HIF1A Human (85 a.a.)

Hypoxia-Inducible Factor-1 Alpha (85 a.a.) Human Recombinant
Cat. No.
BT22587
Source
Escherichia Coli.
Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 80.0% 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

HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-85 a.a.) and having a molecular mass of 11.8 kDa. The HIF1A is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
HIF1A acts as a crucial transcriptional regulator of the cellular response to low oxygen levels (hypoxia). In hypoxic conditions, HIF1A activates the expression of over 40 genes, including those involved in red blood cell production (erythropoietin), glucose uptake and utilization (glucose transporters and glycolytic enzymes), blood vessel formation (vascular endothelial growth factor), and other genes that enhance oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF1A plays a critical role in embryonic blood vessel development, tumor growth and spread (angiogenesis), and the progression of diseases caused by insufficient blood supply (ischemic disease).
Description
Recombinant Human HIF1A, produced in E. coli, is a single polypeptide chain without any attached sugar molecules (non-glycosylated). It comprises 105 amino acids, including amino acids 1 to 85 of the native HIF1A sequence, and has a molecular weight of 11.8 kDa. The HIF1A protein is tagged with a 20 amino acid His-Tag at the N-terminus to facilitate purification, which is performed using proprietary chromatographic techniques.
Physical Appearance
A clear and colorless solution that has been sterilized by filtration.
Formulation
The HIF1A Human solution has a concentration of 0.25 mg/ml and is supplied in a buffer containing 20mM Tris (pH 8.0), 20% glycerol, 1mM DTT, 0.2M NaCl, and 1mM EDTA.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To further enhance stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advised. Avoid repeated freezing and thawing of the product.
Purity
The purity of the HIF1A protein is greater than 80%, as assessed by SDS-PAGE analysis.
Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM RLTISYLRVR KLLDAGDLDI EDDMK.

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). The human recombinant form of HIF-1α, specifically the 85 amino acid (a.a.) variant, is a truncated version of the full-length protein, designed for research and therapeutic purposes.

Structure and Function

HIF-1α is a subunit of the heterodimeric transcription factor Hypoxia-Inducible Factor-1 (HIF-1), which also includes the beta subunit, known as the Aryl Hydrocarbon Receptor Nuclear Translocator (ARNT). The HIF-1 complex is essential for the regulation of genes involved in various physiological processes, including angiogenesis, metabolism, and cell survival under hypoxic conditions .

The 85 a.a. variant of HIF-1α retains the critical domains necessary for its function, including the basic helix-loop-helix (bHLH) domain and the Per-ARNT-Sim (PAS) domain. These domains are responsible for DNA binding and dimerization with ARNT, respectively .

Biological Significance

HIF-1α is considered the master regulator of the cellular response to hypoxia. Under normal oxygen levels, HIF-1α is rapidly degraded by the proteasome. However, under hypoxic conditions, HIF-1α is stabilized and translocates to the nucleus, where it dimerizes with ARNT and binds to hypoxia-responsive elements (HREs) in the promoter regions of target genes .

The activation of HIF-1α leads to the transcription of various genes involved in:

  • Angiogenesis: Promoting the formation of new blood vessels through the upregulation of vascular endothelial growth factor (VEGF).
  • Metabolism: Enhancing glycolysis and glucose uptake by increasing the expression of glycolytic enzymes and glucose transporters.
  • Cell Survival: Inducing the expression of anti-apoptotic proteins and reducing oxidative stress .
Clinical Implications

The dysregulation of HIF-1α has been implicated in several pathophysiological conditions, including cancer, cardiovascular diseases, and chronic kidney disease. Overexpression of HIF-1α is commonly observed in tumors, where it promotes angiogenesis and metabolic adaptation, contributing to tumor growth and survival .

In addition to its role in cancer, HIF-1α is also involved in the response to ischemic conditions, such as myocardial infarction and stroke. Therapeutic strategies targeting HIF-1α are being explored to enhance tissue repair and regeneration in these conditions .

Research Applications

The human recombinant HIF-1α (85 a.a.) is widely used in research to study the molecular mechanisms of hypoxia response and to develop potential therapeutic interventions. It serves as a valuable tool for investigating the regulation of HIF-1α and its downstream targets, as well as for screening potential HIF-1α inhibitors .

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