HIF1A Human
Greater than 90.0% as determined by SDS-PAGE.
Description
HIF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (530-826) and having a molecular mass of 32.8kDa. The protein migrates as a 32.8kDa band on SDS-PAGE. The HIF1-A is purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Hypoxia-Inducible Factor-1 Alpha (HIF-1α) is a crucial transcription factor that plays a significant role in the cellular response to low oxygen levels (hypoxia). It is a subunit of the heterodimeric transcription factor Hypoxia-Inducible Factor-1 (HIF-1), which is composed of HIF-1α and the aryl hydrocarbon receptor nuclear translocator (ARNT), also known as HIF-1β .
HIF-1α is a basic helix-loop-helix (bHLH) PAS domain-containing protein. It consists of several functional domains, including:
- bHLH domain: Involved in DNA binding and dimerization.
- PAS domains: Important for dimerization with HIF-1β.
- Nuclear localization signal: Directs the protein to the nucleus.
- Transactivation domains (CTAD and NTAD): Essential for transcriptional activation.
- Inhibitory domain (ID): Represses the transcriptional activities of CTAD and NTAD .
There are three known isoforms of HIF-1α, formed by alternative splicing. Isoform 1 is the most extensively studied and is considered the canonical structure .
HIF-1α is the master regulator of the cellular and developmental response to hypoxia. It activates the transcription of various genes involved in:
- Energy metabolism: Enhances glycolysis and reduces mitochondrial oxygen consumption.
- Angiogenesis: Promotes the formation of new blood vessels by upregulating vascular endothelial growth factor (VEGF).
- Cell survival: Induces the expression of genes that help cells survive under low oxygen conditions.
- Tumor invasion: Facilitates cancer cell adaptation and invasion in hypoxic tumor microenvironments .
The expression of HIF-1α is tightly regulated by oxygen levels. Under normoxic conditions (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 HIF-1β and activates target gene transcription .
Dysregulation and overexpression of HIF-1α are implicated in various pathophysiological conditions, including:
- Cancer: HIF-1α promotes tumor growth and metastasis by enhancing angiogenesis and metabolic adaptation.
- Ischemic diseases: HIF-1α plays a protective role in conditions such as stroke and myocardial infarction by promoting cell survival and tissue repair.
- Placental development: HIF-1α is essential for normal placental development during early gestation .
Recombinant human HIF-1α is produced using recombinant DNA technology, which involves inserting the HIF1A gene into an expression vector and introducing it into a host cell (e.g., E. coli or mammalian cells) to produce the protein. This recombinant protein is used in various research applications to study its structure, function, and role in disease .
