Recombinant Human Seryl tRNA synthetase His Protein

Novus Biologicals | Catalog # NBP1-78856

Novus Biologicals
Loading...

Key Product Details

Source

E. coli

Tag

His

Applications

SDS-PAGE
Loading...

Product Specifications

Description

A recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 1-514 of Human Seryl tRNA synthetase

Source: E.coli

Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MGSMVLDLDL FRVDKGGDPA LIRETQEKRF KDPGLVDQLV KADSEWRRCR FRADNLNKLK NLCSKTIGEK MKKKEPVGDD ESVPENVLSF DDLTADALAN LKVSQIKKVR LLIDEAILKC DAERIKLEAE RFENLREIGN LLHPSVPISN DEDVDNKVER IWGDCTVRKK YSHVDLVVMV DGFEGEKGAV VAGSRGYFLK GVLVFLEQAL IQYALRTLGS RGYIPIYTPF FMRKEVMQEV AQLSQFDEEL YKVIGKGSEK SDDNSYDEKY LIATSEQPIA ALHRDEWLRP EDLPIKYAGL STCFRQEVGS HGRDTRGIFR VHQFEKIEQF VYSSPHDNKS WEMFEEMITT AEEFYQSLGI PYHIVNIVSG SLNHAASKKL DLEAWFPGSG AFRELVSCSN CTDYQARRLR IRYGQTKKMM DKVEFVHMLN ATMCATTRTI CAILENYQTE KGITVPEKLK EFMPPGLQEL IPFVKPAPIE QEPSKKQKKQ HEGSKKKAAA RDVTLENRLQ NMEVTDA

Purity

>95%, by SDS-PAGE

Predicted Molecular Mass

61.2 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Protein / Peptide Type

Recombinant Protein

Scientific Data Images for Recombinant Human Seryl tRNA synthetase His Protein

SDS-PAGE: Recombinant Human Seryl tRNA synthetase His Protein [NBP1-78856]

SDS-PAGE: Recombinant Human Seryl tRNA synthetase His Protein [NBP1-78856]

SDS-Page: Recombinant Human Seryl tRNA synthetase Protein [NBP1-78856] - 15% SDS-PAGE (3ug)

Formulation, Preparation, and Storage

NBP1-78856
Formulation 20 mM Tris-HCl buffer (pH 8.0), 1 mM DTT, 10% glycerol, 100 mM NaCl
Preservative No Preservative
Concentration 0.5 mg/ml
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.

Background: Seryl tRNA synthetase

SARS (Seryl-tRNA synthetase, cytoplasmic) belongs to the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases function to catalyze the aminoacylation of tRNAs by their corresponding amino acids, thus linking amino acids with tRNA-contained nucleotide triplets. This enzyme catalyzes the attachment of serine to tRNA(Ser). It is probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). Recombinant human SARS protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.

Alternate Names

EC 6.1.1.11, FLJ36399, serine-tRNA ligase, Serine--tRNA ligase, SerRS, SERSserine tRNA ligase 1, cytoplasmic, Seryl-tRNA Ser/Sec synthetase, seryl-tRNA synthetase, seryl-tRNA synthetase, cytoplasmic, Seryl-tRNA(Ser/Sec) synthetase

Gene Symbol

SARS1

Additional Seryl tRNA synthetase Products

Product Documents for Recombinant Human Seryl tRNA synthetase His Protein

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot or batch number in the search box below.

Product Specific Notices for Recombinant Human Seryl tRNA synthetase His Protein

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

Customer Reviews for Recombinant Human Seryl tRNA synthetase His Protein

There are currently no reviews for this product. Be the first to review Recombinant Human Seryl tRNA synthetase His Protein and earn rewards!

Have you used Recombinant Human Seryl tRNA synthetase His Protein?

Submit a review and receive an Amazon gift card!

$25/€18/£15/$25CAN/¥2500 Yen for a review with an image

$10/€7/£6/$10CAN/¥1110 Yen for a review without an image

Submit a review
Amazon Gift Card

FAQs

No product specific FAQs exist for this product.

View all FAQs for Proteins and Enzymes
Loading...