Recombinant Escherichia coli ATP-dependent Clp protease ATP-binding subunit ClpA (clpA)

Code CSB-YP364652ENV
MSDS
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Source Yeast
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Code CSB-EP364652ENV
MSDS
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Source E.coli
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Code CSB-EP364652ENV-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP364652ENV
MSDS
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Source Baculovirus
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Code CSB-MP364652ENV
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
clpA
Uniprot No.
Alternative Names
clpA; lopD; b0882; JW0866ATP-dependent Clp protease ATP-binding subunit ClpA
Species
Escherichia coli (strain K12)
Expression Region
1-758
Target Protein Sequence
MLNQELELSL NMAFARAREH RHEFMTVEHL LLALLSNPSA REALEACSVD LVALRQELEA FIEQTTPVLP ASEEERDTQP TLSFQRVLQR AVFHVQSSGR NEVTGANVLV AIFSEQESQA AYLLRKHEVS RLDVVNFISH GTRKDEPTQS SDPGSQPNSE EQAGGEERME NFTTNLNQLA RVGGIDPLIG REKELERAIQ VLCRRRKNNP LLVGESGVGK TAIAEGLAWR IVQGDVPEVM ADCTIYSLDI GSLLAGTKYR GDFEKRFKAL LKQLEQDTNS ILFIDEIHTI IGAGAASGGQ VDAANLIKPL LSSGKIRVIG STTYQEFSNI FEKDRALARR FQKIDITEPS IEETVQIING LKPKYEAHHD VRYTAKAVRA AVELAVKYIN DRHLPDKAID VIDEAGARAR LMPVSKRKKT VNVADIESVV ARIARIPEKS VSQSDRDTLK NLGDRLKMLV FGQDKAIEAL TEAIKMARAG LGHEHKPVGS FLFAGPTGVG KTEVTVQLSK ALGIELLRFD MSEYMERHTV SRLIGAPPGY VGFDQGGLLT DAVIKHPHAV LLLDEIEKAH PDVFNILLQV MDNGTLTDNN GRKADFRNVV LVMTTNAGVR ETERKSIGLI HQDNSTDAME EIKKIFTPEF RNRLDNIIWF DHLSTDVIHQ VVDKFIVELQ VQLDQKGVSL EVSQEARNWL AEKGYDRAMG ARPMARVIQD NLKKPLANEL LFGSLVDGGQ VTVALDKEKN ELTYGFQSAQ KHKAEAAH
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins.
Gene References into Functions
  1. These results suggest that the presence of gamma phosphate may serve to switch ClpA into a conformational state with high peptide binding activity, whereas affinity is severely attenuated when ADP is bound. PMID: 21376057
  2. Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase PMID: 20380838
  3. one ClpS monomer is sufficient to direct the activity of the ClpA hexamer PMID: 20068042
  4. identified a number of structural features in the N-domain, including a Zn(++) binding motif, several interfaces for binding to ClpS, and a prominent hydrophobic surface area that binds peptides in different configurations PMID: 15037248
  5. determined structure at 12A resolution by cryo-electron microscopy; N-domain region is accentuated in a variance map of ClpAP and in a difference imaging experiment with ClpAP complexed with ClpS PMID: 15037249
  6. ClpA has a single high affinity peptide binding site per hexamer PMID: 15657062
  7. ClpA utilizes two structural elements, one in the N-temrinal domain and the other in the pore of the hexamer, both of which are required for efficient unfolding of some protein substrates. PMID: 18279386
  8. Results suggest that the flexible attachment of the N-domains to ClpA allows their recruitment to the pore on demand for certain substrates, while allowing them to move out of the way for substrates binding directly to the pore. PMID: 18358489
  9. Data support substrate translocation by ClpA via ATP-induced movements of the D2 loop. PMID: 18682217
  10. Application of analytical ultracentrifugation and light scattering techniques reveals that ClpA self-associates in a monomer-tetramer equilibrium in the presence and absence of magnesium at 25 degrees centigrade. PMID: 19650643
  11. ATP hydrolysis in both domains of ClpA was required for efficiently processing substrates of high local stability. PMID: 19726681

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Protein Families
ClpA/ClpB family
Database Links
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