Recombinant Human Prolyl 4-hydroxylase subunit alpha-1 (P4HA1)

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Code CSB-EP017339HU
MSDS
Size US$306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP017339HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) P4HA1.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP017339HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) P4HA1.
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Product Details

Purity
Greater than 85% as determined by SDS-PAGE.
Target Names
P4HA1
Uniprot No.
Research Area
Signal Transduction
Alternative Names
2-oxoglutarate-4-dioxygenase subunit alpha-1; 4-hydroxylase, alpha I subunit; 4-PH alpha-1; P4HA; P4HA1; P4HA1_HUMAN; Procollagen-proline; Procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide I; Prolyl 4-hydroxylase subunit alpha-1
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
18-534aa
Target Protein Sequence
HPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELETAGINFRMATIN
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
64.4 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

The recombinant Human P4HA1 was expressed with the amino acid range of 18-534. The calculated molecular weight for this P4HA1 protein is 63.1 kDa. This protein is generated in a e.coli-based system. The P4HA1 coding gene included the N-terminal 6xHis tag, which simplifies the detection and purification processes of the recombinant P4HA1 protein in following stages of expression and purification.

The human prolyl 4-hydroxylase subunit alpha-1 (P4HA1) is a key component of the prolyl 4-hydroxylase enzyme complex, which plays a critical role in the post-translational modification of collagen. P4HA1 specifically catalyzes the hydroxylation of proline residues in collagen, contributing to the stability and structure of this essential extracellular matrix protein. This enzymatic modification is crucial for collagen's proper folding and function. Collagen, in turn, is a major structural protein in connective tissues, providing strength and support to various tissues and organs in the body. Research on P4HA1 often delves into understanding collagen biosynthesis, tissue development, and the role of collagen in health and diseases, including fibrosis and cancer. Additionally, investigations may explore therapeutic strategies targeting collagen-related disorders by modulating P4HA1 activity.

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Target Background

Function
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Gene References into Functions
  1. miR-122 inhibited migration, invasion, epithelial mesenchymal transition, and metastasis in peritoneal cavity of ovarian cancer cells by targeting P4HA1. PMID: 30136751
  2. High expression of P4HA1 was correlated with the malignancy of gliomas and could serve as a prognostic indicator for patients with high-grade gliomas PMID: 28964577
  3. Our study indicates that P4HA1 plays a pivotal role in the process of GSC-EC transdifferentiation and the structural formation of vascular BMs. PMID: 28415787
  4. we report compound heterozygous frameshift and splice site mutations in P4HA1 that impair but not abolish C-P4H alpha(I) activity. The maternal P4HA1 exon 12 splice donor site mutation causes an internally deleted C-P4H alpha(I) predicted to completely lack catalytic activity. two nucleic acid insertion in exon 9 results in a premature stop in the exon 9 P4HA1 splice form. PMID: 28419360
  5. Findings suggest that the catalytic domain of collagen prolyl 4-hydroxylases (CP4Hs) recognizes the cis conformation of the prolyl peptide bond. PMID: 28001367
  6. Thus, we conclude that miR-30e suppresses proliferation of hepatoma cells through targeting P4HA1 mRNA. PMID: 26966067
  7. Studies indicate P4HA1 copy number gain in a subset of metastatic prostate tumors and its expression is also regulated by microRNA-124. PMID: 25115393
  8. Overexpression of miR-122 markedly attenuated the expression of P4HA1 via targeting a binding site located at 3'-UTR of P4HA1 mRNA PMID: 23178710
  9. Hypoxia-inducible factor 1 (HIF-1) promotes extracellular matrix remodeling under hypoxic conditions by inducing P4HA1, P4HA2, and PLOD2 expression in fibroblasts. PMID: 23423382
  10. IL-6 significantly downregulated P4Halpha1 expression in aortic smooth muscle cells PMID: 23022409
  11. analysis of the 2-His-1-Asp active-site motif in prolyl 4-hydroxylase PMID: 19890397
  12. These in vivo data demonstrated that smokers had thinner atherosclerotic cap thickness and lower levels of P4Halpha and collagen. PMID: 15369792
  13. Collagen prolyl 4-hydroxylase-alpha (I)mRNA is stabilized by interation of RNA-binding proteins hnRNP-A2/B1 with a U(16) element within the 3'-UTR PMID: 16464861
  14. positive (transforming growth factor beta1) and negative (cigarette smoking extract) regulators appear to influence the USF-E-box interaction and affect P4Halpha(I) expression PMID: 16488890
  15. Results suggest that the alteration of translational efficiency by nucleolin, which occurs through a hypoxia inducible factor independent pathway, is an important step in collagen prolyl 4-hydroxylase-alpha(I) regulation under hypoxia. PMID: 16837461
  16. In comparison with healthy cartilage, Osteoarthritis articular chondrocytes exhibit increased in vivo synthesis of collagen prolyl-4-hydroxylase type II, a pivotal enzyme in collagen triple helix formation. PMID: 16877351
  17. HIF-P4H, HIF-1alpha and HIF-2alpha are effective oxygen sensors PMID: 16885164

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Subcellular Location
Endoplasmic reticulum lumen.
Protein Families
P4HA family
Database Links

HGNC: 8546

OMIM: 176710

KEGG: hsa:5033

STRING: 9606.ENSP00000263556

UniGene: Hs.500047

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