Antibody data
- Antibody Data
- Antigen structure
- References [4]
- Comments [0]
- Validations [0]
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- Product number
- ABIN363119 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Spleen tyrosine Kinase (SYK) (AA 321-325) antibody
- Antibody type
- Polyclonal
- Antigen
- Peptide sequence around AA 321-325 (N-P-Y-E-P) derived from Human syk. Antibodies were produced by immunizing rabbits with synthetic peptide and KLH conjugates.
- Description
- The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific immunogen.
- Reactivity
- Human
- Host
- Rabbit
- Epitope
- AA 321-325
- Isotype
- IgG
- Vial size
- 50 μL
- Concentration
- 1 mg/mL
- Storage
- Store at -20°C for long term preservation (recommended). Store at 4°C for short term use.
Submitted references Phosphorylation of Syk activation loop tyrosines is essential for Syk function. An in vivo study using a specific anti-Syk activation loop phosphotyrosine antibody.
Tyrosine kinase SYK: essential functions for immunoreceptor signalling.
Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases.
Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk.
Zhang J, Billingsley ML, Kincaid RL, Siraganian RP
The Journal of biological chemistry 2000 Nov 10;275(45):35442-7
The Journal of biological chemistry 2000 Nov 10;275(45):35442-7
Tyrosine kinase SYK: essential functions for immunoreceptor signalling.
Turner M, Schweighoffer E, Colucci F, Di Santo JP, Tybulewicz VL
Immunology today 2000 Mar;21(3):148-54
Immunology today 2000 Mar;21(3):148-54
Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases.
Deckert M, Elly C, Altman A, Liu YC
The Journal of biological chemistry 1998 Apr 10;273(15):8867-74
The Journal of biological chemistry 1998 Apr 10;273(15):8867-74
Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk.
Law CL, Chandran KA, Sidorenko SP, Clark EA
Molecular and cellular biology 1996 Apr;16(4):1305-15
Molecular and cellular biology 1996 Apr;16(4):1305-15
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