• 信息
  • 详情
  • 联系
  • 推荐
分享好友 产品首页 产品分类 切换频道
1/5
Recombinant Mouse Chemerin (aa 17-156) Protein, CF  25 UG图1

Recombinant Mouse Chemerin (aa 17-156) Protein, CF 25 UG

2024-11-24 19:03IP属地 广东省东莞市 电信00留言

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

2325-CM/CF

 

2325-CM

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.

Reconstitution Reconstitute at 100 μg/mL in sterile PBS.


Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.


Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage:       Use a manual defrost freezer and avoid repeated freeze-thaw cycles.      

  • 12 months from date of receipt, -20 to -70 °C as supplied.

  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.

  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.


Stability & Storage:       Use a manual defrost freezer and avoid repeated freeze-thaw cycles.      

  • 12 months from date of receipt, -20 to -70 °C as supplied.

  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.

  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Chemerin

Mouse Chemerin, also known as Tazarotene-induced Gene-2 (TIG2), is a new, but distant member of the cystatin superfamily (1 - 3). Members of this superfamily contain at least two intrachain disulfide bonds and an alpha -helical structure over a distance of about 100 amino acids (aa) (2, 3). Chemerin is synthesized as a 162 aa precursor that contains a hydrophobic N-terminal sequence, an intervening 140 aa cystatin-fold containing domain, and a six aa C-terminal prosegment (4 - 6). Within the cystatin-fold domain there are three intrachain disulfide bonds that contribute to the characteristic fold (4, 7). The precursor molecule is described as undergoing proteolytic processing at both termini by unknown proteases. The N-terminal 16 aa residue hydrophobic segment is described as being either a signal sequence or a transmembrane (TM) segment for a type II TM protein (5, 8). In either case it gives rise to a soluble proform that undergoes further processing at the C-terminus (5). In mouse, the C-terminal six aa residues are cleaved, giving rise to a monomeric, 16 kDa heparin-binding bioactive molecule (aa 17 - 156) (5 - 7). A shorter form has been described in human (7). The activity seems to be concentrated in the nine aa's preceding the prosegment (aa 148 - 156). Retention of the prosegment blocks activity (4). The 140 aa mature segment is known to bind to the G-protein coupled receptor termed ChemR23 (5, 7). Binding results in macrophage and immature dendritic cell chemotaxis (5). The distribution of this receptor is limited to immune APCs, and it is assumed that Chemerin is an inflammatory molecule. It is unclear which cells are actually producing Chemerin, but keratinocytes, endothelial cells and osteoclasts are potential candidates (1, 7). Mature mouse Chemerin shares 67%, 84% and 82% aa sequence identity to human, rat and hamster Chemerin, respectively (6). There is apparently cross-species activity for the protein (6).

 

举报
收藏 0
评论 0
联系方式