Rabbit Anti-HIF1A Polyclonal Antibodyy #abs130612

Rabbit Anti-HIF1A Polyclonal Antibodyy #abs130612

Please note that the given price is only for your reference. For detailed pricing information, kindly get in touch with our seller, Vecent. Data Examples Western blot analysis on LOVO using HIF1a antibody ,The lane on the left is blocked with the antigen-specific peptide. This product is for...

Description

Catalog-specification

Delivery time

USD price

abs130612-50ug

1-2 Weeks

201

abs130612-100ug

1-2 Weeks

301

Please note that the given price is only for your reference. For detailed pricing information, kindly get in touch with our seller, Vecent.


Overview

Description

Oxygen deprivation, or hypoxia, adversely affects the growth and viability of cells. In response to this condition, hypoxia-inducible factors, such as HIF-1α, Arnt 1 (also known as HIF-1β), EPAS-1 (also known as HIF-2α), and HIF-3α, are activated. These factors are part of the Per-Arnt-Sim (PAS) domain transcription factor family. Their primary role is to restore oxygen homeostasis by inducing glycolysis, erythropoiesis, and angiogenesis. By rearranging the given information, the following highly similar content is generated, while still providing accurate information from the original text.

Other names

ARNT-interacting protein, also known as HIF1-alpha or hypoxia-inducible factor 1 alpha, is a member of the PAS superfamily and a basic helix-loop-helix transcription factor. It is involved in the response to low oxygen levels, or hypoxia, and plays a critical role in regulating cellular metabolism, angiogenesis and erythropoiesis.
HIF1-alpha is also known as a member of PAS protein 1, MOP1 and PASD8. Its structure is composed of two subunits, the alpha and beta subunits. While the beta subunit is stable under all conditions, the alpha subunit is constantly degraded under normoxic conditions, or conditions with sufficient oxygen.
Under hypoxic conditions, HIF1-alpha is stabilized and forms a heterodimer with the beta subunit to activate target genes involved in hypoxia response. It is also involved in the regulation of key cellular processes such as glucose metabolism, apoptosis and cell differentiation.
Overall, ARNT-interacting protein or HIF1-alpha is an important player in the response to hypoxia, and understanding its regulatory mechanisms may provide potential targets for therapeutic interventions in hypoxia-related diseases such as cancer and ischemic diseases.

Source

Rabbit

Specificity

HIF1a antibody detects endogenous levels of HIF1a.

ReactivityHuman;Mouse;Rat

Species Reactivity

Pig;Rabbit;Bovine;Horse;

AntigenHIF1A

Application

The recommended dilutions for using this antibody in various applications are WB 1:500-1:2000, IHC 1:50-1:200, IF 1:200, and ELISA(peptide) 1:20000-1:40000. It is important to note that these dilutions may need to be altered based on factors such as sample type and experimental conditions. We suggest starting with the recommended dilutions and then adjusting as needed. It is also important to ensure that proper controls are included in each experiment to ensure accurate and reliable results. Overall, this antibody is a valuable tool for researchers in a variety of fields and applications.

Immunogen

A synthesized peptide derived from human HIF1a.

Properties

MW120kDa

Concentration

1mg/ml


Purification

Using SulfoLink™ Coupling Resin, the antiserum underwent purification through peptide affinity chromatography. An effective method for isolating the desired molecules, this process yielded a highly purified product.

Clonality

Polyclonal Antibody

Stability & Storage

To ensure optimal storage, it is recommended to store the product at a temperature of -20 °C for a duration of one year. It is important to prevent any repeated freeze/thaw cycles, as they can affect the product's quality.


Storage buffer

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 15 months from date of receipt.

Target

Background

 Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.

Tissue specificity

Expressed in most tissues with highest levels in kidney and heart. Overexpressed in the majority of common human cancers and their metastases, due to the presence of intratumoral hypoxia and as a result of mutations in genes encoding oncoproteins and tumor suppressors. A higher level expression seen in pituitary tumors as compared to the pituitary gland.

Posttranslational modificationS-nitrosylation of Cys-800 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex.Requires phosphorylation for DNA-binding. Phosphorylation at Ser-247 by CSNK1D/CK1 represses kinase activity and impairs ARNT binding. Phosphorylation by GSK3-beta and PLK3 promote degradation by the proteasome.Sumoylated; with SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Both sumoylation and desumoylation seem to be involved in the regulation of its stability during hypoxia. Sumoylation can promote either its stabilization or its VHL-dependent degradation by promoting hydroxyproline-independent HIF1A-VHL complex binding, thus leading to HIF1A ubiquitination and proteasomal degradation. Desumoylation by SENP1 increases its stability amd transcriptional activity. There is a disaccord between various publications on the effect of sumoylation and desumoylation on its stability and transcriptional activity.Acetylation of Lys-532 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation (PubMed:12464182). Deacetylation of Lys-709 by SIRT2 increases its interaction with and hydroxylation by EGLN1 thereby inactivating HIF1A activity by inducing its proteasomal degradation (PubMed:24681946).Polyubiquitinated; in normoxia, following hydroxylation and interaction with VHL. Lys-532 appears to be the principal site of ubiquitination. Clioquinol, the Cu/Zn-chelator, inhibits ubiquitination through preventing hydroxylation at Asn-803. Ubiquitinated by a CUL2-based E3 ligase.In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and EGLN2/PHD1 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). EGLN3/PHD3 has also been shown to hydroxylate Pro-564 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Deubiquitinated by USP20 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). In normoxia, is hydroxylated on Asn-803 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation (PubMed:12080085). This hydroxylation is inhibited by the Cu/Zn-chelator, Clioquinol (PubMed:12080085). Repressed by iron ion, via Fe2+ prolyl hydroxylase (PHD) enzymes-mediated hydroxylation and subsequent proteasomal degradation (PubMed:28296633).The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.

Celluar localization

Cytosol;Nucleus;

UniPort

Q16665


Data Examples

Western blot analysis on LOVO using HIF1a antibody ,The lane on the left is blocked with the antigen-specific peptide.


This product is for research use only, not for use in diagnostic prodecures or in human.


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