Recombinant Papain protein (His tag) is a Papaya Full Length protein, in the 134 to 345 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
>90% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE
No
I P E Y V D W R Q K G A V T P V K N Q G S C G S C W A F S A V V T I E G I I K I R T G N L N E Y S E Q E L L D C D R R S Y G C N G G Y P W S A L Q L V A Q Y G I H Y R N T Y P Y E G V Q R Y C R S R E K G P Y A A K T D G V R Q V Q P Y N E G A L L Y S I A N Q P V S V V L E A A G K D F Q L Y R G G I F V G P C G N K V D H A V A A V G Y G P N Y I L I K N S W G T G W G E N G Y I R I K R G T G N S Y G V C G L Y T S S F Y P V K N
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Papain, Papaya proteinase I, PPI
Recombinant Papain protein (His tag) is a Papaya Full Length protein, in the 134 to 345 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
>90% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE
No
No
Papaya
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
I P E Y V D W R Q K G A V T P V K N Q G S C G S C W A F S A V V T I E G I I K I R T G N L N E Y S E Q E L L D C D R R S Y G C N G G Y P W S A L Q L V A Q Y G I H Y R N T Y P Y E G V Q R Y C R S R E K G P Y A A K T D G V R Q V Q P Y N E G A L L Y S I A N Q P V S V V L E A A G K D F Q L Y R G G I F V G P C G N K V D H A V A A V G Y G P N Y I L I K N S W G T G W G E N G Y I R I K R G T G N S Y G V C G L Y T S S F Y P V K N
Full Length
27.4 kDa
134 to 345
Recombinant
His tag N-Terminus
Liquid
Belongs to the peptidase C1 family.
Blue Ice
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This supplementary information is collated from multiple sources and compiled automatically.
Papain also known as papaya proteinase I is a cysteine protease enzyme derived from the papaya plant. It exhibits a molecular weight of approximately 23.4 kDa. Papain is synthesized primarily in the fruit of the papaya and its enzyme activity depends on the presence of thiol groups. This protease is popular in various industrial applications due to its ability to cleave a wide range of peptide bonds facilitating protein breakdown. Disulfide bonds within papain help stabilize its structure allowing efficient substrate digestion under different conditions.
Papain functions as a proteolytic enzyme aiding in the hydrolysis of proteins into peptides and amino acids. It is not part of a complex but rather operates independently to perform its function. Papain's broad proteolytic activity makes it effective in breaking down tough protein structures in organisms enhancing nutrient availability. The enzyme's activity finds use in meat tenderizing and has a role in certain cellular processes such as protein catabolism.
The enzyme plays a role in dietary protein digestion and degradation pathways. It interacts with other proteases like ficin and bromelain working synergistically to facilitate the denaturation and digestion of proteins. These proteases including papain contribute significantly to metabolic processes that involve protein turnover and nitrogen metabolism in various organisms. Papain substrates often include proteins that require further degradation for metabolic purposes.
Papain's relevance is notable concerning inflammation and wound healing. Studies suggest that papain's proteolytic properties help in removing dead tissue and promoting new tissue formation benefiting chronic wounds and ulcers. Papain also shows potential in managing inflammatory conditions where its degradation of specific protein substrates can minimize inflammatory responses. Proteins like elastase may connect to papain's activity as it mediates tissue regeneration and inflammation resolution.
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