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HSP70/HSPA1B Protein, Human (SF9, His)

Cat. No.: HY-P73105
COA Handling Instructions

HSP70/HSPA1B protein, a vital molecular chaperone, ensures proteome integrity by protecting from stress, aiding protein folding, activating proteolysis, and regulating protein complex assembly. It maintains accurate folding through ATP cycles and co-chaperones like HSP40s, BAG1/2/3, HOPX, and STUB1. Its acetylation state modulates competitive binding with HOPX and STUB1, dictating roles in protein refolding and degradation during stress. Beyond protein homeostasis, HSP70 regulates centrosome integrity, influences SMAD3 and FOXP3 degradation, and acts as a post-attachment receptor in rotavirus A infection. HSP70/HSPA1B Protein, Human (SF9, His) is the recombinant human-derived HSP70/HSPA1B protein, expressed by Sf9 insect cells, with N-His labeled tag. The total length of HSP70/HSPA1B Protein, Human (SF9, His) is 640 a.a., with molecular weight of ~72.2 kDa.

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  • Biological Activity

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Description

HSP70/HSPA1B protein, a vital molecular chaperone, ensures proteome integrity by protecting from stress, aiding protein folding, activating proteolysis, and regulating protein complex assembly. It maintains accurate folding through ATP cycles and co-chaperones like HSP40s, BAG1/2/3, HOPX, and STUB1. Its acetylation state modulates competitive binding with HOPX and STUB1, dictating roles in protein refolding and degradation during stress. Beyond protein homeostasis, HSP70 regulates centrosome integrity, influences SMAD3 and FOXP3 degradation, and acts as a post-attachment receptor in rotavirus A infection. HSP70/HSPA1B Protein, Human (SF9, His) is the recombinant human-derived HSP70/HSPA1B protein, expressed by Sf9 insect cells, with N-His labeled tag. The total length of HSP70/HSPA1B Protein, Human (SF9, His) is 640 a.a., with molecular weight of ~72.2 kDa.

Background

HSP70/HSPA1B protein, a molecular chaperone, plays a central role in diverse cellular processes crucial for proteome maintenance, encompassing protection from stress, facilitation of the folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins, and the assembly and dissociation of protein complexes. As a key component of the protein quality control system, HSP70 ensures the accurate folding of proteins, refolding of misfolded counterparts, and the targeted degradation of proteins, achieved through cycles of ATP binding, ATP hydrolysis, and ADP release mediated by co-chaperones. These co-chaperones exhibit individual specificity, regulating distinct steps of the ATPase cycle, and influencing substrate folding or degradation. The nucleotide-bound state of HSP70 modulates its affinity for polypeptides, with the ATP-bound form displaying low substrate protein affinity, undergoing a conformational change upon ATP hydrolysis to ADP that increases its affinity for substrate proteins. This dynamic process involves repeated cycles of ATP hydrolysis and nucleotide exchange, permitting cycles of substrate binding and release. Three types of co-chaperones include J-domain co-chaperones (e.g., HSP40s), nucleotide exchange factors (e.g., BAG1/2/3), and TPR domain chaperones (e.g., HOPX and STUB1). HSP70 maintains protein homeostasis during cellular stress by orchestrating protein refolding or degradation, with its acetylation/deacetylation state determining the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form engages in chaperone-mediated protein refolding, transitioning to deacetylation and subsequent binding to ubiquitin ligase STUB1 for ubiquitin-mediated protein degradation. Beyond its role in protein homeostasis, HSP70 regulates centrosome integrity during mitosis and is essential for maintaining a functional mitotic centrosome supporting the assembly of a bipolar mitotic spindle. Additionally, it enhances STUB1-mediated SMAD3 ubiquitination and degradation, facilitates STUB1-mediated inhibition of TGF-beta signaling, and is indispensable for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells during inflammation. In the context of microbial infection, particularly in rotavirus A infection, HSP70 serves as a post-attachment receptor facilitating the virus's entry into the cell.

Biological Activity

Measured by its ability to bind human PARP1 in a functional ELISA.

Species

Human

Source

Sf9 insect cells

Tag

N-His

Accession

P0DMV9 (A2-D641)

Gene ID
Molecular Construction
N-term
His
HSP70 (A2-D641)
Accession # P0DMV9
C-term
Synonyms
Heat shock 70 kDa protein 1B; HSP70-2; HSPA1B; HSP72
AA Sequence

AKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAviTVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD

Molecular Weight

Approximately 72.2 kDa

Purity

Greater than 85% as determined by reducing SDS-PAGE

Appearance

Lyophilized powder.

Formulation

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 500 mM NaCl, pH 7.4, 10% Glycerol. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.

Storage & Stability

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Room temperature in continental US; may vary elsewhere.

Documentation

HSP70/HSPA1B Protein, Human (SF9, His) 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.

  • Reconstitution Calculator

  • Dilution Calculator

  • Specific Activity Calculator

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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HSP70/HSPA1B Protein, Human (SF9, His)
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HY-P73105
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