Explore
Validate
Learn
Western blotAntibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations
- Western blot [1]
Submit
Validation data
Reference
Comment
Report error
- Product number
- ABIN953983 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Pancreatic Lipase (PNLIP) (AA 311-341), (C-Term) antibody
- Antibody type
- Polyclonal
- Description
- Protein A column, followed by peptide affinity purification
- Reactivity
- Human
- Host
- Rabbit
- Epitope
- C-Term, AA 311-341
- Vial size
- 0.4 mL
- Storage
- Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer.
- Handling
- Avoid repeated freezing and thawing.
Submitted references Modification of pancreatic lipase properties by directed molecular evolution.
Amplitude of pancreatic lipase lid opening in solution and identification of spin label conformational subensembles by combining continuous wave and pulsed EPR spectroscopy and molecular dynamics.
Trp-107 and trp-253 account for the increased steady state fluorescence that accompanies the conformational change in human pancreatic triglyceride lipase induced by tetrahydrolipstatin and bile salt.
Lid opening and unfolding in human pancreatic lipase at low pH revealed by site-directed spin labeling EPR and FTIR spectroscopy.
Exploring the active site cavity of human pancreatic lipase.
Colin DY, Deprez-Beauclair P, Silva N, Infantes L, Kerfelec B
Protein engineering, design & selection : PEDS 2010 May;23(5):365-73
Protein engineering, design & selection : PEDS 2010 May;23(5):365-73
Amplitude of pancreatic lipase lid opening in solution and identification of spin label conformational subensembles by combining continuous wave and pulsed EPR spectroscopy and molecular dynamics.
Ranaldi S, Belle V, Woudstra M, Bourgeas R, Guigliarelli B, Roche P, Vezin H, Carrière F, Fournel A
Biochemistry 2010 Mar 16;49(10):2140-9
Biochemistry 2010 Mar 16;49(10):2140-9
Trp-107 and trp-253 account for the increased steady state fluorescence that accompanies the conformational change in human pancreatic triglyceride lipase induced by tetrahydrolipstatin and bile salt.
Bourbon-Freie A, Dub RE, Xiao X, Lowe ME
The Journal of biological chemistry 2009 May 22;284(21):14157-64
The Journal of biological chemistry 2009 May 22;284(21):14157-64
Lid opening and unfolding in human pancreatic lipase at low pH revealed by site-directed spin labeling EPR and FTIR spectroscopy.
Ranaldi S, Belle V, Woudstra M, Rodriguez J, Guigliarelli B, Sturgis J, Carriere F, Fournel A
Biochemistry 2009 Jan 27;48(3):630-8
Biochemistry 2009 Jan 27;48(3):630-8
Exploring the active site cavity of human pancreatic lipase.
Colin DY, Deprez-Beauclair P, Allouche M, Brasseur R, Kerfelec B
Biochemical and biophysical research communications 2008 Jun 6;370(3):394-8
Biochemical and biophysical research communications 2008 Jun 6;370(3):394-8
No comments: Submit comment
Supportive validation
- Submitted by
- antibodies-online (provider)
- Main image
- Experimental details
- WB
