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  4. HSPA8/HSC70 Protein, Human (His, Solution)

HSPA8/HSC70 Protein, Human (His, Solution)

Cat. No.: HY-P73915
COA Handling Instructions

HSPA8/HSC70 is a molecular chaperone that protects the proteome and aids in peptide folding, transport, chaperone-mediated autophagy, and protein complex regulation. It is central to quality control, ensuring correct folding and targeting misfolded proteins for degradation through ATP-dependent cycles. HSPA8/HSC70 Protein, Human (His, Solution) is the recombinant human-derived HSPA8/HSC70 protein, expressed by E. coli , with N-His labeled tag. The total length of HSPA8/HSC70 Protein, Human (His, Solution) is 646 a.a., with molecular weight of ~65 kDa.

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Description

HSPA8/HSC70 is a molecular chaperone that protects the proteome and aids in peptide folding, transport, chaperone-mediated autophagy, and protein complex regulation. It is central to quality control, ensuring correct folding and targeting misfolded proteins for degradation through ATP-dependent cycles. HSPA8/HSC70 Protein, Human (His, Solution) is the recombinant human-derived HSPA8/HSC70 protein, expressed by E. coli , with N-His labeled tag. The total length of HSPA8/HSC70 Protein, Human (His, Solution) is 646 a.a., with molecular weight of ~65 kDa.

Background

HSPA8/HSC70, a molecular chaperone, is intricately involved in diverse cellular processes, including proteome protection from stress, facilitation of polypeptide folding and transport, chaperone-mediated autophagy, activation of misfolded protein proteolysis, and modulation of protein complex formation and dissociation. Central to the protein quality control system, it ensures correct protein folding, refolding of misfolded proteins, and regulates protein targeting for subsequent degradation. This function is orchestrated through cycles of ATP binding, ATP hydrolysis, and ADP release, facilitated by co-chaperones. The nucleotide-bound state of HSP70 regulates its affinity for polypeptides, with ATP-bound form having low substrate affinity, and a conformational change upon ATP hydrolysis increasing the affinity for substrates. Co-chaperones, including J-domain co-chaperones (HSP40s), nucleotide exchange factors (NEFs) such as BAG1/2/3, and TPR domain chaperones like HOPX and STUB1, play specific roles in modulating HSP70 activity. Beyond its fundamental role in mitochondrial import, HSPA8/HSC70 also acts as a repressor of transcriptional activation, participates in the spliceosome assembly, and plays a role in selective protein degradation processes, including chaperone-mediated autophagy and ER-associated degradation. Additionally, it interacts with the VGF-derived peptide TLQP-21, indicating its involvement in diverse cellular pathways.

Biological Activity

Hsp70 has ATPase activity at the time of manufacture of 1.514 µM phosphate liberated/h/µg protein in a 200 µL reaction at 37°C in the presence of 10 μL of 4mM ATP using a Malachite Green assay.

Species

Human

Source

E. coli

Tag

N-His

Accession

P11142-1 (M1-D646)

Gene ID
Molecular Construction
N-term
His
HSPA8 (M1-D646)
Accession # P11142-1
C-term
Synonyms
Heat shock cognate 71 kDa protein; LAP-1; HSPA8; HSC70
AA Sequence

MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD

Molecular Weight

Approximately 65 kDa

Purity

Greater than 90% as determined by reducing SDS-PAGE.

Appearance

Solution.

Formulation

Supplied as a 0.22 μm filtered solution of PBS, 10% glycerol, pH 7.5.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

N/A.

Storage & Stability

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping

Shipping with dry ice.

Documentation

HSPA8/HSC70 Protein, Human (His, Solution) Related Classifications

Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

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The reconstitution calculator equation

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration
= ÷

The dilution calculator equation

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
× = ×
C1   V1   C2   V2

The specific activity calculator equation

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)
Unit/mg = 106 ÷ ng/mL

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HSPA8/HSC70 Protein, Human (His, Solution)
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HY-P73915
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