- ￥3290
- Abbiotec
- 美国
- 600273
- 2026年01月01日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
保存于-192℃
- 保质期：
一年
- 英文名：
Human L-Selectin
- 库存：
一定量库存
- 供应商：
美国ABBIOTEC公司
- 规格：
0.01 mg
L-Selectin belongs to a family of divalent cation dependent carbohydrate-binding glycoproteins or adhesion molecules. L-Selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin is shed by proteolytic cleavage and circulating levels in biological fluids are used as an indicator of various pathological conditions. Recombinant human L-selectin comprises a 294 amino acid fragment (39-332) corresponding to the mature L-Selectin extracellular domain and is expressed in E. coli with an amino-terminal hexahistidine tag.
形 态 ：
Each vial contains 0.01 mg protein (liquid) in PBS pH7.4, 50% glycerol. Final concentration 0.1-1 mg/ml.
来 源 ：
E. coli
别 名 ：
L-Selectin; Leukocyte Selectin; L-SEL; Leukocyte adhesion molecule; LAM-1; Leukocyte cell adhesion molecule LECAM-1; TQ1; CD62L; Leukocyte surface antigen Leu-8; DREG; lymph node homing receptor LNHR; MEL-14
纯 度 ：
Purity > 95% as determined by reducing and non-reducing SDS-PAGE, Bradford assay, Western blot and ELISA.
分子量 ：
37.55 kDa
应 用 ：E, WB
保存条件 ：
Store at -20°C. Product is guaranteed one year from the date of shipment.
产品链接 ：http://www.abbiotec.com/proteins/human-l-selectin
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文献和实验L-selectin-PNAd Interactions under Flow Conditions.
lower wall or expressed on a cell monolayer. The present protocol will focus on the interactions between L-selectin expressed on neutrophils and PNAd coated onto the plastic surface. For neutrophil purification see Purification of human
Purification of Human Complement Protein C5
Complement C5 is cleaved by proteolysis in the terminal phase of complement activation generating the pro-inflammatory C5a and membrane attack complex nucleator C5b. Whereas purification of its paralogues C3 and C4 from plasma is relatively
Analysis of Protein Phosphorylation in Human Neutrophils
, serines and threonines. Upon covalent binding of phosphates to these amino acids, the charge and conformation of the corresponding proteins are modified, generally leading to changes in protein functions such as protein-protein interactions and enzymatic
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