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Recombinant Human JO 1 Sf9(JO 1 Sf9)

产品编号:ENZ-335-25ug

产品描述:Recombinant Human JO 1 Sf9(JO 1 Sf9)

反应种属:

实验方法:

标记:

规格:25µg

供应商:Prospec

价格(RMB):1820.00

订购:订购

说明书:

JO 1 Human, Sf9
Histidyl-tRNA Synthetase Human Recombinant, Sf9
Catalog No. ENZ-335

Synonyms:
Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1.

Introduction:
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.

Description:
Histidyl-tRNA Synthetase Human Recombinant produced in baculovirus is a single, glycosylated, polypeptide chain having a molecular mass of 58.3 kDa.
The Histidyl-tRNA Synthetase is fused to 6x His Tag and purified by proprietary chromatographic techniques.

Source:
Sf9 Insect Cells

Physical Appearance:
Sterile Filtered clear solution.

Formulation:
The protein solution contains 20mM HEPES, 250mM sodium chloride 0.1% and 20% Glycerol, (pH 7.5).

Stability:
Lyophilized Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles.

Purity:
Greater than 90.0% as determined by SDS-PAGE.

Protein content:
Protein quantitation was carried out by using 0.25 - 2.0 mg/ml Bradford assay vs. BSA.

Western Blot:
Strongly reactive with human anti Histidyl-tRNA Synthetase antisera.

Usage:
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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