Please contact proteinservices [at] tuni.fi (proteinservices[at]tuni[dot]fi) if you wish to purchase any of the available protein products.<figure role="group"><div class="embedded-file"><svg height="25" width="25" aria-hidden="true" xmlns="http://www.w3.org/2000/svg" viewBox="0 0 24 24"><polygon points="22 18 22 20 2 20 2 18 0 18 0 20 0 22 2 22 22 22 24 22 24 20 24 18 22 18"></polygon><polygon points="12 18 18.55 11.46 17.09 10 13 14.09 13 2 11 2 11 14.09 6.91 10 5.46 11.46 12 18"></polygon></svg>Download<a href="https://content-webapi.tuni.fi/proxy/public/2024-11/proteinservices_orderform_2024.pdf">Order form (PDF, 470.69 KB) </a></div></figure> Protein Service Order Form includes: <ul><li>Research Agreement – Business Operations (University of Tampere) </li><li>General terms and conditions – Business Operations (University of Tampere)</li></ul>

<a href="https://www.tuni.fi/en/about-us/faculty-medicine-and-health-technology">Faculty of Medicine and Health Technology</a> has established protein expression and purification service that manufactures recombinant proteins for academic and industrial partners. We have capability to express proteins with&nbsp;E. coli, insect cells (Sf9&nbsp;and&nbsp;Hi5) and cell free systems depending from the need.

 
We have good variety of purification methods and instruments available to purify and characterize the proteins.

&nbsp;

<h2>General information</h2>

Proteins are recombinant proteins expressed in&nbsp;E. coli&nbsp;except Fibronectin witch is purified from human plasma. All proteins are purified with one-step affinity chromatography, dialyzed and analyzed with SDS-PAGE. Concentration is measured by UV/Vis spectroscopy. Thereafter proteins are lyophilized and kept -80 °C until shipment in ambient temperature.

ProtMarket

ABBREVIATIONS: 
Avidin (Avd)

STRUCTURE: 
Avidins are homotetrameric proteins with four identical subunits, which each have one biotin binding site. 
 
Molecular weight of&nbsp;MONOMER&nbsp;(expected size in reducing SDS-PAGE): 
The molecular weight of recombinant AVIDIN is 14671.5 g/mol 
 
The value above is based on amino acid sequence information and MS measurements. 
Avidins are single polypeptide chains consisting of about 130 amino acid residues and no carbohydrates. 
 
Avd contain one intra-chain disulfide bridges and no free sulfhydryl groups. Avd expressed in&nbsp;E. coli&nbsp;is not glycosylated.

&nbsp;

PHYSICAL PROPERTIES of&nbsp;MONOMER: 
The&nbsp;pI&nbsp;and&nbsp;extinction coefficient&nbsp;of recombinant AVIDIN are 9.69 and 23615 M-1 cm-1 (at 280 nm measured in water), respectively.

SOLUBILITY / SOLUTION STABILITY: 
Avidins are readily soluble in water and can be precipitated by high concentrations of neutral salts such as ammonium sulfate. The solution stability of avidins are very good (especially if the solutions are stored as frozen aliquots). Avidins are stable at high temperatures. In addition, biotin increases stability significantly. At somewhat lower temperatures aggregation may occur, but at relatively slow rates.

METHOD OF PREPARATION: 
The vector containing the avidin gene was transformed into&nbsp;E. coli&nbsp;BL21-AI cells. Single colonies were grown overnight in LB medium containing with appropriate antibiotics. Then, small cultures were transferred to fermenting medium and incubated overnight with constant shaking. Each of these seeds were used to start a 4-L fermentation at 28 °C in a fermentor. The culture was induced with IPTG and L(+)-arabinose. After induction the culture was maintained overnight after which feed solution was applied at a constant speed for the final 22 hours. 
 
Protein was purified with 2-iminobiotin-SepharoseTM 4 Fast Flow as previously described (1). Purity and quality of the isolated protein was analyzed with a UV/VIS spectrophotometer and SDS-PAGE (see appendix).

PRODUCT DESCRIPTION / USAGE: 
The main biological function of avidin is not known but most likely it has antimicrobial properties. 
 
-Avidin binds biotin with high affinity Kd ~ 10-15M 
-Avidin binds HABA (4-hydroxyazobenzene-2-carboxylic acid) with moderate affinity, resulting in a color change.

SEQUENCE

QTVARKCSLTGKW TNDLGSNMTI GAVNSRGEFT GTYITAVTAT SNEIKESPLH GTQNTINKRTQPTFGFTVNW KFSESTTVFT GQCFIDRNGK EVLKTMWLLR SSVNDIGDDW KATRVGINIFTRLRTQKE

REFERENCES

<ol>
	<li>Biotin induces tetramerization of a recombinant monomeric avidin. A model for protein-protein interactions. Laitinen OH, Marttila AT, Airenne KJ, Kulik T, Livnah O, Bayer EA, Wilchek M, Kulomaa MS. J Biol Chem. 2001 Mar 16;276(11):8219-24.</li>
	<li>Efficient production of active chicken avidin using a bacterial signal peptide in Escherichia coli. Hytönen VP, Laitinen OH, Airenne TT, Kidron H, Meltola NJ, Porkka EJ, Hörhä J, Paldanius T, Määttä JA, Nordlund HR, Johnson MS, Salminen TA, Airenne KJ, Ylä-Herttuala S, Kulomaa MS. Biochem J. 2004 384(Pt 2):385-90.</li>
</ol>

RECOMBINANT AVIDIN from E.COLI

RECOMBINANT AVIDIN

STRUCTURE: 
Avidins are homotetrameric proteins with four identical subunits, which each have one biotin binding site. 
 
Molecular weight of&nbsp;MONOMER&nbsp;(expected size in reducing SDS-PAGE): 
The molecular weight of Switchavidin is 14617.3 g/mol 
 
The molecular weight estimate is based on amino acid sequence information and MS measurements. 
 
Avidins are single polypeptide chains consisting of about 130 amino acid residues and no carbohydrates. 
 
Switchavidin contains one intra-chain disulfide bridges and no free sulfhydryl groups. It is fee of carbohydrates.

PHYSICAL PROPERTIES of&nbsp;MONOMERS:

The&nbsp;pI&nbsp;and&nbsp;extinction coefficient&nbsp;of Switchavidin are 7.02 and 23615 M-1 cm-1 (at 280 nm measured in water), respectively.

SOLUBILITY / SOLUTION STABILITY: 
Avidins are readily soluble in water and can be precipitated by high concentrations of neutral salts such as ammonium sulfate. The solution stability of avidins are very good (especially if the solutions are stored as frozen aliquots). Avidins are stable at high temperatures and after when heated to 50 °C irreversible denaturation starts. In addition, biotin increases stability significantly. At somewhat lower temperatures aggregation may occur, but at relatively slow rates.

METHOD OF PREPARATION: 
The vector containing the mutated avidin gene was transformed into&nbsp;E. coli&nbsp;BL21-AI cells. Single colonies were grown overnight in LB medium containing with appropriate antibiotics. Then, small cultures were transferred to fermenting medium and incubated overnight with constant shaking. Each of these seeds were used to start a 4-L fermentation at 28 °C in a fermentor. The culture was induced with IPTG and L(+)-arabinose. After induction the culture was maintained overnight after which feed solution was applied at a constant speed for the final 22 hours. 
 
Protein was purified with 2-iminobiotin-SepharoseTM 4 Fast Flow as previously described (1). Purity and quality of the isolated protein was analyzed with a UV/VIS spectrophotometer and SDS-PAGE (see appendix).

PRODUCT DESCRIPTION / USAGE: 
The main biological function of avidin is not known but most likely it has antimicrobial properties. 
 
-Avidin binds biotin with high affinity Kd ~ 10-15M 
-Avidin binds HABA (4-hydroxyazobenzene-2-carboxylic acid) with moderate affinity, resulting in a color change. 
-Switchavidin may be released permanently from biotinylated materials by applying a mixture of 2.5% citric acid and 0.25% SDS (2).

REFERENCES

<ol>
	<li>Biotin induces tetramerization of a recombinant monomeric avidin. A model for protein-protein interactions. Laitinen OH, Marttila AT, Airenne KJ, Kulik T, Livnah O, Bayer EA, Wilchek M, Kulomaa MS. J Biol Chem. 2001 Mar 16;276(11):8219-24.</li>
	<li>Reversible biofunctionalization of surfaces with a switchable mutant of avidin. Pollheimer P, Taskinen B, Scherfler A, Gusenkov S, Creus M, Wiesauer P, Zauner D, Schöfberger W, Schwarzinger C, Ebner A, Tampé R, Stutz H, Hytönen VP, Gruber HJ. Bioconjug Chem. 2013 Oct 16;24(10):1656-68</li>
	<li>Switchavidin: reversible biotin-avidin-biotin bridges with high affinity and specificity. Taskinen B, Zauner D, Lehtonen SI, Koskinen M, Thomson C, Kähkönen N, Kukkurainen S, Määttä JA, Ihalainen TO, Kulomaa MS, Gruber HJ, Hytönen VP. Bioconjug Chem. 2014 25(12):2233-43.</li>
</ol>

Switchavidin from E.coli (2,3)

SwitchAVIDIN

ABBREVIATIONS: 
Chimeric avidin (CA); Avidin (Avd)

STRUCTURE: 
Avidins are homotetrameric proteins with four identical subunits, which each have one biotin binding site.

Molecular weight of&nbsp;MONOMER&nbsp;(expected size in reducing SDS-PAGE): 
The molecular weight of CHARGE-NEUTRALIZED CHIMERIC AVIDIN is 14383.2 g/mol

This value is based on amino acid sequence information and MS measurements. 
Avidins are single polypeptide chains consisting of about 130 amino acid residues and no carbohydrates.

CA contains one intra-chain disulfide bridge and no free sulfhydryl groups. CA expressed in&nbsp;E. coli&nbsp;is not glycosylated.

&nbsp;

PHYSICAL PROPERTIES of&nbsp;MONOMER: 
The&nbsp;pI&nbsp;and&nbsp;extinction coefficient&nbsp;of CHIMERIC AVIDIN are 9.69 and 25105 M-1 cm-1 (at 280 nm measured in water), respectively.

SOLUBILITY / SOLUTION STABILITY: 
CA is readily soluble in water and can be precipitated by high concentrations of neutral salts such as ammonium sulfate. The solution stability of avidins are very good (especially if the solutions are stored as frozen aliquots). Avidins are stable at high temperatures. In addition, biotin increases stability significantly. At somewhat lower temperatures aggregation may occur, but at relatively slow rates.

METHOD OF PREPARATION: 
The vector containing the mutated avidin gene was transformed into&nbsp;E. coli&nbsp;BL21-AI cells. Single colonies were grown overnight in LB medium containing with appropriate antibiotics. Then, small cultures were transferred to fermenting medium and incubated overnight with constant shaking. Each of these seeds were used to start a 4-L fermentation at 28 °C in a fermentor. The culture was induced with IPTG and L(+)-arabinose. After induction the culture was maintained overnight after which feed solution was applied at a constant speed for the final 22 hours.

Protein was purified with 2-iminobiotin-SepharoseTM 4 Fast Flow as previously described (1). Purity and quality of the isolated protein was analyzed with a UV/VIS spectrophotometer and SDS-PAGE (see Figure 1.).

PRODUCT DESCRIPTION / USAGE: 
The main biological function of avidin is not known but most likely it has antimicrobial properties. 
-Avidin binds biotin with high affinity Kd ~ 10-15M 
-Avidin binds HABA (4-hydroxyazobenzene-2-carboxylic acid) with moderate affinity, resulting in a color change.

LICENSING: 
The use of CA for commercial exploitation requires license from Orion Diagnostica. 
Orion Diagnostica is a mid-sized, reliable European IVD company with over 40 years’ experience. We develop, manufacture and market diagnostic tests and test solutions. Our focus is in accurate and affordable clinical diagnostic and hygiene monitoring tests, which are easy to use and provide fast results. Company has over 40 years’ experience in diagnostic test systems for doctor’s offices, healthcare centres and laboratories. The test systems are designed to assist healthcare professionals in diagnosing, making appropriate treatment decisions and following up treatment response. Orion Diagnostica is part of Orion Group, the leading healthcare company in Finland. 
Partnerships and networking are important for Orion Diagnostica throughout the entire value chain of operations. We collaborate with other companies in product development, manufacturing and marketing and sales of products internationally. 
For Orion Diagnostica, successful partnership management is a business priority. We have the processes, structures, competences, and the right mind set in place to ensure efficiency and flexibility. Orion Diagnostica would be happy to receive and evaluate collaboration proposals around different assets that would fit Orion Diagnostica's focuses, resources and capabilities. 
Please see details on our company website:&nbsp;<a href="http://www.oriondiagnostica.com/">www.oriondiagnostica.com</a>&nbsp;and contact us via contact form:&nbsp;<a href="http://www.oriondiagnostica.com/Contact-us/">http://www.oriondiagnostica.com/Contact-us/</a>

&nbsp;

<figure role="group"><img src="https://content-webapi.tuni.fi/image-style/max_1300x1300/proxy/public/2021-05/orion.png?itok=V60d_M-9" alt="Orion diagnostica logo" ><figcaption>www.oriondiagnostica.com</figcaption></figure>

SEQUENCE

QTVARKCSLT GKWTNDLGSN MTIGAVNSRG EFTGTYITAV ADNPGNITLS PLLGIQHKRA SQPTFGFTVN WKFSESTTVF TGQCFIDRNG KEVLKTMWLL RSSVNDIGDD WKATRVGYNI FTRLRTQKE

REFERENCES

<ol>
	<li>Biotin induces tetramerization of a recombinant monomeric avidin. A model for protein-protein interactions. Laitinen OH, Marttila AT, Airenne KJ, Kulik T, Livnah O, Bayer EA, Wilchek M, Kulomaa MS. J Biol Chem. 2001 Mar 16;276(11):8219-24.</li>
	<li>Chimeric Avidin--NMR structure and dynamics of a 56 kDa homotetrameric thermostable protein. Tossavainen H, Kukkurainen S, Määttä JA, Kähkönen N, Pihlajamaa T, Hytönen VP, Kulomaa MS, Permi P. PLoS One. 2014 Jun 24;9(6):e100564.</li>
	<li>Structural and functional characteristics of chimeric avidins physically adsorbed onto functionalized polythiophene thin films. Albers WM, Pelto JM, Suspène C, Määttä JA, Yassar A, Hytönen VP, Vikholm-Lundin IM, Tappura K. ACS Appl Mater Interfaces. 2012 Aug;4(8):4067-77.</li>
	<li>Chimeric avidin shows stability against harsh chemical conditions--biochemical analysis and 3D structure. Määttä JA, Eisenberg-Domovich Y, Nordlund HR, Hayouka R, Kulomaa MS, Livnah O, Hytönen VP. Biotechnol Bioeng. 2011 Mar;108(3):481-90.</li>
	<li>Neutralized chimeric avidin binding at a reference biosensor surface. Ray S, Steven RT, Green FM, Höök F, Taskinen B, Hytönen VP, Shard AG. Langmuir. 2015 31(6):1921-30.</li>
</ol>

<figure role="group"><img src="https://content-webapi.tuni.fi/image-style/max_1300x1300/proxy/public/2021-05/chimeric_avidin.jpg?itok=4uBJC7DV" alt="Reducing SDS-PAGE figure" ><figcaption>Figure 1. Reducing SDS-PAGE figure from the purification of CHIMERIC AVIDIN. Expected protein (monomer) is between 10 to 17 kDa molecular weight marker bands.</figcaption></figure>

CHIMERIC AVIDIN fromE.COLI

CHIMERIC AVIDIN

ABBREVIATIONS: 
Charge-Neutralized Chimeric Avidin (CNCA)

STRUCTURE: 
Avidins are homotetrameric proteins with four identical subunits, which each have one biotin binding site. 
 
Molecular weight of&nbsp;MONOMER&nbsp;(expected size in reducing SDS-PAGE): 
The molecular weight of CHARGE-NEUTRALIZED CHIMERIC AVIDIN is 14324.0 g/mol 
 
This value is based on amino acid sequence information and MS measurements. 
 
Avidins are single polypeptide chains consisting of about 130 amino acid residues and no carbohydrates. 
CNCA contains one intra-chain disulfide bridge and no free sulfhydryl groups. CNCA expressed in&nbsp;E. coli&nbsp;is not glycosylated.

PHYSICAL PROPERTIES of&nbsp;MONOMER: 
The&nbsp;pI&nbsp;and&nbsp;extinction coefficient&nbsp;of CHARGE-NEUTRALIZED CHIMERIC AVIDIN are 6.92 and 25105 M-1 cm-1 (at 280 nm measured in water), respectively.

SOLUBILITY / SOLUTION STABILITY: 
CNCA is readily soluble in water and can be precipitated by high concentrations of neutral salts such as ammonium sulfate. The solution stability of avidins are very good (especially if the solutions are stored as frozen aliquots). Avidins are stable at high temperatures. In addition, biotin increases stability significantly. At somewhat lower temperatures aggregation may occur, but at relatively slow rates.

METHOD OF PREPARATION: 
The vector containing the mutated avidin gene was transformed into&nbsp;E. coli&nbsp;BL21-AI cells. Single colonies were grown overnight in LB medium containing with appropriate antibiotics. Then, small cultures were transferred to fermenting medium and incubated overnight with constant shaking. Each of these seeds were used to start a 4-L fermentation at 28 °C in a fermentor. The culture was induced with IPTG and L(+)-arabinose. After induction the culture was maintained overnight after which feed solution was applied at a constant speed for the final 22 hours. 
 
Protein was purified with 2-iminobiotin-SepharoseTM 4 Fast Flow as previously described (1). Purity and quality of the isolated protein was analyzed with a UV/VIS spectrophotometer and SDS-PAGE (see Figure 1.).

PRODUCT DESCRIPTION / USAGE: 
The main biological function of avidin is not known but most likely it has antimicrobial properties. 
 
-Avidin binds biotin with high affinity Kd ~ 10-15M 
-Avidin binds HABA (4-hydroxyazobenzene-2-carboxylic acid) with moderate affinity, resulting in a color change.

LICENSING:

The use of CNCA for commercial exploitation requires license from Orion Diagnostica. 
 
Orion Diagnostica is a mid-sized, reliable European IVD company with over 40 years’ experience. We develop, manufacture and market diagnostic tests and test solutions. Our focus is in accurate and affordable clinical diagnostic and hygiene monitoring tests, which are easy to use and provide fast results. Company has over 40 years’ experience in diagnostic test systems for doctor’s offices, healthcare centres and laboratories. The test systems are designed to assist healthcare professionals in diagnosing, making appropriate treatment decisions and following up treatment response. Orion Diagnostica is part of Orion Group, the leading healthcare company in Finland. 
 
Partnerships and networking are important for Orion Diagnostica throughout the entire value chain of operations. We collaborate with other companies in product development, manufacturing and marketing and sales of products internationally. 
 
For Orion Diagnostica, successful partnership management is a business priority. We have the processes, structures, competences, and the right mind set in place to ensure efficiency and flexibility. Orion Diagnostica would be happy to receive and evaluate collaboration proposals around different assets that would fit Orion Diagnostica's focuses, resources and capabilities.

Please see details on our company website:&nbsp;<a href="http://www.oriondiagnostica.com/">www.oriondiagnostica.com</a>&nbsp;and contact us via contact form:&nbsp;<a href="http://www.oriondiagnostica.com/Contact-us/">http://www.oriondiagnostica.com/Contact-us/</a>

<figure role="group"><img src="https://content-webapi.tuni.fi/image-style/max_1300x1300/proxy/public/2021-05/orion.png?itok=V60d_M-9" alt="Orion diagnostica logo" ><figcaption>www.oriondiagnostica.com</figcaption></figure>

SEQUENCE

QTVARKCSLT GEWTNDLGSN&nbsp; MTIGAVNSNG EFTGTYITAV ADNPGNITLS PLLGIQHKRA SQPTFGFTVN WKFSESTTVF TGQCFIDRNG KEVLKTMWLL RSSVNDIGDD WKATRVGYNI FTRLHTQEE

&nbsp;

REFERENCES

<ol>
	<li>Biotin induces tetramerization of a recombinant monomeric avidin. A model for protein-protein interactions. Laitinen OH, Marttila AT, Airenne KJ, Kulik T, Livnah O, Bayer EA, Wilchek M, Kulomaa MS. J Biol Chem. 2001 Mar 16;276(11):8219-24.</li>
	<li>Chimeric Avidin--NMR structure and dynamics of a 56 kDa homotetrameric thermostable protein. Tossavainen H, Kukkurainen S, Määttä JA, Kähkönen N, Pihlajamaa T, Hytönen VP, Kulomaa MS, Permi P. PLoS One. 2014 Jun 24;9(6):e100564.</li>
	<li>Structural and functional characteristics of chimeric avidins physically adsorbed onto functionalized polythiophene thin films. Albers WM, Pelto JM, Suspène C, Määttä JA, Yassar A, Hytönen VP, Vikholm-Lundin IM, Tappura K. ACS Appl Mater Interfaces. 2012 Aug;4(8):4067-77.</li>
	<li>Chimeric avidin shows stability against harsh chemical conditions--biochemical analysis and 3D structure. Määttä JA, Eisenberg-Domovich Y, Nordlund HR, Hayouka R, Kulomaa MS, Livnah O, Hytönen VP. Biotechnol Bioeng. 2011 Mar;108(3):481-90.</li>
	<li>Neutralized chimeric avidin binding at a reference biosensor surface. Ray S, Steven RT, Green FM, Höök F, Taskinen B, Hytönen VP, Shard AG. Langmuir. 2015 31(6):1921-30.</li>
</ol>

<figure role="group"><img src="https://content-webapi.tuni.fi/image-style/max_1300x1300/proxy/public/2021-05/fig1.jpg?itok=STNYUS8F" alt="SDS-PAGE figure" ><figcaption>Figure 1. SDS-PAGE figure from the purification of CHARGE-NEUTRALIZED CHIMERIC AVIDIN. Expected protein (monomer) is between 10 to 17 kDa molecular weight marker bands.</figcaption></figure>

&nbsp;

 CHARGE-NEUTRALIZED CHIMERIC AVIDIN from E.COLI

CHARGE-NEUTRALIZED CHIMERIC AVIDIN

ABBREVIATIONS: 
Charge-Neutralized Chimeric Avidin (CNCA), Charge-Neutralized Chimeric Avidin with C-terminal Cys (CNCA-C).

STRUCTURE: 
Avidins are homotetrameric proteins with four identical subunits, which each have one biotin binding site. 
 
Molecular weight of protein&nbsp;MONOMER&nbsp;(expected size in reducing SDS-PAGE): 
The molecular weight of CHARGE-NEUTRALIZED CHIMERIC AVIDIN is 14427.1 g/mol 
The molecular weight estimate is based on amino acid sequence information and MS measurements. 
 
Avidins are single polypeptide chains consisting of about 130 amino acid residues and no carbohydrates. 
 
CNCA with C-terminal cysteine contains one intra-chain disulfide bridge and one free sulfhydryl group per monomer (four free sulfhydryl groups per tetramer). CNCA-C expressed in&nbsp;E. coli&nbsp;is not glycosylated.

PHYSICAL PROPERTIES of&nbsp;MONOMERS: 
The&nbsp;pI&nbsp;and&nbsp;extinction coefficient&nbsp;of CHARGE-NEUTRALIZED CHIMERIC AVIDIN with linkable cysteine in C-terminal are 6.91 and 25105 M-1 cm-1 (at 280 nm measured in water), respectively.

SOLUBILITY / SOLUTION STABILITY: 
Avidins are readily soluble in water and can be precipitated by high concentrations of neutral salts such as ammonium sulfate. The solution stability of avidins are very good (especially if the solutions are stored as frozen aliquots). Avidins are stable at high temperatures. In addition, biotin increases stability significantly. At somewhat lower temperatures aggregation may occur, but at relatively slow rates.

METHOD OF PREPARATION: 
The vector containing the mutated avidin gene was transformed into&nbsp;E. coli&nbsp;BL21-AI cells. Single colonies were grown overnight in LB medium containing with appropriate antibiotics. Then, small cultures were transferred to fermenting medium and incubated overnight with constant shaking. Each of these seeds were used to start a 4-L fermentation at 28 °C in a fermentor. The culture was induced with IPTG and L(+)-arabinose. After induction the culture was maintained overnight after which feed solution was applied at a constant speed for the final 22 hours. 
 
Protein was purified with 2-iminobiotin-SepharoseTM 4 Fast Flow as previously described (1). Purity and quality of the isolated protein was analyzed with a UV/VIS spectrophotometer and SDS-PAGE (see appendix).

PRODUCT DESCRIPTION / USAGE: 
The main biological function of avidin is not known but most likely it has antimicrobial properties. 
 
-Avidin binds biotin with high affinity Kd ~ 10-15M 
-Avidin binds HABA (4-hydroxyazobenzene-2-carboxylic acid) with moderate affinity, resulting in a color change.

LICENSING:

The use of CNCA-C for commercial exploitation requires license from Orion Diagnostica. 
 
Orion Diagnostica is a mid-sized, reliable European IVD company with over 40 years’ experience. We develop, manufacture and market diagnostic tests and test solutions. Our focus is in accurate and affordable clinical diagnostic and hygiene monitoring tests, which are easy to use and provide fast results. Company has over 40 years’ experience in diagnostic test systems for doctor’s offices, healthcare centres and laboratories. The test systems are designed to assist healthcare professionals in diagnosing, making appropriate treatment decisions and following up treatment response. Orion Diagnostica is part of Orion Group, the leading healthcare company in Finland. 
 
Partnerships and networking are important for Orion Diagnostica throughout the entire value chain of operations. We collaborate with other companies in product development, manufacturing and marketing and sales of products internationally. 
 
For Orion Diagnostica, successful partnership management is a business priority. We have the processes, structures, competences, and the right mind set in place to ensure efficiency and flexibility. Orion Diagnostica would be happy to receive and evaluate collaboration proposals around different assets that would fit Orion Diagnostica's focuses, resources and capabilities.

Please see details on our company website:&nbsp;<a href="http://www.oriondiagnostica.com/">www.oriondiagnostica.com</a>&nbsp;and contact us via contact form:&nbsp;<a href="http://www.oriondiagnostica.com/Contact-us/">http://www.oriondiagnostica.com/Contact-us/</a>

<figure role="group"><img src="https://content-webapi.tuni.fi/image-style/max_1300x1300/proxy/public/2021-05/orion.png?itok=V60d_M-9" alt="Orion diagnostica logo" ><figcaption>www.oriondiagnostica.com</figcaption></figure>

SEQUENCE

QTVARKCSLT GEWTNDLGSN MTIGAVNSNG EFTGTYITAV ADNPGNITLS PLLGIQHKRA SQPTFGFTVN WKFSESTTVF TGQCFIDRNG KEVLKTMWLL RSSVNDIGDD WKATRVGYNI FTRLHTQEEC

REFERENCES

<ol>
	<li>Biotin induces tetramerization of a recombinant monomeric avidin. A model for protein-protein interactions. Laitinen OH, Marttila AT, Airenne KJ, Kulik T, Livnah O, Bayer EA, Wilchek M, Kulomaa MS. J Biol Chem. 2001 Mar 16;276(11):8219-24.</li>
	<li>Chimeric Avidin--NMR structure and dynamics of a 56 kDa homotetrameric thermostable protein. Tossavainen H, Kukkurainen S, Määttä JA, Kähkönen N, Pihlajamaa T, Hytönen VP, Kulomaa MS, Permi P. PLoS One. 2014 Jun 24;9(6):e100564.</li>
	<li>Structural and functional characteristics of chimeric avidins physically adsorbed onto functionalized polythiophene thin films. Albers WM, Pelto JM, Suspène C, Määttä JA, Yassar A, Hytönen VP, Vikholm-Lundin IM, Tappura K. ACS Appl Mater Interfaces. 2012 Aug;4(8):4067-77.</li>
	<li>Chimeric avidin shows stability against harsh chemical conditions--biochemical analysis and 3D structure. Määttä JA, Eisenberg-Domovich Y, Nordlund HR, Hayouka R, Kulomaa MS, Livnah O, Hytönen VP. Biotechnol Bioeng. 2011 Mar;108(3):481-90.</li>
	<li>Neutralized chimeric avidin binding at a reference biosensor surface. Ray S, Steven RT, Green FM, Höök F, Taskinen B, Hytönen VP, Shard AG. Langmuir. 2015 31(6):1921-30.</li>
</ol>

CHARGE-NEUTRALIZED CHIMERIC AVIDIN with linkable cysteine in C-terminal from E.COLI

CHARGE-NEUTRALIZED CHIMERIC AVIDIN with linkable cysteine in C-terminal

ABBREVIATIONS: FN

STRUCTURE: 
Fibronectin exists as a protein dimer, consisting of two nearly identical monomers linked by a pair of disulfide bonds. The fibronectin protein is produced from a single gene, but alternative splicing of its pre-mRNA leads to the creation of several isoforms. 
 
Two types of fibronectin are present in vertebrates:

<ul type="disc">
	<li>soluble plasma fibronectin (formerly called "cold-insoluble globulin", or CIg) is a major protein component of blood plasma (300 μg/ml) and is produced in the liver by hepatocytes.</li>
	<li>insoluble cellular fibronectin is a major component of the extracellular matrix. It is secreted by various cells, primarily fibroblasts, as a soluble protein dimer and is then assembled into an insoluble matrix in a complex cell-mediated process.</li>
</ul>

Molecular weight of isoform 1 of fibronectin is 262,625 Da based on amino acid sequence information and the observed size in reducing SDS-PAGE is around 250 kDa. 
 
Fibronectin binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectin is involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. It is also involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, and is essential for osteoblast mineralization. It also participates in the regulation of type I collagen deposition by osteoblasts.

PHYSICAL PROPERTIES: 
Calculated isoelectic point (pI) of FN is &nbsp; 5.5-6.3. 
Extinction coefficient&nbsp;of FN is&nbsp;367375 M-1 cm-1 (at 280 nm measured in water).

SOLUBILITY / SOLUTION STABILITY: 
Fibronectin is shipped at ambient temperature. Upon arrival store dry at –20°C or lower. Lyophilized product is moisture-sensitive. Reconstituted and sterile-filtered product can be stored for 1 month at +2...8°Cis

METHOD OF PREPARATION: 
Fibronectin is a major protein found in human plasma and is purified by affinity chromatography on Gelatin Sepharose 4B (GE Healthcare Life Sciences). It is eluted using XXX and dialyzed to YYY. It is then lyophilized in concentration of 1.4 mg/ml after dialysis to 150 mM NaCl, 10 mM sodium phosphate pH 7.5 and 1% Trehalose to ensure stability in storage and during shipping. Purity is over 95% based on SDS-PAGE (band around 250 kDa)

PRODUCT DESCRIPTION / USAGE:

Reconstitution of lyophilized fibronectin is done by using 1 ml of warm (37°C) PBS per 1.4 mg of lyophilized fibronectin. Incubate at 37°C for 3 hours, occasionally inverting the vial. Do not vortex. Reconstituted solution contains 1 mg/ml of soluble fibronectin and a minor quantity of insoluble fibronectin aggregate. Filter slowly through prewetted 0.2 µm membrane filter. Concentration 1 mg/ml of fibronectin corresponds to A280 - 1.4

REFERENCES

<ul>
	<li>Fibronectin at a glance. Pankov R, Yamada KM. Journal of Cell Science 115 (Pt 20): 3861–3. doi:10.1242/jcs.00059.</li>
	<li>Talin-bound NPLY motif recruits integrin-signaling adapters to regulate cell spreading and mechanosensing. Pinon P, Pärssinen J, Vazquez P, Bachmann M, Rahikainen R, Jacquier MC, Azizi L, Määttä JA, Bastmeyer M, Hytönen VP, Wehrle-Haller B. J Cell Biol. 2014,205(2):265-81.</li>
</ul>

Protein FIBRONECTIN / Gene FN1 / Organism Homo sapiens (Human)

Fibronectin

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Institute of Biosciences and Medical Technology (BioMediTech) has developed new avidin proteins which offer new or better tools for avidin-biotin technology. We offer thermally stable avidin named&nbsp;Chimeric avidin&nbsp;(Tm &gt; 105 °C) and neutralized version of it (Charge-neutralized chimeric avidin). Moreover, we have used successfully cysteine introduced at the C-terminal end of protein to attach it covalently to the biosensor surfaces. Various avidins are available with C-terminal cysteine (Chimeric avidin with C-terminal cysteine;&nbsp;Charge-neutralized chimeric avidin with C-terminal cysteine).&nbsp;Switchavidin&nbsp;offers regenerable avidin for many purposes, including development of reusable sensor surfaces.

We have capability to make covalent attachments of dyes, fluorophores, biotin etc. to the proteins by request.

<figure role="group"><img src="https://content-webapi.tuni.fi/image-style/max_1300x1300/proxy/public/2021-05/ncavidin_silver.png?itok=toHlakiS" alt="Structure of tetrameric avidin with four biotin molecules in their binding pockets" ><figcaption>Figure 1. Structure of tetrameric avidin with four biotin molecules in their binding pockets.</figcaption></figure>

<h2>Related articles</h2>

Chimeric avidin shows good stability in harsh chemical conditions – Biochemical analysis and 3D structure. 
Määttä JA, Eisenberg-Domovich Y, Nordlund H, Hayouka R, Kulomaa MS, Livnah, O, Hytönen VP. (2010) 
Biotechnol Bioeng. 2011 Mar;108(3):481-90.

<ul>
	<li>Chimeric avidin</li>
	<li>Charge-neutralized chimeric avidin</li>
</ul>

<hr>
Heikkinen JJ, Riihimäki TA, Määttä JA, Suomela SE, Kantomaa J, Kulomaa MS, Hytönen VP, Hormi OE. (2011) 
Covalent biofunctionalization of cellulose acetate with thermostable chimeric avidin. ACS Appl Mater Interfaces. 2011 Jul;3(7):2240-5. 
Epub 2011 Jun 16.

<ul>
	<li>Chimeric avidin</li>
	<li>Charge-neutralized chimeric avidin</li>
</ul>

<hr>
Structural and Functional Characteristics of Chimeric Avidins Physically Adsorbed onto Functionalized Polythiophene Thin Films. 
Albers WM, Pelto JM, Suspène C, Määttä JA, Yassar A, Hytönen VP, Vikholm-Lundin IM, Tappura K. (2012) 
ACS Appl Mater Interfaces. 2012 Jul 24. [Epub ahead of print]

<ul>
	<li>Chimeric avidin with C-terminal cysteine</li>
	<li>Charge-neutralized chimeric avidin with C-terminal cysteine</li>
</ul>

<hr>
Cysteine-tagged chimeric avidin forms high binding capacity layers directly on gold. 
Vikholm-Lundin IM, Auer S, Paakkunainen M, Määttä JA, Muntera T, Leppiniemi J, Hytönen VP, Tappura K. (2012) 
Sensors and Actuators B: Chemical. 2012 May; 171-172:440-448.

<ul>
	<li>Chimeric avidin with C-terminal cysteine</li>
	<li>Charge-neutralized chimeric avidin with C-terminal cysteine</li>
</ul>

<hr>
Switchavidin: reversible biotin-avidin-biotin bridges with high affinity and specificity. 
Taskinen B, Zauner D, Lehtonen SI, Koskinen M, Thomson C, Kähkönen N, Kukkurainen S, Määttä JA, Ihalainen TO, Kulomaa M, Gruber HJ, Hytonen VP (2014). 
Bioconjug Chem. 2014 Nov 18.

<ul>
	<li>Switchavidin</li>
</ul>

ProtMarket

ProtMarket

General information

RECOMBINANT AVIDIN

RECOMBINANT AVIDIN from E.COLI

SwitchAVIDIN

Switchavidin from E.coli (2,3)

CHIMERIC AVIDIN

CHIMERIC AVIDIN fromE.COLI

CHARGE-NEUTRALIZED CHIMERIC AVIDIN

CHARGE-NEUTRALIZED CHIMERIC AVIDIN from E.COLI

CHARGE-NEUTRALIZED CHIMERIC AVIDIN with linkable cysteine in C-terminal

CHARGE-NEUTRALIZED CHIMERIC AVIDIN with linkable cysteine in C-terminal from E.COLI

Fibronectin

Protein FIBRONECTIN / Gene FN1 / Organism Homo sapiens (Human)

Background

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