HSP90AA1 Protein (full length) (rho-1D4 tag)

N° du produit ABIN7126014

Détail du produit

Antigène: HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))

Type de proteíne: Recombinant

Attributs du protein: full length

Origine: CHO cells

Source: Cellules d'insectes

Purification/Conjugué: Cette HSP90AA1 protéine est marqué à la rho-1D4 tag.

Application: Western Blotting (WB), SDS-PAGE (SDS), ELISA, Crystallization (Crys), Functional Studies (Func)

Séquence: MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR YESLTDPSKL DSGKELHINI IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYT AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYMEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED KEEEKEKEEK GIDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF DLFENRKKKN NIKLYVRRVF IMDNCEELFP EYLNFIRGVV DSEDLPLNIS REILQQSKIL KVIRKNLVRK CLELFHELAE DKENYKKFYE QFSKNIKLGI HEDSQNRKKL SELLRYYTSA SGDEMVSLKD YCTRMKENQK HIYFITGETK DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK TLVSVTKEGL ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI VTSTYGWTAN MERIIKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK AEADKNDKSV KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID EDDPTVDDTS AAVTEEMPPL EGDDDTSRME EVD
Sequence without tag. The location of the tag depends on protein. You may also submit your preference when ordering.

Attributs du produit:

• Made in Germany - from design to production - by highly experienced protein experts.
• CHO Heat shock protein HSP 90-alpha Protein (raised in Insect Cells) purified by multi-step, protein-specific process to ensure crystallization grade.
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a custom-made protein and will be made for the first time for your order. This protein will be produced on the basis of on a Custom Service Project. We will make sure that every step in the production is successful from the design of the expression plasmid to the expression and purification of the final protein. Our experts in the lab will ensure that you receive a correctly folded protein.

The concentration of our recombinant proteins is measured using the absorbance at 280nm. The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer. The concentration of the protein is calculated using its specific absorption coefficient. We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

Purification: Three step purification of proteins expressed in baculovirus infected SF9 insect cells:

1. Membrane proteins are fractioned by ultracentrifugation and subsequently solubilized with different detergents (detergent screen). Samples are analyzed by Western blot.
2. The best performing detergent is used for solubilization and the proteins are purified via their rho1D4 tag via two rho1D4 antibody columns: one DTT resistant, the other one not. Eluate fractions are analyzed by Western blot.
3. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatograph. Eluate fractions are analyzed by SDS-PAGE and Western blot.

Pureté: >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Stérilité: 0.22 μm filtered

niveau d'endotoxine: Endotoxins have not been removed. Please contact us if you require an endotoxin-free version of this product.

Classe de qualité: Crystallography grade

Biological Activity Comment: Protein has not been tested for activity yet.

Information d'application

Indications d'application: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Stockage

Format: Liquid

Buffer: 150 mM NaCL, 20 mM NaH2PO4 pH 7.4, 10 % glycerol. Note: Isoelectric point of protein taken into account regarding pH .

Conseil sur la manipulation: Avoid repeated freeze-thaw cycles.

Stock: -80 °C

Stockage commentaire: Store at -80°C.

Date de péremption: Unlimited (if stored properly)

Détail du antigène

Antigène: HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))

Autre désignation: Heat shock protein HSP 90-alpha (HSP90AA1 Produits)

Synonymes: EL52 Protein, HSP86 Protein, HSP89A Protein, HSP90A Protein, HSP90N Protein, HSPC1 Protein, HSPCA Protein, HSPCAL1 Protein, HSPCAL4 Protein, HSPN Protein, Hsp89 Protein, Hsp90 Protein, LAP2 Protein, Hsp86 Protein, Hspca Protein, htpG Protein, 86kDa Protein, 89kDa Protein, AL024080 Protein, AL024147 Protein, Hsp86-1 Protein, hsp4 Protein, HSP90 Protein, HSP90AA1 Protein, fb17b01 Protein, hsp90 Protein, hsp90a Protein, hsp90a.1 Protein, hsp90alpha Protein, wu:fb17b01 Protein, zgc:86652 Protein, Hsp90alpha Protein, heat shock protein 90 alpha family class A member 1 Protein, heat shock protein 90, alpha (cytosolic), class A member 1 Protein, Heat Shock Protein 90, cytosolic Protein, heat shock protein 90A Protein, molecular chaperone Protein, heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1 Protein, heat shock protein HSP 90-alpha Protein, heat shock protein 90kDa alpha (cytosolic), class A member 1 Protein, HSP90AA1 Protein, Hsp90aa1 Protein, HSP90A Protein, hsp90A Protein, hsp90aa1.1 Protein, LOC108698781 Protein

Sujet: 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. 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 mitochondrial outer membrane which promotes host antiviral response. {ECO:0000250|UniProtKB:P07900}.

UniProt: P46633

Pathways: M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals