HSP90AA1 Protein, Human, Recombinant (His)

Name: HSP90AA1 Protein, Human, Recombinant (His)
Brand: TargetMol
SKU: TMPH-01429
Rating: 4.5 (1 reviews)

(Synonyms: Renal carcinoma antigen NY-REN-38, Lipopolysaccharide-associated protein 2 (LAP-2;LPS-associated protein 2), HSPCA, HSPC1, HSP90AA1, HSP90A, Heat shock protein HSP 90-alpha, Heat shock protein family C member 1, Heat shock 86 kDa (HSP 86;HSP86)) Copy Product Info

Synonyms: Renal carcinoma antigen NY-REN-38, Lipopolysaccharide-associated protein 2 (LAP-2;LPS-associated protein 2), HSPCA, HSPC1, HSP90AA1, HSP90A, Heat shock protein HSP 90-alpha, Heat shock protein family C member 1, Heat shock 86 kDa (HSP 86;HSP86)

Catalog No. TMPH-01429 Copy Product Info

Purity: 98%

HSP90AA1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 36.0 kDa and the accession number is P07900.

Pack Size	Price	USA Stock	Global Stock
5 µg	$75	20 days	20 days
10 µg	$119	20 days	20 days
20 µg	$198	20 days	20 days
50 µg	$297	20 days	20 days
100 µg	$427	20 days	20 days
200 µg	$658	20 days	20 days
500 µg	$1,170	20 days	20 days
1 mg	$1,830	20 days	20 days

For In stock only · Estimated delivery: USA Stock (1-2 days) Global Stock (5-7 days)

Add to Cart

Add to Quotation

For research use only—not for human use. No sales to individuals. Use as intended only.

Questions

Batch Information

Select Batch

Purity:98%

Appearance:Lyophilized powder

Color:White

Resource Download

COA User Guide of Recombinant Proteins

Product Introduction

Bioactivity

Bioactivity	Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description	HSP90AA1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 36.0 kDa and the accession number is P07900.
Species	Human
Expression System	E. coli
Tag	N-6xHis
Accession Number	P07900
Amino Acid	KTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKK
Construction	292-559 aa
Protein Purity	> 85% as determined by SDS-PAGE.
Endotoxin	< 1.0 EU/μg of the protein as determined by the LAL method.
Formulation	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	Reconstitute the lyophilized protein in sterile deionized water. The product concentration should not be less than 100 μg/mL. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Synonyms	Renal carcinoma antigen NY-REN-38, Lipopolysaccharide-associated protein 2 (LAP-2;LPS-associated protein 2), HSPCA, HSPC1, HSP90AA1, HSP90A, Heat shock protein HSP 90-alpha, Heat shock protein family C member 1, Heat shock 86 kDa (HSP 86;HSP86)
Research Background	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. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Mediates the association of TOMM70 with IRF3 or TBK1 in mitochodria outer membrane which promotes host antiviral response.

Chemical Properties

Molecular Weight

36.0 kDa (predicted)

Storage & Solubility Information

Shipping	In general, lyophilized powders are shipped with blue ice, while solutions are shipped with dry ice.
Storage	Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.