HIF1AN Human

Hypoxia-Inducible Factor-1 Alpha Inhibitor Human Recombinant
Cat. No.
BT22770
Source
Escherichia Coli.
Synonyms
FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

HIF1AN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-349) and having a molecular mass of 40.2kDa.

The HIF1AN is purified by proprietary chromatographic techniques.

Product Specs

Introduction
HIF1AN, a key regulator of the hypoxia-inducible factor (HIF) pathway, plays a crucial role in tumor development and progression. Overexpression of HIF1AN is associated with increased tumor aggressiveness in pancreatic endocrine tumors. HIF1AN hydroxylates Notch ICD at specific residues essential for its function as a transactivator in cellular processes, including neurogenesis and myogenesis. Furthermore, HIF1AN is commonly found in invasive breast carcinoma, and its role in the hypoxic response and survival suggests that tumor regulation of HIF1AN is a critical mechanism for HIF pathway activation. As an asparaginyl hydroxylase enzyme, HIF1AN regulates the transcriptional activity of HIF. Belonging to the Fe2+ and 2-oxoglutarate-dependent dioxygenase superfamily, HIF1AN hydroxylates a specific asparagine residue (Asn-803) within the HIF1A C-terminal transactivation domain. Under normal oxygen conditions (normoxia), HIF1AN-mediated hydroxylation of the HIF1α transactivation domain blocks the interaction between HIF1A and p300/CBP, thereby suppressing the transcriptional activity of HIF1A target genes.
Description
Recombinant human HIF1AN, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 349 amino acids (1-349) with a molecular weight of 40.2 kDa. The purification process utilizes proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The protein solution is provided at a concentration of 1 mg/ml in a buffer containing 20mM Tris-HCl at pH 8.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.
Source
Escherichia Coli.
Amino Acid Sequence
MAATAAEAVA SGSGEPREEA GALGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMAN FQNFKPRSNR EEMKFHEFVE KLQDIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGYKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE RFPNFQNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN.

Product Science Overview

Introduction

Hypoxia-Inducible Factor-1 Alpha (HIF-1α) is a crucial transcription factor that plays a significant role in cellular response to low oxygen levels (hypoxia). It is a subunit of the heterodimeric transcription factor HIF-1, which is composed of HIF-1α and the aryl hydrocarbon receptor nuclear translocator (ARNT or HIF-1β). HIF-1α is encoded by the HIF1A gene and is considered the master regulator of the cellular and developmental response to hypoxia .

Structure and Function

HIF-1α contains several important domains, including a basic helix-loop-helix (bHLH) domain, two Per-ARNT-Sim (PAS) domains, and a C-terminal transactivation domain (CTAD). These domains are essential for its stability, dimerization with HIF-1β, and transcriptional activity . Under normoxic conditions, HIF-1α is rapidly degraded via the ubiquitin-proteasome pathway. However, under hypoxic conditions, HIF-1α is stabilized, translocates to the nucleus, dimerizes with HIF-1β, and activates the transcription of various genes involved in angiogenesis, metabolism, and cell survival .

Role in Disease

HIF-1α is overexpressed in many human cancers and is heavily implicated in promoting tumor growth and metastasis through its role in initiating angiogenesis and regulating cellular metabolism to overcome hypoxia . Additionally, HIF-1α plays a role in other pathophysiologies, including chronic obstructive pulmonary disease (COPD) and sepsis .

Hypoxia-Inducible Factor-1 Alpha Inhibitor (Human Recombinant)

The development of HIF-1α inhibitors, including human recombinant versions, aims to target the dysregulated HIF-1α pathway in various diseases. These inhibitors can potentially suppress tumor growth and metastasis by inhibiting HIF-1α’s ability to activate hypoxia-responsive genes. The therapeutic potential of HIF-1α inhibitors is being explored in preclinical and clinical studies for cancer and other hypoxia-related diseases .

Mechanism of Action

HIF-1α inhibitors work by preventing the stabilization and activity of HIF-1α under hypoxic conditions. This can be achieved through various mechanisms, such as promoting the degradation of HIF-1α, inhibiting its dimerization with HIF-1β, or blocking its transcriptional activity. By targeting HIF-1α, these inhibitors aim to disrupt the hypoxia-induced signaling pathways that contribute to disease progression .

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