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Recombinant Human Transmembrane prolyl 4-hydroxylase (P4HTM), partial

Recombinant Human Transmembrane prolyl 4-hydroxylase (P4HTM), partial

Baculovirus
Mammalian cell

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Abbreviation

P4HTM

Purity

>85% (SDS-PAGE)

Target Names

P4HTM

Uniprot NO.

Q9NXG6

Species

Homo sapiens (Human)

Source

Yeast

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

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°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

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°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.

Gene References into Functions

The results suggest that SESN2 increases degradation of HIF-1A via AMPK-PHD regulation that contributes to inhibition of in vitro and in vivo tumorigenesis. PMID:27840318
This review will expand our knowledge of biology of HIFs, PHDs, PHD inhibitors, and bone regeneration, and it may also aid the design of novel therapies for accelerating bone repair and regeneration or inhibiting bone tumours. [review] PMID:24895555
Results suggest that increased expression of prolyl hydroxylase (PH) might play an role in the physiology of uterine leiomyoma during the menstrual cycle. PMID:23241241
Data suggest that PH-4 is a novel hypoxia-inducible factor-prolyl hydroxylase that may be involved in the degradation of hypoxia-inducible transcription factors under normoxia. PMID:12163023
the longest and shortest isoenzymes have major transcripts encoding inactive polypeptides, which suggest novel regulation by alternative splicing. PMID:12788921
crystal structure of the peptide-substrate-binding domain PMID:15456751
This review summarizes recent progress in elucidating the molecular mechanisms of hypoxia-inducible factor (HIF)-1 activation, focusing on the role of oxygen-dependent asparaginyl hydroxylase in hypoxia signal transduction. PMID:16154531

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Subcellular Location

Endoplasmic reticulum membrane; Single-pass type II membrane protein.

Tissue Specificity

Widely expressed with highest levels in adult pancreas, heart, skeletal muscle, brain, placenta, kidney and adrenal gland. Expressed at lower levels in epiphyseal cartilage and in fibroblasts.

Database Links

HGNC: 28858

UNIGENE: Hs.654944

KEGG: hsa:54681

STRING: 9606.ENSP00000341422

OMIM: 614584

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