G18318-50 50 µg Unavailable
LS-G18318-1 1 mg Unavailable

Most Popular HSPA1A Proteins

Human HSPA1A Protein (Recombinant) - LS-G3446
E. coli Expression System
661 AA
None
Purified
Sodium Dodecyl Sulfate - Polyacrylamide Gel Electrophoresis Image
Bovine HSPA1A Protein (Recombinant His) (aa1-641) - LS-G13317
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Human HSPA1A Protein (Recombinant His) (aa1-641) - LS-G13322
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Sodium Dodecyl Sulfate - Polyacrylamide Gel Electrophoresis Image
Mouse HSPA1A Protein (Recombinant His) (aa1-641) - LS-G13328
E. coli Expression System
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Purified / Lyophilized
Sodium Dodecyl Sulfate - Polyacrylamide Gel Electrophoresis Image
Human HSPA1A Protein (Recombinant His) - LS-G18318
E. coli Expression System
His
Purified

100% Guaranteed
LS-G18318
Recombinant Protein
HSPA1A
Human
70.0 kDa
HSP 70kDa produced in E.Coli is a single, non-glycosylated polypeptide chain (1-641 a.a.) containing 661 amino acids fused to a 20 a.a. His-tag at N-terminus and having a total Mw of 72.2 kDa.
E. coli
E. coli
His
Greater than 95% by SDS-PAGE
Not Tested
Not Tested
20 mM Tris-HCl, pH 7.5, 20 mM DTT
Store lyophilized at 4°C. Once reconstituted, aliquot and store at -20°C. Avoid freeze-thaw cycles.
For research use only.

About HSPA1A

NM_005345 NP_005336.3

HSPA1A Protein, Heat shock 70kDa protein 1A Protein, Heat shock 70 kDa protein 1/2 Protein, Heat shock 70kD protein 1A Protein, HSP70-1/HSP70-2 Protein, HSPA1 Protein, HSP70-1A Protein, Heat shock 70 kd protein 1 Protein, Heat shock-induced protein Protein, Iroquois homeobox protein 4 Protein, HSP70-1 Protein, Hsp70.1 Protein, HSP70.1/HSP70.2 Protein, HSP70I Protein, HSP72 Protein

In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins.

Requested From: 
Date Requested: 8/24/2017

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