Product Name: HS3ST5 Antibody
Species Reactivity: Human, Mouse, Rat
Tested Applications: ELISA, WB
Applications: HS3ST5 antibody can be used for detection of HS3ST5 by ELISA at 1:1562500. HS3ST5 antibody can be used for detection of HS3ST5 by western blot at 0.5 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 – 100,000.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 40 kDa
Immunogen: Antibody produced in rabbits immunized with a synthetic peptide corresponding a region of human HS3ST5.
Host Species: Rabbit
Purification: Antibody is purified by peptide affinity chromatography method.
Physical State: Lyophilized
CAS NO.: 890190-22-4
Product: BEC (hydrochloride)
Buffer: Antibody is lyophilized in PBS buffer with 2% sucrose. Add 50 μL of distilled water. Final antibody concentration is 1 mg/mL.
Concentration: 1 mg/ml
Storage Conditions: For short periods of storage (days) store at 4˚C. For longer periods of storage, store HS3ST5 antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: HS3ST5, 3-OST-5, 3OST5, HS3OST5, NBLA04021
Accession NO.: NP_705840
Protein Ino: 45267824
Official Symbol: HS3ST5
Geneid: 222537
Background: HS3ST5 is the rate limiting enzyme for synthesis of HSact. It performs the crucial step modification in the biosynthesis of anticoagulant heparan sulfate (HSact) that is to complete the structure of the antithrombin pentasaccharide binding site. HS3ST5 also generates GlcUA-GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry.HS3ST5 belongs to a group of heparan sulfate 3-O-sulfotransferases (EC 2.8.2.23) that transfer sulfate from 3-prime-phosphoadenosine 5-prime phosphosulfate (PAPS) to heparan sulfate and heparin (Mochizuki et al., 2003 [PubMed 12740361]).
PubMed ID:http://aac.asm.org/content/24/1/1.abstract
