Recombinant Human Heat shock protein HSP 90-alpha(HSP90AA1),partial

Code CSB-EP010802HU1
Product Type Recombinant Protein
Size US$1726
Uniprot No. P07900
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.
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Storage Buffer Tris-based buffer,50% glycerol
Alias Heat shock 86 kDa ;HSP 86 ;HSP86Lipopolysaccharide-associated protein 2 ;LAP-2 ;LPS-associated protein 2Renal carcinoma antigen NY-REN-38
Species Homo sapiens (Human)
Purity Greater than 90% as determined by SDS-PAGE.
Sequence DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSD
Source E.coli
Gene Names HSP90AA1
Expression Region 9-232aa
Tag Info N-terminal 6xHis-SUMO-tagged
Mol. Weight 41.2kDa
Protein Description Partial
Storage 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.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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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
Subcellular Location Nucleus, Cytoplasm, Melanosome, Cell membrane
Protein Families Heat shock protein 90 family
Database Links

HGNC: 5253

OMIM: 140571

KEGG: hsa:3320

STRING: 9606.ENSP00000335153

UniGene: Hs.525600

Pathway Estrogen signaling pathway
PI3K-Akt signaling pathway
Necroptosis
Protein processing in endoplasmic reticulum
Antigen processing and presentation
IL-17 signaling pathway
NOD-like receptor signaling pathway
Th17 cell differentiation

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