Recombinant Human Heat shock protein HSP 90-alpha (HSP90AA1), partial
Product Specifications
Product Name Alternative
Heat shock 86KDA ; HSP 86 ; HSP86Lipopolysaccharide-associated protein 2 ; LAP-2 ; LPS-associated protein 2Renal carcinoma antigen NY-REN-38
Abbreviation
Recombinant Human HSP90AA1 protein, partial
Gene Name
HSP90AA1
UniProt
P07900
Expression Region
9-232aa
Organism
Homo sapiens (Human)
Target Sequence
DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSD
Tag
N-terminal 6xHis-tagged
Type
Developed Protein
Source
Yeast
Field of Research
Neuroscience
Relevance
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.
Endotoxin
Not test
Purity
Greater than 90% as determined by SDS-PAGE.
Activity
Not Test
Form
Liquid or Lyophilized powder
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Function
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function
Molecular Weight
27.2 kDa
References & Citations
Nucleotide sequence of a full-length cDNA for 90KDA heat-shock protein from human peripheral blood lymphocytes.Soeda E., Yokoyama K., Yamazaki M., Akaogi K., Miwa T., Imai T.Nucleic Acids Res. 17:7108-7108 (1989)
Storage Conditions
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Protein Length
Partial
Available Sizes
Curated Selection
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