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AB281339

Recombinant Proteinase K (Active)

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(1 Publication)

Recombinant Proteinase K (Active) is a Parengyodontium album Full Length protein, in the 106 to 384 aa range, expressed in Yeast, with >95%, < 0.25 EU/mg endotoxin level, suitable for SDS-PAGE, FuncS.

View Alternative Names

Proteinase K, Endopeptidase K, Tritirachium alkaline proteinase, PROK, Endopeptidase K, Tritirachium alkaline proteinase

6 Images
Functional Studies - Recombinant Proteinase K (Active) (AB281339)
  • FuncS

Supplier Data

Functional Studies - Recombinant Proteinase K (Active) (AB281339)

Agarose gel analysis of RNAase activity in ab281339.

Functional Studies - Recombinant Proteinase K (Active) (AB281339)
  • FuncS

Supplier Data

Functional Studies - Recombinant Proteinase K (Active) (AB281339)

Specific activity >30 Units/mg.

Functional Studies - Recombinant Proteinase K (Active) (AB281339)
  • FuncS

Supplier Data

Functional Studies - Recombinant Proteinase K (Active) (AB281339)

Functional analysis of ab281339.

Functional Studies - Recombinant Proteinase K (Active) (AB281339)
  • FuncS

Supplier Data

Functional Studies - Recombinant Proteinase K (Active) (AB281339)

Agarose gel analysis of residual nucleic acid in ab281339.

Functional Studies - Recombinant Proteinase K (Active) (AB281339)
  • FuncS

Supplier Data

Functional Studies - Recombinant Proteinase K (Active) (AB281339)

Agarose gel analysis of DNAase activity in ab281339.

SDS-PAGE - Recombinant Proteinase K (Active) (AB281339)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Proteinase K (Active) (AB281339)

SDS-PAGE analysis of ab281339. 15% gel. Reducing conditions.

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 0.25 EU/mg

Expression system

Yeast

Tags

His tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific activity >30 units/mg.

Accession

P06873

Animal free

Yes

Carrier free

No

Species

Parengyodontium album

Reconstitution

Reconstitute in water

Storage buffer

pH: 8 Constituents: 6% Trehalose, 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"AAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFEGRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNGSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQSSGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLDIFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACRYIADTANKGDLSNIPFGTVNLLAYNNYQA","proteinLength":"Full Length","predictedMolecularWeight":"28.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":384,"aminoAcidStart":106,"nature":"Recombinant","expressionSystem":"Yeast","accessionNumber":"P06873","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Proteinase K also known by alternate names like pronase dako proteinase K prokeinase K protein K and protease K is a serine protease widely used in molecular biology. This enzyme derived from the fungus Engyodontium album has a molecular mass of approximately 28.9 kDa. Proteinase K demonstrates high proteolytic activity effectively breaking down proteins by cleaving peptide bonds adjacent to the carboxyl group of aliphatic and aromatic amino acids. Researchers often utilize this enzyme in DNA and RNA purification protocols due to its ability to inactivate nucleases. It is typically expressed in microbial or cell-free systems optimized for high yield and activity.
Biological function summary

Proteinase K plays a critical role in protein degradation. It exhibits robust activity even in the presence of detergents and high temperatures characteristics that make it a powerful tool in the removal of proteins during nucleic acid isolation. This enzyme is not a part of any complex within the organism but acts independently in protein digestion processes. Its ability to function under extreme conditions expands its utility across various biological applications.

Pathways

Proteinase K engages in pathways related to protein catabolism and turnover. It does not contribute directly to metabolic pathways within living organisms; however it assists experimental pathways in vitro by efficiently degrading proteins. Proteinase K's proteolytic capabilities make it instrumental in preventing protein contamination aiding the study of valid biological interactions without extraneous protein interference. Related proteins like pepsin and trypsin also participate in protein degradation but they have different activity profiles and optimal conditions.

Proteinase K is frequently employed in research on genetic disorders and infectious diseases. While the enzyme itself is not associated with causing diseases its role in DNA and RNA extraction is vital for diagnosing conditions such as hereditary diseases and viral infections. Through these processes Proteinase K indirectly interacts with proteins relevant to diseases like cystic fibrosis and HIV. By facilitating the isolation of pure nucleic acids Proteinase K supports studies aiming to elucidate the genetic and viral proteins connected with these disorders.

Specifications

Form

Lyophilized

General info

Function

Hydrolyzes keratin at aromatic and hydrophobic residues.

Sequence similarities

Belongs to the peptidase S8 family.

Product protocols

Target data

Hydrolyzes keratin at aromatic and hydrophobic residues.
See full target information Proteinase K

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Regenerative therapy 20:41-50 PubMed35402663

2022

YY1-induced lncRNA XIST inhibits cartilage differentiation of BMSCs by binding with TAF15 to stabilizing FUT1 expression.

Applications

Unspecified application

Species

Unspecified reactive species

Jian-Ying He,Min Cheng,Jia-Lian Ye,Chuan-Hua Peng,Jian Chen,Bin Luo,Xian-Yu Zhang,Qiang Fu
View all publications

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