Tris-based Buffers - Category Selection Guide
Tris-buffered saline at three strengths, a Tween-containing TBST, and a sterile Tris-HCl buffer — twelve catalog numbers across five product pages. This page is a category reference; pick the strength and format your protocol needs and click View for its product page.
| Cat. No. | Format | Size |
|---|---|---|
|
Tris Buffered Saline TBS, 1X (Tris Buffered Saline), Non-Sterile 1X · 3 catalog numbers · 500 ml · 1000 ml · 10 L
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| DCP-TBS1X_500ml | 1X | 500 ml |
| DCP-TBS1X_1000ml | 1X | 1000 ml |
| DCP-TBS1X_10 Liter | 1X | 10 L |
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Tris Buffered Saline TBS, 10X (Tris Buffered Saline), Non-Sterile 10X · 2 catalog numbers · 500 ml · 1000 ml
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| DCP-TBS10X_500 ml | 10X | 500 ml |
| DCP-TBS10X_1000 ml | 10X | 1000 ml |
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Tris Buffered Saline TBS, 20X (Tris Buffered Saline), Non-Sterile 20X · 2 catalog numbers · 500 ml · 1000 ml
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| DCP-TBS20X_500 ml | 20X | 500 ml |
| DCP-TBS20X_1000 ml | 20X | 1000 ml |
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Tris Buffered Saline TBST (Tris-buffered saline, 0.1% Tween 20) 0.1% Tween 20 · 2 catalog numbers · 500 ml · 1000 ml
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| DCP-TBST0.1X_500ml | 0.1% Tween 20 | 500 ml |
| DCP-TBST0.1X_1 L | 0.1% Tween 20 | 1000 ml |
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Tris-HCl Buffer, Sterile Sterile · 3 catalog numbers · 100 ml · 500 ml · 1000 ml
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| DCP-THB1X_100 ml | Sterile | 100 ml |
| DCP-THB1X_500 ml | Sterile | 500 ml |
| DCP-THB1X_1000 ml | Sterile | 1000 ml |
Not sure which one? Check the Tris chemistry reference · See applications by format · Read the FAQ
One buffer chemistry, five ways to buy it
Tris-buffered saline (TBS) is an isotonic, non-toxic buffer used in various biochemical experiments to maintain a narrow, slightly alkaline pH range of 7-9. While the conjugate acid of Tris has a pKa of 8.07 at 25 °C, the solution pH shift is observed as temperature changes (0.03 units per degree Celsius). TBS buffer is commonly used as a laboratory reagent for washing, diluting, cell culture processing, Western blotting, ELISA and multiple assays and immunohistochemistry steps. Tris acts as a buffering agent, and NaCl regulates the solution’s tonicity, allowing it to be isotonic or hypertonic based on the desired concentration.
- Three TBS strengths: 1X, 10X and 20X, all published as Non-Sterile.
- One detergent format: TBST — Tris-buffered saline with 0.1% Tween 20.
- One sterile format: Tris-HCl Buffer, Sterile, in 100 ml, 500 ml and 1000 ml.
- Buffering chemistry: Tris acts as the buffering agent and NaCl regulates tonicity, allowing the solution to be isotonic or hypertonic based on the desired concentration.
- pH behaviour: a narrow, slightly alkaline range of 7–9, with the conjugate acid at pKa 8.07 at 25 °C and a shift of 0.03 units per degree Celsius.
- Contaminant control: Protease (−), DNAse (−), RNAse (−), Endonuclease (−).
- Filtration: all reagents filtered TWICE (2X) through 0.1 micron membrane filters. No mycoplasma.
- CategoryTris-based Buffers
- Conjugate acid pKa (25 °C)8.07
- pH shift with temperature0.03 units per °C
- Buffered pH range7–9
- Buffering agentTris
- Tonicity agentNaCl
- TBS strengths stocked1X, 10X, 20X
- Detergent formatTBST, 0.1% Tween 20
- Nuclease / protease statusProtease (−), DNAse (−), RNAse (−), Endonuclease (−)
- Filtration0.1 µm membrane, twice (2X); no mycoplasma
A mild buffer with one property you have to plan around
Tris is the default buffer of the protein bench for reasons the source states plainly — and it carries one well-documented quirk that decides whether a cold-room protocol lands where you think it does. Cards citing a bracketed number are supported by the reference list at the foot of the page.
Buffering where proteins live
TBS holds a narrow, slightly alkaline pH range of 7–9, with the conjugate acid of Tris at pKa 8.07 at 25 °C — the region where most protein work is done.
pH moves with temperature
The source states the shift directly: 0.03 pH units per degree Celsius. Adjust the pH at the temperature the buffer will actually be used at, not at the bench and then in the cold room.
Tonicity is a separate dial
Tris does the buffering; NaCl regulates the solution’s tonicity, allowing it to be isotonic or hypertonic based on the desired concentration. Two independent variables, two independent decisions.
Mild toward the sample
The source describes Tris-HCl as a mild buffer that does not significantly interfere with or inhibit most biochemical processes and protein-protein interactions, and whose buffering capacity prevents abrupt pH changes during purification that could denature or degrade proteins.
The buffer the standard methods were written in
Tris-glycine gel and running-buffer systems[7] and the original electrophoretic transfer and immunodetection procedure[8] are both built on Tris, which is why so many protocols specify a Tris base rather than a phosphate one.
Contaminant control is specified
Protease (−), DNAse (−), RNAse (−), Endonuclease (−), all reagents filtered TWICE (2X) through 0.1 micron membrane filters, and no mycoplasma — the source states all four for the family.
The number to plan around
A Tris buffer titrated at the bench does not hold that pH in a 4 °C purification or a 37 °C incubation. At 0.03 units per degree Celsius, a twenty-degree move is roughly six-tenths of a pH unit — enough to move a protein away from the window a protocol assumes. Titrate at the working temperature.
Two passes through a 0.1 micron membrane
The source states one purity line for the whole family, and it applies to every catalog number on this page: all reagents filtered TWICE (2X) through 0.1 micron membrane filters, with no mycoplasma, and with protease, DNAse, RNAse and endonuclease all reported negative.
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1
0.1 µm Membrane filtration I
First pass through a 0.1 micron membrane filter, removing large particulates and aggregates.
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2
0.1 µm Membrane filtration II
Second pass through a 0.1 micron membrane filter. The source states TWICE (2X) for all reagents in this family, and reports no mycoplasma.
The published values, and what the controlling literature says
Every numeric claim the source makes about Tris was checked twice against the primary physical-chemistry literature before this page was written. The outcome of each check is stated below, so nothing has to be taken on trust.
| Parameter | As published by Diagnocine | Controlling literature | Verification outcome |
|---|---|---|---|
| Conjugate acid pKa at 25 °C | 8.07 | 8.075 in water by emf measurement[1,2]; 8.071 ± 0.009 by potentiometry at infinite dilution[3] | check_circle Confirmed twice. Source value stands; no correction made. |
| pH shift with temperature | 0.03 units per degree Celsius | Tris has one of the largest temperature coefficients among common biological buffers, established from its dissociation constant measured from 0 to 50 °C[1] | check_circle Consistent with the published temperature dependence. |
| Working pH range | 7–9, narrow and slightly alkaline | Consistent with a pKa near 8.07, since useful buffering spans roughly one pH unit either side of the pKa[4] | check_circle Consistent. |
| Buffering agent / tonicity agent | Tris buffers; NaCl regulates tonicity | Not a literature question — a formulation statement | Reproduced as published. |
| Detergent in TBST | 0.1% Tween 20 | Tween 20 was introduced into this workflow as a non-ionic detergent that blocks unoccupied protein-binding sites on nitrocellulose[5] | Reproduced as published; see the FAQ for the caveat on Tween 20 used alone[6]. |
Which format for which bench workflow
The source publishes two application lists: one for TBS and one for Tris-HCl buffer. Each is reproduced below under the formats it belongs to, one item per line, with nothing added.
- Washing
- Diluting
- Cell culture processing
- Western blotting
- ELISA and multiple assays
- Immunohistochemistry steps
- The same TBS application list applies, since the source publishes TBST as Tris-buffered saline carrying 0.1% Tween 20: washing, diluting, cell culture processing, Western blotting, ELISA and multiple assays, and immunohistochemistry steps.
- The detergent is what distinguishes it: Tween 20 entered this workflow as a non-ionic detergent used to block unoccupied protein-binding sites on nitrocellulose.[5]
- Blocking and washing choices are not interchangeable — a direct comparison of albumin, milk and Tween 20 on nitrocellulose found both quantitative and qualitative differences in the antigens detected.[9]
- Gel electrophoresis
- Nucleic acid work
- Protein extraction and purification
- Preparing SDS-PAGE gel solutions
- Electrophoresis running buffers
- Cell culture media
The five products side by side
Every value in this table is reproduced from the catalog exactly as published, including the group label the source places over the first four rows.
| Product | Source group | Format | Catalog numbers | Sizes |
|---|---|---|---|---|
| TBS, 1X (Tris Buffered Saline), Non-Sterile | Tris Buffered Saline | 1X | DCP-TBS1X_500ml DCP-TBS1X_1000ml DCP-TBS1X_10 Liter |
500 ml, 1000 ml, 10 L |
| TBS, 10X (Tris Buffered Saline), Non-Sterile | Tris Buffered Saline | 10X | DCP-TBS10X_500 ml DCP-TBS10X_1000 ml |
500 ml, 1000 ml |
| TBS, 20X (Tris Buffered Saline), Non-Sterile | Tris Buffered Saline | 20X | DCP-TBS20X_500 ml DCP-TBS20X_1000 ml |
500 ml, 1000 ml |
| TBST (Tris-buffered saline, 0.1% Tween 20) | Tris Buffered Saline | 0.1% Tween 20 | DCP-TBST0.1X_500ml DCP-TBST0.1X_1 L |
500 ml, 1000 ml |
| Tris-HCl Buffer, Sterile | no group label in source | Sterile | DCP-THB1X_100 ml DCP-THB1X_500 ml DCP-THB1X_1000 ml |
100 ml, 500 ml, 1000 ml |
Frequently asked questions
The questions that come up when a purchasing spec meets a bench protocol.
Physical-chemistry and method literature behind the values above
The Diagnocine source description carries no citation list of its own. The sources below are the ones used to verify its numbers and to support the cited statements on this page; each was checked against its published record before it was listed.
- Bates RG, Hetzer HB (1961). Dissociation constant of the protonated acid form of 2-amino-2-(hydroxymethyl)-1,3-propanediol [tris(hydroxymethyl)aminomethane] and related thermodynamic quantities from 0 to 50°. J Phys Chem 65(4):667–671. doi:10.1021/j100822a017 — the primary determination of the Tris pKa and its temperature dependence.
- Etz ES, Robinson RA, Bates RG (1973). Dissociation constant of protonated tris(hydroxymethyl)aminomethane in N-methylpropionamide and related thermodynamic quantities from 10 to 55°C. J Solution Chem 2(4):405–415. doi:10.1007/BF00713253 — second, independent statement of pKa 8.075 in water at 25 °C.
- Schindler P, Robinson RA, Bates RG (1968). Solubility of tris(hydroxymethyl)aminomethane in water-methanol solvent mixtures and medium effects in the dissociation of the protonated base. J Res Natl Bur Stand 72A(2):141–148. doi:10.6028/jres.072A.014
- Good NE, Winget GD, Winter W, Connolly TN, Izawa S, Singh RMM (1966). Hydrogen ion buffers for biological research. Biochemistry 5(2):467–477. doi:10.1021/bi00866a011
- Batteiger B, Newhall WJ 5th, Jones RB (1982). The use of Tween 20 as a blocking agent in the immunological detection of proteins transferred to nitrocellulose membranes. J Immunol Methods 55(3):297–307. doi:10.1016/0022-1759(82)90089-8
- Bird CR, Gearing AJH, Thorpe R (1988). The use of Tween 20 alone as a blocking agent for immunoblotting can cause artefactual results. J Immunol Methods 106(2):175–179.
- Laemmli UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(5259):680–685. doi:10.1038/227680a0 — the Tris-based discontinuous gel and running-buffer system.
- Towbin H, Staehelin T, Gordon J (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76(9):4350–4354. doi:10.1073/pnas.76.9.4350
- Spinola SM, Cannon JG (1985). Different blocking agents cause variation in the immunologic detection of proteins transferred to nitrocellulose membranes. J Immunol Methods 81(1):161–165. doi:10.1016/0022-1759(85)90132-2
