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Sphingosine Kinase 1 Polyclonal FITC Antibody

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    Sphingosine Kinase 1 Polyclonal FITC Antibody
  • Sphingosine Kinase 1 Polyclonal FITC Antibody
Cat No: 10012201
Cayman

The primary use of this antibody conjugate is for the detection of SPHK1 in intact cells by direct immunolabeling methods such as flow cytometry or immunofluorescence microscopy. SPHK1 is one of the enzymes involved in sphingolipid metabolism. SPHK1 c...

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: 500 µl

This product can only be bought through Cayman Chemical. Please contact us.

Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • SPHK-1 metabolism sphingolipids phosphorylation sphingosine-1-phosphate cell proliferation death immunofluorescence IF flow cytometry FC western blots WB SPHKs blotting immunoblotting
Product Overview:
The primary use of this antibody conjugate is for the detection of SPHK1 in intact cells by direct immunolabeling methods such as flow cytometry or immunofluorescence microscopy. SPHK1 is one of the enzymes involved in sphingolipid metabolism. SPHK1 catalyzes the phosphorylation of sphingosine to sphingosine-1-phosphate. This reaction plays an important role in determining cell proliferation versus cell death.{13916,14481} SPHK1 is found in a wide variety of tissues and cell types including kidney, liver, spleen, heart, platelets, and human tumors.{13076} On a cellular level, it is found in the cytosolic and membrane fractions.{14482} Based on the amino acid sequence, this protein has a molecular weight of approximately 43 kDa. Some reported post translational modifications may explain the shift in band migration to 50 kDa.{14483} NOTE: Multiple isoforms of SPHK1 are known and one is 470 amino acids. This likely explains the 50 kDa band observed.
Size 500 µl
Shipping dry ice
Host Rabbit
Antigen Synthetic peptide from an internal region of human SPHK1
Application(s)

FC and WB

Formulation 100 µg of Peptide affinity-purified antibody conjugated to fluorescein
Custom Code 3822.19
UNSPSC code 12352203

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Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.

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