WESTERN BLOT
**Western Blot**
~~ ULB +
Lysosomes have lots of proteases. We want to protect proteins as we lyse cells.
Lysosomes will not work when pH around 5.
Protease Inhibitors 2. Phosphatase inhibitors
1. Protease Inhibitors: Cocktail
Aptoninin: Serine protease inhibitor
Chymastatine: Serine and Cysteine protease inhibitor
Leupeptin: Serine and Cysteine protease inhibitor
Pepstain: general Inhibitor (blocks lots of Proteases)
2. Phosphatase inhibitors: Cell signaling
Beta- glycerophotase *
Sodium molybdate *
Sodium othoranadate *
*main ones*
DMSF
3. DTT : Breaks disulfide bridges
Make ULB (Lysis Buffer)
SDS
Tris
NaCl
NaF pH inhibitor
DTT
Do 5’ fold and 10’ fold dilutions with lysis buffer and do reading of those
whichever one gives you reading within the linear range of the assay is one you’ll use.
*Western Blot*
RNA —→ Protein
Translation —> Western Blot
Isolate Protein from tissue or cells
Lyse cells — make homogenate
Basis* ULB
Lysis Buffer (ULB):
1. Detergent: (SDS) non-ionic detergent*
NP-40
Triton X100
5% w/v
2. Tris: pH regulator*
pH 7.5
50 mM
3. NaCl (salt) - 50 mM*
Dissolves into ionic form when mixed with H2O
Change the salinity of the solution around the cell
create hypotonic solution
lots of ions inside cells
Water rushes in, destabilizing the membrane
Lyses cell
4. NaF: Phosphate inhibitor - 50mM
Make Buffer
Weight out solids
Add water (amt. based on solvent)
Add HCl to bring pH down to 7.5
Add water
Protein Assay:
Protein Assay: Bradford Assay
Commassile Brilliant blue G - 250 dye
Dye binds to basic amino acids arginine and aromatic a.a
changes to blue
More protein you have, more dye that binds, more blue you get
If we do lysis and have concentrated protein lysate we’ll have to serail dilute a couple of times.
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y=mx+b x is mult by 2 or 5.
look at notes for math portion
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SDS-Page: (gel electrophoresed for proteins)
Sodium dodecyl sulfate Polyacrylamide gel electrophoresis (8% -12%)
anionic detergent
Coats proteins
uniform negate charge
Acrylamide
thin, run up and down, separate proteins.
Glycine
an amino acid that can be protonated or deprotonated
TEMED
the catalyst causes the cross-pattern
APS
catalyst polymerizes acrylamide
Loading dye for SDS-PAGE
Mix diluted proteins with loading dye
Tris Buffer -7.5
Bromophenol Blue
Glycerol
DTT
Glycine
Gel components: what do they do?
Tris pH 6.8 standing
Tris ph 8.8 running
Glycine
SDS
Acrylamide
Bis - acrylamide
APS
TEMED
H2O
Running buffer
SDS
Glycine
Tris
Shape- linear
denature 95C for 5 min
Breaks disulfide bridges (DTT or Beta- mercaptoethanol)
Reducing agents
~~Transfer
Buffer
Glycine
Tris
Structure for gel stain
Metal plate
filter paper
PVDF membrane (methanol)
Gel
Filter paper
Metal plate
PVDF has the transfer
Stain membrane with
Ponceau S (red dye)
protein adhesión
Wash H2O
Block with milk in T-TBS
Clean off any weakly associated bonds
Saline weak ion and bonding
weak hydrophobic
Process:
Milk - fill all open spaces on the membrane
Wash T-TBS
3x -5min
Incubate with 1` antibody diluted with MyHC
in 5% milk + T-TBS (10mL)
1-2hr @RT
Wash T-TBS
3x -5min
Incubate with 2` antibody
5% milk + T-TBS (30-60 min)
Wash T-TBS
3x -5min
Develop
light production
What is the purpose of using a secondary antibody for western blotting?
Bind to the primary antibody, Amplify the level of the detection signal, and Eliminate the need to enzyme-conjugate every primary antibody.