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折扣/货期| 货号：91-441 | 规格：0.05 mg | 目录价：￥7581.6 |
产品详情
* 以下信息仅供参考，详情请以原厂网站为准
产品名称:
MBL-2 Recombinant Protein
别名:
Mannose-Binding Protein C, MBP-C, Collectin-1, MBP1, Mannan-Binding Protein, Mannose-Binding Lectin, MBL2, COLEC1, MBL
表达系统:
Human Cells
保存温度:
Lyophilized protein should be stored at -20˚C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7˚C for 2-7 days.
Aliquots of reconstituted samples are stable at -20˚C for 3 months.
Reconstituted protein solution can be stored at 4-7˚C for 2-7 days.
Aliquots of reconstituted samples are stable at -20˚C for 3 months.
运输温度:
Blue Ice
产品形式:
Lyophilized
存储溶液:
Lyophilized from a 0.2 um filtered solution of 20mM PB, 150mM NaCl, 5% Threhalose, pH 7.2. It is not recommended to reconstitute to a concentration less than 100 ug/ml. Dissolve the lyophilized protein in ddH2O.
产地:
美国
生产商:
Prosci
功能与背景:
Mannose-Binding Protein C (MBP-C) belongs to the Collectin family of innate immune defense proteins. MBL binds to an array of carbohydrate patterns on pathogen surfaces. Collectin family members share common structural features: a cysteine rich amino-terminal domain, a collagen-like region, an alpha-helical coiled-coil neck domain and a carboxy terminal C-type Lectin or carbohydrate recognition domain (CRD). MBL homotrimerizes to form a structural unit joined by N-terminal disulfide bridges. These homotrimers further associates into oligomeric structures of up to 6 units. Whereas two forms of MBL proteins exist in rodents and other animals. Human MBL-2 is 25 kDa. Human MBL-2 is a secreted glycoprotein that is synthesized as a 248 amino acid (aa) precursor that contains a 20 aa signal sequence, a 21 aa cysteine-rich region, a 58 aa collagen-like segment and a 111 aa C-type lectin domain that binds to neutral bacterial carbohydrates.
纯度:
Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test.
Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test.
Accession #:
P11226
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