Recombinant Human AGRN protein (rFc Tag)

种属

Human

纯度

>90 %, SDS-PAGE

标签

rFc Tag

生物活性

未测试

Cat no : Eg5123

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Synonyms

Agrin, Agrin C-terminal 110 kDa subunit, Agrin C-terminal 22 kDa fragment, Agrin C-terminal 90 kDa fragment, Agrin N-terminal 110 kDa subunit



产品信息

纯度 >90 %, SDS-PAGE
内毒素 <0.1 EU/μg protein, LAL method
生物活性
Not tested
来源 HEK293-derived Human AGRN protein Ala1260-Pro2045 (Accession# O00468-6) with a rabbit IgG Fc tag at the N-terminus.
基因ID 375790
蛋白编号 O00468-6
预测分子量 109.5 kDa
SDS-PAGE 100-140 kDa, reducing (R) conditions
组分 Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
复溶 Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
储存条件
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
运输条件 The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

背景信息

Agrin, a large heparan sulfate proteoglycan, is expressed in neuronal, as well as nonneuronal tissues. Nerve-derived agrin has been demonstrated to play an essential role in development and maintenance of the neuromuscular junction. The agrin gene encodes a protein of more than 2000 amino acids with predicted molecular weight of 225 kDa but can display as 600 kDa protein due to extensive N-terminal glycosylation. Neurotrypsin cleaves the proteoglycan agrin at two homologous, highly conserved sites, liberating a middle 90-kDa and a C-terminal 22-kDa fragment from the membrane or ECM-bound N-terminal moiety of agrin.

参考文献:

1. Bezakova, Gabriela, and Markus A Ruegg. Nature reviews. Molecular cell biology vol. 4,4 (2003): 295-308. 2. Kummer, Terrance T et al. Current opinion in neurobiology vol. 16,1 (2006): 74-82. 3. Stephan, Alexander et al. FASEB journal : official publication of the Federation of American Societies for Experimental Biology vol. 22,6 (2008): 1861-73.

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