Product info:

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.

Alternative names:

HSPA6; HSP70B

Species reactivity:

Human, Mouse, Rat

Host:

Rabbit

Cellular localisation:

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Isotype:

IgG

Immunogen:

Recombinant fusion protein containing a sequence corresponding to amino acids 474-643 of human HSPA6 (NP_002146.2).

Positive control:

Jurkat, Mouse heart, Rat brain, Rat heart

AA Sequence:

PQIEVTFDIDANGILSVTATDRSTGKANKITITNDKGRLSKEEVERMVHEAEQYKAEDEAQRDRVAAKNSLEAHVFHVKGSLQEESLRDKIPEEDRRKMQDKCREVLAWLEHNQLAEKEEYEHQKRELEQICRPIFSRLYGGPGVPGGSSCGTQARQGDPSTGPIIEEVD

Purification:

Affinity purification

Molecular weight:

Calculated MW: 71kDa Observed MW: 71kDa

Form:

Liquid

Applications:

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Dilution:

WB 1:500 - 1:2000 IHC 1:50 - 1:200

Storage buffer:

Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Storage:

Store at 4°C short term. For long-term storage, aliquot and store at -20°C or below. Stable for 12 months at -20°C. Avoid repeated freeze-thaw cycles.

More info:

Email: info@sobekbio.com

Orders:

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