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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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