AV53653
Anti-ST6GALNAC2 antibody produced in rabbit
affinity isolated antibody
别名:
Anti-SIAT7, Anti-SIAT7B, Anti-SIATL1, Anti-ST6 -N-acetylgalactosaminide α-2,6-sialyltransferase 2, Anti-ST6GalNAII, Anti-STHM
生物来源
rabbit
质量水平
偶联物
unconjugated
抗体形式
affinity isolated antibody
抗体产品类型
primary antibodies
克隆
polyclonal
表单
buffered aqueous solution
分子量
42 kDa
种属反应性
human, horse, rat, rabbit, pig
浓度
0.5 mg - 1 mg/mL
技术
western blot: suitable
NCBI登记号
UniProt登记号
运输
wet ice
储存温度
−20°C
靶向翻译后修饰
unmodified
基因信息
human ... ST6GALNAC2(10610)
一般描述
ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase is an enzyme encoded by the ST6GALNAC2 gene in humans. It belongs to the family of sialyltransferases. It is found in various human cell lines and is also expressed in most cell types with notable exceptions for several myeloid and lymphoid cell lines.
免疫原
Synthetic peptide directed towards the middle region of human ST6GALNAC2
应用
Anti-ST6GALNAC2 antibody produced in rabbit is suitable for western blotting at a concentration of 1μg/mL.
生化/生理作用
ST6GALNAC2 is primarily expressed in skeletal muscle, heart, kidney, placenta, lung and leukocytes. Overexpression of ST6GALNAC2 abolishes the cell surface HECA-452/CLA expression, reduces the number of rolling leukocytes on P- and L-selectin-bearing substrates as well as enhances the median rolling velocity of remaining cells during the synthesis of the leukocyte selectin ligand on human P-selectin glycoprotein ligand-1. Increased expression of the sialyltransferase ST6GalNAc-II indirectly reduces the galactosylation of the O-glycan substrate.
外形
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
其他说明
Synthetic peptide located within the following region: VNTMKNSLVSYWNLGFTSVPQGQDLQYIFIPSDIRDYVMLRSAILGVPVP
免责声明
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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储存分类代码
10 - Combustible liquids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
Georgia Sotiropoulou et al.
Molecular medicine (Cambridge, Mass.), 8(1), 42-55 (2002-05-02)
We sought to identify genes with altered expression during human breast cancer progression by applying mRNA comparisons of normal and tumor mammary cell lines with increasingly malignant phenotypes. The gene encoding a new sialyltransferase (STM) was found to be down-regulated
Hitoshi Suzuki et al.
The Journal of biological chemistry, 289(8), 5330-5339 (2014-01-09)
IgA nephropathy (IgAN), the most common primary glomerulonephritis, is characterized by renal immunodeposits containing IgA1 with galactose-deficient O-glycans (Gd-IgA1). These immunodeposits originate from circulating immune complexes consisting of anti-glycan antibodies bound to Gd-IgA1. As clinical disease onset and activity of
Milan Raska et al.
Journal of molecular biology, 369(1), 69-78 (2007-04-10)
Glycosylation defects occur in several human diseases. In IgA nephropathy, IgA1 contains O-glycans that are galactose-deficient and consist mostly of core 1 alpha2,6 sialylated N-acetylgalactosamine, a configuration suspected to prevent beta1,3 galactosylation. We confirmed the same aberrancy in IgA1 secreted
B Samyn-Petit et al.
Biochimica et biophysica acta, 1474(2), 201-211 (2000-04-01)
A cDNA clone encoding a human Galbeta1-3GalNAc alpha2, 6-sialyltransferase (designated hST6GalNAc II) was identified employing the PCR with degenerated primers to the sialylmotifs, followed by BLAST analysis of databanks. This sialyltransferase sequence is similar to that of previously cloned ST6GalNAc
Chi Y Lo et al.
The Journal of biological chemistry, 288(20), 13974-13987 (2013-04-04)
The binding of selectins to carbohydrate ligands expressed on leukocytes regulates immunity and inflammation. Among the human selectin ligands, the O-linked glycans at the N-terminus of the leukocyte cell-surface molecule P-selectin glycoprotein ligand-1 (PSGL-1, CD162) are important because they bind
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