Helix pomatia Lectin (HPA) - Cy5
€0.00
In stock
SKU
BW-21761168
liquid, from snail
Molecular Weight: 79 kDa
Helix pomatia agglutinin (HPA) is isolated from edible snail by affinity chromatography. It is a lectin secreted by albumen gland that produces perivitelline fluid and is composed of protein and polysaccharide complexes that coat each fertilized egg. HPA has the property to aggregate bacteria such as group C streptococci and Listeria monocytogenes, and ability to bind to the surface of herpes virus. This lectin has been shown to agglutinate blood group A red cells but not those of B or O. HPA binds GalNAc present on the Tn antigen, but not its galactosylated form, with potential to also recognize the T antigen. HPA has specificity for GalNAc and GlcNac, with its main inhibitor being N-acetylgalactosamine. This lectin consists of six identical protein subunits, each containing one intra-chain disulfide bond and a carbohydrate binding site, with a total molecular weight of 79 kDa. HPA is a glycoprotein with roughly 7% carbohydrate content and presence of different glycoforms. The structure of HPA brings two sets of three binding sites on opposite hydrophilic and charged faces of the molecule in a construction that allows two bacteria to be bound at the same time, promoting aggregation and efficient protection of snail eggs. HPA has been successfully used as an indicator of metastatic spread in several epithelial neoplasms including breast, colorectum, gastric, prostate and oesophageal cancers. It has also been used in cell binding studies for urinary bladder carcinoma cell lines and an osteogenic sarcoma cell line.
Cy5, when bound to HPA, can show the binding pattern of this lectin in cellular imaging and flow cytometry. The excitation wavelength required for Cy5 to fluoresce is high enough to avoid overlap with most other fluorochromes, making it useful for dual-labeling experiments. Because of this high excitation, there is typically less background from autofluorescence of biological specimens. This product comes in a stabilized liquid form.
Specifications:
Source: Helix pomatia (Roman Snail)
Activity: Specific to blood group A (A1 and A2).
Carbohydrate Specificity: GalNAc, GlcNac
Inhibitory Carbohydrate: N-Acetylgalactosamine
Divalent Ions Required: None required
Conjugation: Cy5
Storage and Stability:
Store frozen at -20°C in amber vials in appropriate aliquot sizes. Avoid freeze thaw cycles. Can be stored at 2-8°C for short term use.
Molecular Weight: 79 kDa
Helix pomatia agglutinin (HPA) is isolated from edible snail by affinity chromatography. It is a lectin secreted by albumen gland that produces perivitelline fluid and is composed of protein and polysaccharide complexes that coat each fertilized egg. HPA has the property to aggregate bacteria such as group C streptococci and Listeria monocytogenes, and ability to bind to the surface of herpes virus. This lectin has been shown to agglutinate blood group A red cells but not those of B or O. HPA binds GalNAc present on the Tn antigen, but not its galactosylated form, with potential to also recognize the T antigen. HPA has specificity for GalNAc and GlcNac, with its main inhibitor being N-acetylgalactosamine. This lectin consists of six identical protein subunits, each containing one intra-chain disulfide bond and a carbohydrate binding site, with a total molecular weight of 79 kDa. HPA is a glycoprotein with roughly 7% carbohydrate content and presence of different glycoforms. The structure of HPA brings two sets of three binding sites on opposite hydrophilic and charged faces of the molecule in a construction that allows two bacteria to be bound at the same time, promoting aggregation and efficient protection of snail eggs. HPA has been successfully used as an indicator of metastatic spread in several epithelial neoplasms including breast, colorectum, gastric, prostate and oesophageal cancers. It has also been used in cell binding studies for urinary bladder carcinoma cell lines and an osteogenic sarcoma cell line.
Cy5, when bound to HPA, can show the binding pattern of this lectin in cellular imaging and flow cytometry. The excitation wavelength required for Cy5 to fluoresce is high enough to avoid overlap with most other fluorochromes, making it useful for dual-labeling experiments. Because of this high excitation, there is typically less background from autofluorescence of biological specimens. This product comes in a stabilized liquid form.
Specifications:
Source: Helix pomatia (Roman Snail)
Activity: Specific to blood group A (A1 and A2).
Carbohydrate Specificity: GalNAc, GlcNac
Inhibitory Carbohydrate: N-Acetylgalactosamine
Divalent Ions Required: None required
Conjugation: Cy5
Storage and Stability:
Store frozen at -20°C in amber vials in appropriate aliquot sizes. Avoid freeze thaw cycles. Can be stored at 2-8°C for short term use.
| Is Featured? | No |
|---|
Write Your Own Review