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STXBP3 antibody
STXBP3
Reactivity: Human, Mouse
WB, ELISA
Host: Mouse
Monoclonal
3G12
unconjugated
Product Details anti-STXBP3 Antibody
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Target
See all STXBP3 Antibodies
STXBP3
(Syntaxin Binding Protein 3 (STXBP3))
Reactivity
All reactivities for STXBP3 antibodies
Human, Mouse
Host
All hosts for STXBP3 antibodies
Mouse
Clonality
All clonalities for STXBP3 antibodies
Monoclonal
Conjugate
All conjugates for STXBP3 antibodies
This STXBP3 antibody is un-conjugated
Application
All applications for STXBP3 antibodies
Western Blotting (WB), ELISA
Purification
The antibody was purified from mouse ascitic fluids by protein-G affinity chromatography
Immunogen
Recombinant PSP , Accession / GI number: NP_004568
Clone
3G12
Isotype
Kappa
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Discover our top product STXBP3 Primary Antibody
Alternatives
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Application Details
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Application Notes
Recommended dilution 1:1000
Restrictions
For Research Use only
Handling
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Format
Liquid
Concentration
1mg/ml
Buffer
In Phosphate-Buffered Saline (pH7.4) with 0.1% Sodium Azide
Preservative
Sodium azide
Precaution of Use
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
-20 °C
Target Details for STXBP3
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Target
STXBP3
(Syntaxin Binding Protein 3 (STXBP3))
Alternative Name
PSP (STXBP3 Products )
Synonyms
MUNC18-3 antibody, MUNC18C antibody, PSP antibody, UNC-18C antibody, Munc18-c antibody, wu:fb71h06 antibody, zgc:63761 antibody, stxbp3 antibody, MGC115462 antibody, Munc-18c antibody, Stxbp3 antibody, Sxtbp3 antibody, Unc18-3 antibody, syntaxin binding protein 3 antibody, syntaxin binding protein 3 L homeolog antibody, STXBP3 antibody, Stxbp3 antibody, stxbp3 antibody, stxbp3.L antibody
Background
Human phosphoserine phosphatase (HPSP), specific for D- and L- phosphoserine, has been identified in all human tissues. HPSP is a Mg(2+)-dependent phosphoserine phosphatase. The three dimensional structure of HPSP reveals the structural and functional role of the divalent cation in the active site of phosphatases. In particular, the complex structures reveal that the open-closed environmental change of the active site, generated by local rearrangement of the alpha-helical bundle domain, is important for the substrate recognition and hydrolysis.
Pathways
Hormone Transport
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