Recombinant Bovine cAMP-dependent protein kinase type I-alpha regulatory subunit (PRKAR1A)

Code CSB-YP018694BO
MSDS
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Source Yeast
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Code CSB-EP018694BO
MSDS
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Source E.coli
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Code CSB-EP018694BO-B
MSDS
Size Pls inquire
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-BP018694BO
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP018694BO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PRKAR1A
Uniprot No.
Alternative Names
PRKAR1A; cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit; N-terminally processed]
Species
Bos taurus (Bovine)
Expression Region
1-380
Target Protein Sequence
MASGTTASEE ERSLRECELY VQKHNIQALL KDSIVQLCTA RPERPMAFLR EYFEKLEKEE AKQIQNLQKA GSRADSREDE ISPPPPNPVV KGRRRRGAIS AEVYTEEDAA SYVRKVIPKD YKTMAALAKA IEKNVLFSHL DDNERSDIFD AMFPVSFIAG ETVIQQGDEG DNFYVIDQGE MDVYVNNEWA TSVGEGGSFG ELALIYGTPR AATVKAKTNV KLWGIDRDSY RRILMGSTLR KRKMYEEFLS KVSILESLDK WERLTVADAL EPVQFEDGQK IVVQGEPGDE FFIILEGSAA VLQRRSENEE FVEVGRLGPS DYFGEIALLM NRPRAATVVA RGPLKCVKLD RPRFERVLGP CSDILKRNIQ QYNSFVSLSV
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
Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
Gene References into Functions
  1. Data suggest that enzyme activation by cAMP involves highly stable conformation of Prkar1a as it binds to Prkaca; glycine residue, G235, appears to function as hinge in B/C helix conserved in Prkar1a; this "Flipback" conformation plays role in cAMP association to A domain of Prkar1a. (Prkar1a = cyclic AMP-dependent protein kinase RIalpha subunit; Prkaca = cyclic AMP-dependent protein kinase catalytic subunit) PMID: 28661131
  2. Data suggest PRKAR1A contains two structurally homologous cAMP-binding domains that exhibit marked differences in dynamic profiles in activation/inhibition of Prkaca; conservation of structure does not necessarily imply conservation of dynamics. PMID: 26618408
  3. Thermodynamic analysis of protein kinase A (PKA) Ialpha activation was performed using Quantum 3.3.0 docking software and a Gaussian 03W quantum mechanical computational package. PMID: 20367611
  4. Results describe the structures of the protein kinase A RIalpha subunit D/D domain alone and in complex with D-AKAP2. PMID: 20159461
  5. Data show that RSK1 regulates PKAc activity in a cAMP-independent manner, and PKARIalpha by associating with RSK1 regulates its activation and its biological functions. PMID: 20048145
  6. angle X-ray scattering studies indicate RIalpha, RIIalpha, and RIIbeta homodimers differ markedly in overall shape despite extensive sequence homology and similar molecular masses;cAMP binding does not cause large conformational changes(Prkar1a, Prkar2a) PMID: 15046986
  7. the PKA RIalpha subunit dynamic C helix mediates isoform-specific domain reorganization upon C subunit binding PMID: 16109722

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Subcellular Location
Cell membrane.
Protein Families
CAMP-dependent kinase regulatory chain family
Tissue Specificity
Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.
Database Links
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301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
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7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
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