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产品名称
起订量
单价(含增值税)
库存(PCS)
起订数量
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Recombinant Human GALNT3/Polypeptide GalNAc transf48T/96T￥ 0.001
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Recombinant Human GALNT3/Polypeptide GalNAc transfGV-P01791-10ug￥ 1800.001
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Recombinant Human GALNT3/Polypeptide GalNAc transfGV-P01791-50ug￥ 4720.001
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Recombinant Human GALNT3/Polypeptide GalNAc transfGV-P01791-500ug￥ 13520.001
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Recombinant Human GALNT3/Polypeptide GalNAc transfGV-P01791-1mg￥ 20400.001
产品简介
| Known as | Polypeptide N-acetylgalactosaminyltransferase 3; Polypeptide GalNAc transferase 3; GalNAc-T3; pp-GaNTase 3; Protein-UDP acetylgalactosaminyltransferase 3; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3; HFTC; HHS |
| Derived from | Human Cells |
| Purity | Greater than 95% as determined by reducing SDS-PAGE. |
| Formulation | Supplied as a 0.2 μm filtered solution of 20mM PB,150mM NaCl,pH7.4. |
| Storage | Store at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening.Please minimize freeze-thaw cycles. |
| Endotoxin | Less than 0.1 ng/ug (1 EU/ug) as determined by LAL test. |
| Background | Polypeptide N-acetylgalactosaminyltransferase 3(GALNT3) belongs to the glycosyltransferase 2 family and galNAc-T subfamily. It expressed in organs that contain secretory epithelial glands and it highly expressed in pancreas, skin, kidney and testis. There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding .This protein plays a major role in regulating phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults. |
| 规格 | 10ug50ug500ug1mg |
注意：
1.本产品仅供科研使用。请勿用于医药、临床诊断或治疗，食品及化妆品等用途。请勿存放于普通住宅区。
2.为了您的安全和健康，请穿好实验服并佩戴一次性手套和口罩操作。
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