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SDS-PAGE

PHPT1 / PHP14 recombinant protein

Recombinant Human PHPT1 / PHP14 Protein (His tag)

Gene Names
PHPT1; PHP; PHP14; CGI-202; HSPC141; HEL-S-132P
Purity
> 97 % as determined by SDS-PAGE
Synonyms
PHPT1 / PHP14; Recombinant Human PHPT1 / PHP14 Protein (His tag); PHPT1; PHP14; PHPT1 / PHP14 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
> 97 % as determined by SDS-PAGE
Form/Format
Lyophilized from sterile PBS, pH 7.4
Sequence Length
124
Application Notes
The recombinant human PHPT1 consisting of 135 amino acids and has a calculated molecular mass of 15.2 kDa as estimated in SDS-PAGE under reducing conditions.
Predicted N Terminal
Met
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 PHPT1 / PHP14 recombinant protein
Background: PHPT1, also known as 14 kDa phosphohistidine phosphatase, phosphohistidine phosphatase 1, protein janus-A homolog, PHP14, is a cytoplasm protein which belongs to the janus family. PHPT1 / PHP14 is expressed abundantly in heart and skeletal muscle. Phosphatases are a diverse group of enzymes that regulate numerous cellular processes. Much of what is known relates to the tyrosine, threonine, and serine phosphatases, whereas the histidine phosphatases have not been studied as much. Protein histidine phosphorylation exists widely in vertebrates, and it plays important roles in signal transduction and other cellular functions. Protein histidine phosphorylation accounts for about 6% of the total protein phosphorylation in eukaryotic cells. The knowledge about eukaryotic PHPT (protein histidine phosphatase) is still very limited. To date, only one vertebrate PHPT has been discovered, and two crystal structures of human PHPT1 have been solved. PHPT1 / PHP14 can dephosphorylate a variety of proteins (e.g. ATP-citrate lyase and the beta-subunit of G proteins). A putative active site has been identified by its electrostatic character, ion binding, and conserved protein residues.

Description: A DNA sequence encoding the human PHPT1 (Q9NRX4-1) (Ala 2-Tyr 125) was expressed, with a polyhistidine tag at the N-terminus.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
13,672 Da
NCBI Official Full Name
14 kDa phosphohistidine phosphatase isoform 2
NCBI Official Synonym Full Names
phosphohistidine phosphatase 1
NCBI Official Symbol
PHPT1
NCBI Official Synonym Symbols
PHP; PHP14; CGI-202; HSPC141; HEL-S-132P
NCBI Protein Information
14 kDa phosphohistidine phosphatase
UniProt Protein Name
14 kDa phosphohistidine phosphatase
UniProt Gene Name
PHPT1
UniProt Synonym Gene Names
PHP14; PHP

NCBI Description

This gene encodes an enzyme that catalyzes the reversible dephosphorylation of histidine residues in proteins. It may be involved in the dephosphorylation of G-beta and ATP citrate lyase and in negatively regulating CD4 T lymphocytes by dephosphorylation and inhibition of KCa3.1 channels. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2013]

Uniprot Description

PHPT1: a phosphohistidine phosphatase. Present preferentially in heart and skeletal muscle. Insensitive to inhibition by okadaic acid and EDTA.

Protein type: Carbohydrate Metabolism - fructose and mannose; Cofactor and Vitamin Metabolism - riboflavin; Cofactor and Vitamin Metabolism - thiamine; EC 3.1.3.-; Motility/polarity/chemotaxis; Phosphatase

Chromosomal Location of Human Ortholog: 9q34.3

Cellular Component: cytosol

Molecular Function: calcium channel inhibitor activity; phosphohistidine phosphatase activity

Biological Process: negative regulation of lyase activity; negative regulation of T cell receptor signaling pathway; protein amino acid dephosphorylation

Research Articles on PHPT1 / PHP14

Similar Products

Product Notes

The PHPT1 / PHP14 phpt1 (Catalog #AAA2545502) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The recombinant human PHPT1 consisting of 135 amino acids and has a calculated molecular mass of 15.2 kDa as estimated in SDS-PAGE under reducing conditions. Researchers should empirically determine the suitability of the PHPT1 / PHP14 phpt1 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 "PHPT1 / PHP14, 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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