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SDS-PAGE

SMYD3 / ZMYND1 recombinant protein

Recombinant Human SMYD3 / ZMYND1 Protein (GST tag)

Gene Names
SMYD3; KMT3E; ZMYND1; ZNFN3A1; bA74P14.1
Purity
> 88 % as determined by SDS-PAGE
Synonyms
SMYD3 / ZMYND1; Recombinant Human SMYD3 / ZMYND1 Protein (GST tag); FLJ21080; KMT3E; MGC104324; ZMYND1; ZNFN3A1; bA74P14.1; SMYD3; SMYD3 / ZMYND1 recombinant protein
Ordering
For Research Use Only!
Host
Baculovirus-Insect Cells
Purity/Purification
> 88 % as determined by SDS-PAGE
Form/Format
Lyophilized from sterile 20mM Tris, 150mM NaCl, 0.5mM DTT, 0.5mM GSH, pH 8.0
Sequence Length
369
Application Notes
The recombinant human SMYD3/GST chimera consists of 559 amino acids and predicts a molecular mass of 656 kDa. It migrates as an approxiamtely 58 kDa band in SDS-PAGE under reducing conditions.
Predicted N Terminal
Met
Endotoxin
< 1.0 EU per mug of the protein as determined by the LAL method
Preparation and Storage
Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

SDS-PAGE
Related Product Information for SMYD3 / ZMYND1 recombinant protein
Background: SET and MYND domain-containing protein 3, also known as Zinc finger MYND domain-containing protein 1, SMYD3, and ZMYND, is a member of the histone-lysine methyltransferase family. SMYD3 contains one MYND-type zinc finger and one SET domain. SMYD3 is a histone H3 lysine-4-specific methyltransferase. It is expressed in skeletal muscles and testis. It is overexpressed in a majority of colorectal carcinoma (CRC) and hepatocellular carcinoma (HCC). SMYD3 plays an important role in transcriptional regulation in human carcinogenesis. It activates the transcription of a set of downstream genes. Of these downstream genes, there are several oncogenes and genes associated with cell adhesion (including those of N-Myc, CrkL, Wnt10b, L-selectin, CD31 and galectin-4), which have been shown to have effects on cell viability, adhesion, migration and metastasis. Increased SMYD3 expression is essential for the proliferation of breast cancer cells. SMYD3 may be a promising new target of therapeutic intervention for the treatment of cancers or other pathological processes associated with cell adhesion and migration.

Description: A DNA sequence encoding the human SMYD3 isoform 2 (NP_073580.1) (Lys 35-Ser 369) was fused with the GST tag at the N-terminus.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
42,625 Da
NCBI Official Full Name
histone-lysine N-methyltransferase SMYD3 isoform 2
NCBI Official Synonym Full Names
SET and MYND domain containing 3
NCBI Official Symbol
SMYD3
NCBI Official Synonym Symbols
KMT3E; ZMYND1; ZNFN3A1; bA74P14.1
NCBI Protein Information
histone-lysine N-methyltransferase SMYD3
UniProt Protein Name
Histone-lysine N-methyltransferase SMYD3
UniProt Gene Name
SMYD3
UniProt Synonym Gene Names
ZMYND1; ZNFN3A1

NCBI Description

This gene encodes a histone methyltransferase which functions in RNA polymerase II complexes by an interaction with a specific RNA helicase. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2011]

Uniprot Description

SMYD3: Histone methyltransferase. Specifically methylates 'Lys- 4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences. Belongs to the histone-lysine methyltransferase family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 2.1.1.43; Methyltransferase; Methyltransferase, protein lysine

Chromosomal Location of Human Ortholog: 1q44

Cellular Component: nucleoplasm

Molecular Function: histone-lysine N-methyltransferase activity

Research Articles on SMYD3 / ZMYND1

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Product Notes

The SMYD3 / ZMYND1 smyd3 (Catalog #AAA2545862) is a Recombinant Protein produced from Baculovirus-Insect Cells and is intended for research purposes only. The product is available for immediate purchase. The recombinant human SMYD3/GST chimera consists of 559 amino acids and predicts a molecular mass of 656 kDa. It migrates as an approxiamtely 58 kDa band in SDS-PAGE under reducing conditions. Researchers should empirically determine the suitability of the SMYD3 / ZMYND1 smyd3 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "SMYD3 / ZMYND1, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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