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AB86916

Recombinant Human HIF1AN/FIH-1 protein (Tag Free)

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(1 Publication)

Recombinant Human HIF1AN/FIH-1 protein (Tag Free) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

FIH1, HIF1AN, Hypoxia-inducible factor 1-alpha inhibitor, Factor inhibiting HIF-1, Hypoxia-inducible factor asparagine hydroxylase, FIH-1

1 Images
SDS-PAGE - Recombinant Human HIF1AN/FIH-1 protein (Tag Free) (AB86916)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human HIF1AN/FIH-1 protein (Tag Free) (AB86916)

15% SDS-PAGE analysis of 3μg ab86916

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9NWT6

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.316% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Previously labelled as HIF1AN.

Sequence info

[{"sequence":"MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9NWT6","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

HIF1AN also known as FIH-1 (Factor Inhibiting HIF-1) is an enzyme primarily engaged in the hydroxylation of asparagine residues on hypoxia-inducible factor (HIF) alpha subunits. This action negatively regulates HIF by inhibiting its transcriptional activity. It has an approximate molecular weight of 40 kDa. HIF1AN is ubiquitously expressed in various tissues reflecting its critical role in cellular oxygen homeostasis.
Biological function summary

HIF1AN acts as an important regulator under normoxic conditions by maintaining the HIF complex in its inactive state. It does not operate alone; instead it is part of a larger protein complex that includes the HIF-alpha subunits and pVHL the latter marking HIF for degradation. This regulation ensures that the cellular response to oxygen levels is tightly controlled preventing unwarranted expression of hypoxia-related genes when oxygen is sufficient.

Pathways

The role of HIF1AN is integral in the HIF signaling and cellular response to hypoxia pathways. It is particularly associated with the modulation of the HIF pathway through its interaction with proteins such as HIF-1α and VHL. This relationship ensures a controlled activation of pathways that respond to low oxygen scenarios affecting processes like angiogenesis. The interactions between HIF1AN VHL and HIF-1α demonstrate HIF1AN's pivotal role in regulating gene expression linked to oxygen levels.

HIF1AN has connections to conditions like cancer and ischemic diseases. Its regulatory effects on HIF activity mean alterations in HIF1AN expression or function can contribute to tumor growth due to its role in promoting angiogenesis and metabolic adaptation in hypoxic tumor microenvironments. HIF1AN also has indirect links to the tumor suppressor protein VHL with mutations in VHL leading to aberrations in HIF-1α regulation further implicating HIF1AN in oncogenesis.

Specifications

Form

Liquid

Additional notes

ab86916 was purified using conventional chromatography techniques.

General info

Function

Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.

Subcellular localisation

Nucleus

Product protocols

Target data

Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.
See full target information HIF1AN

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Nature biotechnology : PubMed39663371

2024

Intestinal mucosal barrier repair and immune regulation with an AI-developed gut-restricted PHD inhibitor.

Applications

Unspecified application

Species

Unspecified reactive species

Yanyun Fu,Xiao Ding,Man Zhang,Chunlei Feng,Ziqi Yan,Feng Wang,Jianyu Xu,Xiaoxia Lin,Xiaoyu Ding,Ling Wang,Yaya Fan,Taotao Li,Yushu Yin,Xing Liang,Chenxi Xu,Shan Chen,Fadi E Pulous,David Gennert,Frank W Pun,Petrina Kamya,Feng Ren,Alex Aliper,Alex Zhavoronkov
View all publications

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