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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃.
- 保质期:
Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
- 英文名:
Recombinant Human C-X-C motif chemokine 3 (CXCL3)
- 库存:
200
- 供应商:
武汉华美生物工程有限公司
- 规格:
20μg
英文名称:
Recombinant Human C-X-C motif chemokine 3 (CXCL3)品名简称:
Recombinant Human CXCL3 protein货号:
CSB-EP006249HU规格:
20μg价格:
1344LC-MS/Western Blot:
/SDS-PAGE:
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.纯度:
Greater than 90% as determined by SDS-PAGE.内毒素:
Not test生物活性:
/基因名:
CXCL3Uniprot No.:
P19876别名:
GRO-gamma(1-73)Growth-regulated protein gamma ;GRO-gammaMacrophage inflammatory protein 2-beta ;MIP2-beta种属:
Homo sapiens (Human)蛋白长度:
Full Length of Mature Protein来源:
E.coli分子量:
11.9 kDa表达区域:
35-107aa氨基酸序列:
ASVVTELRCQCLQTLQGIHLKNIQSVNVRSPGPHCAQTEVIATLKNGKKACLNPASPMVQKIIEKILNKGSTN蛋白标签:
N-terminal 6xHis-tagged产品提供形式:
Liquid or Lyophilized powder缓冲液:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.储存条件:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.保质期:
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.货期:
13-23 business days注意事项:
Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.功能1:
Ligand for CXCR2 . Has chotactic activity for neutrophils. May play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. In vitro, the processed form GRO-gamma(5-73) shows a fivefold higher chotactic activity for neutrophilic granulocytes.1 Publication功能2:
Ligand for CXCR2 (By similarity). Has chemotactic activity for neutrophils. May play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. In vitro, the processed form GRO-gamma(5-73) shows a fivefold higher chemotactic activity for neutrophilic granulocytes.文献:
Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005)研究领域:
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文献和实验Utilizing NMR to Study the Structure of Growth-Inhibitory Proteins
for three-dimensional structure determination as well as for the structure-function analysis of proteins (1 ,2 ). Table 1 Tumor Suppressor Proteins Whose Structures Have Been Determined by NMR Spectroscopy in Solution, with Protein Data Bank Identification
resonance energy transfer (BRET) allows monitoring of protein?protein interactions in real time in living cells. One candidate interacting protein is fused to a luminescent energy donor, such as Renilla luciferase, and the other to a fluorescent energy
Proteomics and the Analysis of Proteomic Data: An Overview of Current Protein‐Profiling Technologies
Wolters, D.A., Washburn, M.P., and Yates, J.R. 3rd. 2001. An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 73:5683‐5690.
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