Mouse Serum Amyloid A-3 (SAA-3) Microtiter Plate

Species Reactivity	Key Applications	Host	Format	Antibody Type
H, R	WB, ICC, IH(P)	Rb	Unpurified	Monoclonal Antibody

Species Reactivity

Key Applications

Host

Format

Antibody Type

H, R

WB, ICC, IH(P)

Unpurified

Monoclonal Antibody

Description
Catalogue Number	04-1006
Description	Anti-HIF-1α Antibody, clone EP1215Y, rabbit monoclonal
Alternate Names	ARNT interacting protein ARNT-interacting protein Basic-helix-loop-helix-PAS protein MOP1 HIF-1 alpha HIF1 alpha, member of PAS protein 1 hypoxia inducible factor 1
Background Information	Hypoxia, a condition of low tissue O2 concentration, plays an important role in normal physiological processes and tumor formation. Under hypoxic conditions mammalian cells up regulate the expression of hypoxic genes, including induction of angiogenesis and a switch to anaerobic metabolism, in order to survive. HIF-1 (Hypoxia Inducible Factor-1) is one of the key regulators of the transcriptional response to oxygen deprivation (1). HIF-1 is composed of two subunits, HIF-1αand HIF-1β also known as aryl hydrocarbon receptor nuclear translocator (ARNT)) that are members of the basic helix-loop-helix (bHLH) Per-Arnt-Sim (PAS) (bHLH-PAS) family of transcription factors. HIF-1 is essential for angiogenesis, embryonic development, and is associated with tumor progression, erythropoiesis, vascular development/remodeling, vasodilation, and glucose/energy metabolism. The over expression of HIF-1αhas been demonstrated in many common human cancers including prostate and breast, in which HIF-1α levels are associated with increase vascularitry and tumor progression. Besides physiological hypoxia, genetic abnormalities frequently detected in human cancers, such as loss of function mutations (Von Hippel-Lindau, p53, and PTEN), are associated with induction of HIF1 activity and expression of HIF-1-inducible genes (1).

Description

Catalogue Number

04-1006

Description

Anti-HIF-1α Antibody, clone EP1215Y, rabbit monoclonal

Alternate Names

ARNT interacting protein
ARNT-interacting protein
Basic-helix-loop-helix-PAS protein MOP1
HIF-1 alpha
HIF1 alpha, member of PAS protein 1
hypoxia inducible factor 1

Background Information

Hypoxia, a condition of low tissue O2 concentration, plays an important role in normal physiological processes and tumor formation. Under hypoxic conditions mammalian cells up regulate the expression of hypoxic genes, including induction of angiogenesis and a switch to anaerobic metabolism, in order to survive. HIF-1 (Hypoxia Inducible Factor-1) is one of the key regulators of the transcriptional response to oxygen deprivation (1). HIF-1 is composed of two subunits, HIF-1αand HIF-1β also known as aryl hydrocarbon receptor nuclear translocator (ARNT)) that are members of the basic helix-loop-helix (bHLH) Per-Arnt-Sim (PAS) (bHLH-PAS) family of transcription factors. HIF-1 is essential for angiogenesis, embryonic development, and is associated with tumor progression, erythropoiesis, vascular development/remodeling, vasodilation, and glucose/energy metabolism. The over expression of HIF-1αhas been demonstrated in many common human cancers including prostate and breast, in which HIF-1α levels are associated with increase vascularitry and tumor progression. Besides physiological hypoxia, genetic abnormalities frequently detected in human cancers, such as loss of function mutations (Von Hippel-Lindau, p53, and PTEN), are associated with induction of HIF1 activity and expression of HIF-1-inducible genes (1).

Product Information
Format	Unpurified
Control	Ramos + CoCl2 lysate
Presentation	Rabbit Monoclonal in buffer containing 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl containing 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Product Information

Format

Unpurified

Control

Ramos + CoCl2 lysate

Presentation

Rabbit Monoclonal in buffer containing 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl containing 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Applications
Application	Please note that this product will not be available for sale after March 15, 2015. Please select one of the other antibodies against this target.
Key Applications	Western Blotting Immunocytochemistry Immunohistochemistry (Paraffin)
Application Notes	Immunohistochemistry Analysis: A 1:100-250 dilution from a previous lot detected HIF-1α in human liver carcinoma tissue. Immunocytochemistry Analysis: A 1:100-250 dilution from a previous lot was used in IC.

Applications

Application

Please note that this product will not be available for sale after March 15, 2015. Please select one of the other antibodies against this target.

Key Applications

Western Blotting
Immunocytochemistry
Immunohistochemistry (Paraffin)

Application Notes

Immunohistochemistry Analysis: A 1:100-250 dilution from a previous lot detected HIF-1α in human liver carcinoma tissue.
Immunocytochemistry Analysis: A 1:100-250 dilution from a previous lot was used in IC.

Biological Information
Immunogen	Synthetic peptide corresponding to residues near the C-terminus of human HIF-1α.
Epitope	C-terminus
Clone	EP1215Y
Host	Rabbit
Specificity	This antibody recognizes HIF-1α at and around the C-terminus.
Isotype	IgG
Species Reactivity	Human Rat
Antibody Type	Monoclonal Antibody
Entrez Gene Number	NM_001530.2
Gene Symbol	HIF-1alpha HIF1 HIF1-ALPHA MOP1 PASD8 bHLHe78
Purification Method	Unpurified
UniProt Number	Q16665
UniProt Summary	FUNCTION: 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, 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 CREBPB 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. SUBUNIT STRUCTURE: Interacts with the HIF1A beta/ARNT subunit; heterodimerization is required for DNA binding. Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability By similarity. Interacts with CREBBP and EP300 (via TAZ-type 1 domains). Interacts with NCOA1, NCOA2, APEX and HSP90. Interacts (hydroxylated within the ODD domain) with VHLL (via beta domain); the interaction, leads to polyubiquitination and subsequent HIF1A proteasomal degradation. During hypoxia, sumoylated HIF1A also binds VHL; the interaction promotes the ubiquitination of HIF1A. Interacts with SENP1; the interaction desumoylates HIF1A resulting in stabilization and activation of transcription. Interacts (Via the ODD domain) with ARD1A; the interaction appears not to acetylate HIF1A nor have any affect on protein stability, during hypoxia. Interacts with RWDD3; the interaction enhances HIF1A sumoylation. Interacts with TSGA10 By similarity. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note: Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under 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. INDUCTION: Under reduced oxygen tension. Induced also by various receptor-mediated factors such as growth factors, cytokines, and circulatory factors such as PDGF, EGF FGF-2 FGF-2 IGF-2, TGF-1 beta, HGF, TNF alpha, IL-1 beta, angiotensin-2 and thrombin. However, this induction is less intense than that stimulated by hypoxia. DOMAIN: Contains two independent C-terminal transactivation domains, NTAD and CTAD, which function synergistically. Their transcriptional activity is repressed by an intervening inhibitory domain (ID). PTM: In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD1 and EGLN2/PHD2. EGLN3/PHD3 has also been shown to hydroxylate Pro-564. The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation. Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization. In normoxia, is hydroxylated on Asn-803 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation. This hydroxylation is inhibited by the Cu/Zn-chelator, Clioquinol. S-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. Sumoylated; by SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Desumoylation by SENP1 leads to increased HIF1A stability and transriptional activity By similarity. Ubiquitinated; 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. The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains. SEQUENCE SIMILARITIES: Contains 1 basic helix-loop-helix (bHLH) domain. Contains 1 PAC (PAS-associated C-terminal) domain. Contains 2 PAS (PER-ARNT-SIM) domains.
Molecular Weight	~120 kDa

Biological Information

Immunogen

Synthetic peptide corresponding to residues near the C-terminus of human HIF-1α.

Epitope

C-terminus

Clone

EP1215Y

Host

Rabbit

Specificity

This antibody recognizes HIF-1α at and around the C-terminus.

Isotype

IgG

Species Reactivity

Human
Rat

Antibody Type

Monoclonal Antibody

Entrez Gene Number

NM_001530.2

Gene Symbol

HIF-1alpha
HIF1
HIF1-ALPHA
MOP1
PASD8
bHLHe78

Purification Method

Unpurified

UniProt Number

Q16665

UniProt Summary

FUNCTION: 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, 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 CREBPB 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.
SUBUNIT STRUCTURE: Interacts with the HIF1A beta/ARNT subunit; heterodimerization is required for DNA binding. Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability By similarity. Interacts with CREBBP and EP300 (via TAZ-type 1 domains). Interacts with NCOA1, NCOA2, APEX and HSP90. Interacts (hydroxylated within the ODD domain) with VHLL (via beta domain); the interaction, leads to polyubiquitination and subsequent HIF1A proteasomal degradation. During hypoxia, sumoylated HIF1A also binds VHL; the interaction promotes the ubiquitination of HIF1A. Interacts with SENP1; the interaction desumoylates HIF1A resulting in stabilization and activation of transcription. Interacts (Via the ODD domain) with ARD1A; the interaction appears not to acetylate HIF1A nor have any affect on protein stability, during hypoxia. Interacts with RWDD3; the interaction enhances HIF1A sumoylation. Interacts with TSGA10 By similarity.
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note: Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under 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.
INDUCTION: Under reduced oxygen tension. Induced also by various receptor-mediated factors such as growth factors, cytokines, and circulatory factors such as PDGF, EGF FGF-2 FGF-2 IGF-2, TGF-1 beta, HGF, TNF alpha, IL-1 beta, angiotensin-2 and thrombin. However, this induction is less intense than that stimulated by hypoxia.
DOMAIN: Contains two independent C-terminal transactivation domains, NTAD and CTAD, which function synergistically. Their transcriptional activity is repressed by an intervening inhibitory domain (ID).
PTM: In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD1 and EGLN2/PHD2. EGLN3/PHD3 has also been shown to hydroxylate Pro-564. The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation. Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization.
In normoxia, is hydroxylated on Asn-803 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation. This hydroxylation is inhibited by the Cu/Zn-chelator, Clioquinol.
S-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.
Sumoylated; by SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Desumoylation by SENP1 leads to increased HIF1A stability and transriptional activity By similarity.
Ubiquitinated; 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.
The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.
SEQUENCE SIMILARITIES: Contains 1 basic helix-loop-helix (bHLH) domain.
Contains 1 PAC (PAS-associated C-terminal) domain.
Contains 2 PAS (PER-ARNT-SIM) domains.

Molecular Weight

~120 kDa

Product Usage Statements
Quality Assurance	Evaluated by Western Blot on Ramos + CoCl2 lysates. Western Blot Analysis: A 1:2,000 dilution of this antibody was used to detect HIF-1α in Ramos + CoCl2 lysate.
Usage Statement	Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Product Usage Statements

Quality Assurance

Evaluated by Western Blot on Ramos + CoCl2 lysates.
Western Blot Analysis: A 1:2,000 dilution of this antibody was used to detect HIF-1α in Ramos + CoCl2 lysate.

Usage Statement

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage and Shipping Information
Storage Conditions	Stable for 1 year at -20ºC from date of receipt. Handling Recommendations: Upon first thaw, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.

Storage and Shipping Information

Storage Conditions

Stable for 1 year at -20ºC from date of receipt. Handling Recommendations: Upon first thaw, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.

Packaging Information
Material Size	100 µL

Packaging Information

Material Size

100 µL

实验耗材

分子生物学试剂

蛋白与免疫学

生化试剂

细胞及检测试剂

色谱及层析

仪器设备

实验服务

办公用品

Mouse Serum Amyloid A-3 (SAA-3) Microtiter Plate

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