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Recombinant Human HSF1 Protein, Myc/DDK-tagged, C13 and N15-labeled

Cat.No. : HSF1-3964H
Product Overview : HSF1 MS Standard C13 and N15-labeled recombinant protein (NP_005517) with a C-terminal MYC/DDK tag, was expressed in HEK293 cells.
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Description : The product of this gene is a transcription factor that is rapidly induced after temperature stress and binds heat shock promoter elements (HSE). This protein plays a role in the regulation of lifespan. Expression of this gene is repressed by phosphorylation, which promotes binding by heat shock protein 90.
Source : HEK293
Species : Human
Tag : Myc/DDK
Molecular Mass : 57.1 kDa
AA Sequence : MDLPVGPGAAGPSNVPAFLTKLWTL VSDPDTDALICWSPSGNSFHVFDQG QFAKEVLPKYFKHNNMASFVRQLNM YGFRKVVHIEQGGLVKPERDDTEFQ HPCFLRGQEQLLENIKRKVTSVSTL KSEDIKIRQDSVTKLLTDVQLMKGK QECMDSKLLAMKHENEALWREVASL RQKHAQQQKVVNKLIQFLISLVQSN RILGVKRKIPLMLNDSGSAHSMPKY SRQFSLEHVHGSGPYSAPSPAYSSS SLYAPDAVASSGPIISDITELAPAS PMASPGGSIDERPLSSSPLVRVKEE PPSPPQSPRVEEASPGRPSSVDTLL SPTALIDSILRESEPAPASVTALTD ARGHTDTEGRPPSPPPTSTPEKCLS VACLDKNELSDHLDAMDSNLDNLQT MLSSHGFSVDTSALLDLFSPSVTVP DMSLPDLDSSLASIQELLSPQEPPR PPEAENSSPDSGKQLVHYTAQPLFL LDPGSVDTGSNDLPVLFELGEGSYF SEGDGFAEDPTISLLTGSEPPKAKD PTVSTRTRPLEQKLISEEDLAANDI LDYKDDDDKV
Purity : > 80% as determined by SDS-PAGE and Coomassie blue staining
Stability : Stable for 3 months from receipt of products under proper storage and handling conditions.
Storage : Store at -80 centigrade. Avoid repeated freeze-thaw cycles.
Concentration : 50 μg/mL as determined by BCA
Storage Buffer : 100 mM glycine, 25 mM Tris-HCl, pH 7.3.
Gene Name : HSF1 heat shock transcription factor 1 [ Homo sapiens (human) ]
Official Symbol : HSF1
Synonyms : HSF1; heat shock transcription factor 1; heat shock factor protein 1; HSTF1; HSF 1; HSTF 1;
Gene ID : 3297
mRNA Refseq : NM_005526
Protein Refseq : NP_005517
MIM : 140580
UniProt ID : Q00613

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (7)

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In which cellular compartments is HSF1 predominantly localized? 10/06/2022

HSF1 is predominantly localized in the cytoplasm of cells, and it undergoes nuclear translocation upon activation.

What role does HSF1 play in the regulation of protein homeostasis and the heat shock response? 07/14/2022

The role of HSF1 includes regulating protein homeostasis and the heat shock response, ensuring cellular proteostasis.

What diseases or conditions are associated with dysregulation or abnormal expression of HSF1? 11/07/2020

Dysregulation or abnormal expression of HSF1 is associated with conditions such as cancer, neurodegenerative disorders, and metabolic diseases.

How does HSF1 influence cellular processes such as apoptosis and senescence? 06/07/2020

HSF1 influences cellular processes such as apoptosis and senescence, playing a role in cell fate decisions under stress conditions.

What is the primary function of heat shock factor 1 (HSF1) in cellular stress responses? 02/21/2018

Heat shock factor 1 (HSF1) primarily functions in cellular stress responses, orchestrating the heat shock response.

Are there therapeutic implications or potential targets related to HSF1 in diseases involving cellular stress? 12/19/2017

There are potential therapeutic implications related to HSF1 in diseases involving cellular stress, making it a target for drug development.

How does HSF1 become activated in response to cellular stress, and what are its target genes? 07/03/2016

HSF1 becomes activated in response to cellular stress, such as heat shock, and it induces the expression of heat shock proteins.

Customer Reviews (3)

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Reviews
08/30/2021

    The manufacturer's commitment to open science principles resonated with our lab's dedication to transparent research.

    12/17/2018

      We valued the educational webinars and documentation that enhanced our team's proficiency in utilizing the product.

      12/16/2017

        Its association with impactful research publications contributed to its reputation as a valuable scientific tool.

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