Antibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations
- Western blot [1]
- Immunohistochemistry [1]
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- Product number
- ABIN359344 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-PKM2 (C-Term) antibody
- Antibody type
- Polyclonal
- Description
- Prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS
- Reactivity
- Human
- Host
- Rabbit
- Epitope
- C-Term
- Vial size
- 0.4 mL
- Storage
- Store the antibody undiluted at 2-8°C for one month or (in aliquots) at-20°C for longer.
- Handling
- Avoid repeated freezing and thawing.
Submitted references A protein interaction framework for human mRNA degradation.
Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.
Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.
Properties of the nonhelical end domains of vimentin suggest a role in maintaining intermediate filament network structure.
Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth.
Lehner B, Sanderson CM
Genome research 2004 Jul;14(7):1315-23
Genome research 2004 Jul;14(7):1315-23
Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J
Nature biotechnology 2003 May;21(5):566-9
Nature biotechnology 2003 May;21(5):566-9
Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.
Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A
The Journal of biological chemistry 2002 Jun 28;277(26):23807-14
The Journal of biological chemistry 2002 Jun 28;277(26):23807-14
Properties of the nonhelical end domains of vimentin suggest a role in maintaining intermediate filament network structure.
Lowrie DJ Jr, Stickney JT, Ip W
Journal of structural biology 2000 Nov;132(2):83-94
Journal of structural biology 2000 Nov;132(2):83-94
Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth.
Williams JM, Chen GC, Zhu L, Rest RF
Molecular microbiology 1998 Jan;27(1):171-86
Molecular microbiology 1998 Jan;27(1):171-86
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Supportive validation
- Submitted by
- antibodies-online (provider)
- Main image
- Experimental details
- WB
Supportive validation
- Submitted by
- antibodies-online (provider)
- Main image
- Experimental details
- IHC