Hsc70 Protein (full length) (rho-1D4 tag)

N° du produit ABIN7126020

Détail du produit

Antigène: Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))

Type de proteíne: Recombinant

Attributs du protein: full length

Origine: CHO cells

Source: Cellules d'insectes

Purification/Conjugué: Cette Hsc70 protéine est marqué à la rho-1D4 tag.

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

Séquence: MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE AKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRNDK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
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 cognate 71 kDa protein (Heat shock 70 kDa protein 8) 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: Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))

Autre désignation: Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8) (HSPA8 Produits)

Synonymes: hsc54 Protein, hsc70 Protein, hsc71 Protein, hsp71 Protein, hsp73 Protein, hspa10 Protein, lap1 Protein, nip71 Protein, HSC54 Protein, HSC70 Protein, HSC71 Protein, HSP71 Protein, HSP73 Protein, HSPA10 Protein, LAP1 Protein, NIP71 Protein, Hsc70 Protein, 2410008N15Rik Protein, Hsc71 Protein, Hsc73 Protein, Hsp73 Protein, Hspa10 Protein, wu:fb01g06 Protein, wu:fi48b06 Protein, heat shock protein family A (Hsp70) member 8 L homeolog Protein, heat shock protein family A (Hsp70) member 8 Protein, heat shock 70kDa protein 8 Protein, heat shock protein 8 Protein, hspa8.L Protein, HSPA8 Protein, Hspa8 Protein, hspa8 Protein

Sujet: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21. {ECO:0000250|UniProtKB:P11142}.

UniProt: P19378