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>   首页   >   产品   >   一抗   >   代谢   >   CHST10 Antibody   

CHST10 Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - CHST10 Antibody AP50588
    Western blot analysis of lysate from human brain tissue lysate,using CHST10 Antibody(AP50588). AP50588 was diluted at 1:1000. A goat anti-rabbit IgG H&L(HRP) at 1:5000 dilution was used as the secondary antibody.Lysate at 35ug.
  • 2 - CHST10 Antibody AP50588
    Immunohistochemistry analysis of paraffin-embedded human lung carcinoma tissue, using CHST10 antibody.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC
Primary Accession O43529
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality polyclonal
Calculated MW 42207 Da
Additional Information
Gene ID 9486
Other Names Carbohydrate sulfotransferase 10, 282-, HNK-1 sulfotransferase, HNK-1ST, HNK1ST, HuHNK-1ST, CHST10
Dilution WB~~ 1:1000
IHC~~1:50-1:100
Format Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.09% (W/V) sodium azide and 50% glycerol.
Storage Conditions-20℃
Protein Information
Name CHST10 {ECO:0000303|PubMed:23269668, ECO:0000312|HGNC:HGNC:19650}
Function Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA- (1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis (PubMed:9478973). Sulfates terminal glucuronyl residue of the laminin globular (LG)-domain binding epitope on DAG1/alpha-dystroglycan and prevents further polymerization by LARGE1 glycosyltransferase. Likely defines the chain length of LG epitope, conferring binding specificity to extracellular matrix components (PubMed:32149355). Plays a role in down-regulating the steroid hormones. Sulfates glucuronidated estrogens and androgens with an impact in hormone cycle and fertility. Has a preference for glucuronyl moiety at the 3-hydroxyl group of a sterol ring rather than the 17-hydroxyl group, showing high catalytic efficiency for 17beta-estradiol 3-O-(beta-D-glucuronate) and dehydroepiandrosterone 3-O-(beta-D-glucuronate) hormones (PubMed:23269668).
Cellular Location Golgi apparatus membrane {ECO:0000250|UniProtKB:O54702}; Single-pass type II membrane protein
Tissue Location In fetal tissues, it is predominantly expressed in brain, and weakly expressed in lung, kidney and liver. In adult, it is highly expressed in brain, testis, ovary, expressed at intermediate level in heart, pancreas, skeletal muscle, spleen and thymus, and weakly expressed in other tissues. In brain, it is expressed at higher level in the frontal lobe.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Catalyzes the transfer of sulfate to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis.

REFERENCES

Ong E.,et al.J. Biol. Chem. 273:5190-5195(1998).
Yu W.,et al.Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Hillier L.W.,et al.Nature 434:724-731(2005).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

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