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EPO Flt3-L Flt3-L (Murine) Angiostatin GroES 
GroEL Myoglobin PEX, His tagged BD-1   BD-2
Endostatin        

 

 

Erythropoietin  

Cat. No.

CCT01

Product Overview

Recombinant Human EPO is expressed in CHO cells. The mature protein consists of a 165 amino acid polypeptide chain heavily glycosylated at three N-linked and O-linked glycosylation sites yielding a total molecular mass of 35-45kDa. About 40% of the fully glycosylated EPO molecule consists of carbohydrate.

Description

Erythropoietin (EPO) is a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

Purity

≥98% as determined by SDS-PAGE and HPLC analyses

Formulation

Sterile filtered lyophilized powder.

Specific Activity

rHuEPO is fully biologically active when compared to standards. Its specific activity is ≥1.2×105 IU/mg.

Endotoxin

Less than 0.1EU/µg determined by LAL test.

Reconstitution

It is recommended to reconstitute the lyophilized rHuEPO in sterile buffer not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Storagee

Lyophilized rHuEPO although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Reconstituted rHuEPO aliquots should be stored at –20°C for maximal stability up to three years. Aliquot to avoid repeated freeze-thaw cycles.

Gene Information

Gene Name

EPO

Synonyms

EP; MGC138142; Epoetin; Erythropoietin Precursor

GeneID

2056

mRNA Refseq

NM_000799

Protein Refseq

NP_000790

MIM

133170

UniProt ID

P01588

Chromosome Location

7q22

Pathway

Cytokine-cytokine receptor interaction; Hematopoietic cell lineage; Jak-STAT signaling pathway

Function

erythropoietin receptor binding IEA ;hormone activity IEA ;protein binding

 



Crystal structure of EPO. Available structures: 1buy, 1cn4, 1eer

 

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Fms-related Tyrosine Kinase 3 Ligand 

Cat. No.

CCT02

Product Overview

Recombinant Human Flt3-Ligand produced in E.coli is a soluble 17.6 kDa polypeptide containing 155 amino acid residues, which comprises the extracellular domain of the transmembrane flt3-ligand protein

Description

Flt-3 ligand (FL) is a recently identified hematopoietic cytokine whose activities are mediated by binding to the transmembrane glycoprotein Flt-3. Flt-3 was first discovered as a member of the class III subfamily of receptor tyrosine kinases (RTK) whose expression among hematopoietic cells was found to be restricted to highly enriched stem/progenitor cell populations. Additional class III RTKs include the receptors from SCF, M-CSF and PDGF. Not surprisingly, Flt-3 ligand is also structurally related to M-CSF and SCF. All three cytokines have been shown to exist both as type I transmembrane proteins and as soluble proteins. The predominant human FL isoform is a transmembrane protein that can undergo proteolytic cleavage to generate a soluble form of the protein. An alternatively-spliced FL mRNA, encoding a soluble form of the human FL, has also been identified. FL is widely expressed in various human and mouse tissues. At the amino acid sequence level, human and mouse FL are approximately 72% identical and the two proteins exhibit cross-species activity. FL has been shown to synergize with a wide variety of hematopoietic cytokines to stimulate the growth and differentiation of early hematopoietic progenitors.

Purity

≥98% as determined by HPLC and SDS-PAGE.

Formulation

Sterile filtered lyophilized powder, with 20mM Tris-HCl, 20mM NaCl, pH7.4.

Specific Activity

rHuFlt3-L is fully biologically active when compared to standards. Its specific activity is ≥1×106IU/mg.

Endotoxin

Less than 10 IEU/mg of rHuFlt3-L determined by LAL test.

Reconstitution

It is recommended to reconstitute the lyophilized rHuFlt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Storagee

Lyophilized rHuFlt3-L although stable at room temperature for 3 weeks, should be stored desiccated below -18oC. Upon reconstitution rHuFlt3-L should be stored at 4oC between 2-7 days and for future use below -18oC. Aliquot to avoid repeated freeze-thaw cycles.

Gene Information

Gene Name

FLT3LG

Synonyms

FL, Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3, Flt3 ligand, Flt3L, SL cytokine precursor

GeneID

2323

mRNA Refseq

NM_001459

Protein Refseq

NP_001450

MIM

600007

UniProt ID

P49771

Chromosome Location

19q13.3

Pathway

Cytokine-cytokine receptor interaction; Hematopoietic cell lineage

Function

cytokine activity

 



Crystal structure of Flt3-L. PDB rendering based on 1ete.

 

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FMS-like Tyrosine Kinase 3 Ligand (Murine)  

Cat. No.

CCT03

Product Overview

Recombinant murine Flt3-L produced in E.coli is a 16.4kDa globular protein containing 120 amino acid residues.

Description

Flt-3 ligand (FL) is a recently identified hematopoietic cytokine whose activities are mediated by binding to the transmembrane glycoprotein Flt-3. Flt-3 was first discovered as a member of the class III subfamily of receptor tyrosine kinases (RTK) whose expression among hematopoietic cells was found to be restricted to highly enriched stem/progenitor cell populations. Additional class III RTKs include the receptors from SCF, M-CSF and PDGF. Not surprisingly, Flt-3 ligand is also structurally related to M-CSF and SCF. All three cytokines have been shown to exist both as type I transmembrane proteins and as soluble proteins. The predominant human FL isoform is a transmembrane protein that can undergo proteolytic cleavage to generate a soluble form of the protein. An alternatively-spliced FL mRNA, encoding a soluble form of the human FL, has also been identified. FL is widely expressed in various human and mouse tissues. At the amino acid sequence level, human and mouse FL are approximately 72% identical and the two proteins exhibit cross-species activity. FL has been shown to synergize with a wide variety of hematopoietic cytokines to stimulate the growth and differentiation of early hematopoietic progenitors.

Purity

≥95% as determined by HPLC and SDS-PAGE.

Formulation

Sterile filtered lyophilized powder, with 50mM Tris,100mM NaCl, pH8.5.

Specific Activity

rmFlt3-L is fully biologically active when compared to standard. The specific activity is ≥1×105 IU/mg.

Endotoxin

Less than 1 IEU/µg determined by LAL test.

Reconstitution

It is recommended to reconstitute the lyophilized rmFlt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Storagee

Lyophilized rmFlt3-L although stable at room temperature for 3 weeks, should be stored desiccated below -18oC. Reconstituted rmFlt3-L aliquots should be stored at –20oC for maximal stability up to six months. Aliquot to avoid repeated freeze-thaw cycles.

Gene Information

Gene Name

Flt3l

Synonyms

Ly72L, Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3, Flt3 ligand, Flt3L, SL cytokine precursor

GeneID

14256

mRNA Refseq

NM_013520

Protein Refseq

NP_038548

UniProt ID

Q61104

Chromosome Location

7 B2-C; 7 23.0 cM

Pathway

Cytokine-cytokine receptor interaction; Hematopoietic cell lineage

Function

cytokine activity; kinase activity

 



Crystal structure of Flt3-L. PDB rendering based on 1ete.

 

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Angiostatin  

Cat. No.

CCT04

Product Overview

Recombinant Human Angiostatin produced in Pichia has a molecular mass of 30498.6Da.

Description

Angiostatin is a ~30 kDa fragment of plasminogen that has been shown to act as a potent inhibitor of angiogenesis and tumor growth in vitro and in vivo. Recombinant angiostatin is expressed in E. coli.

Purity

≥95% as determined by  SDS-PAGE and HPLC

Component

Angiostatin K 1-3 1mg/mL, NaAc 20 mM, NaCl 150 mM, pH 5.5.

Specific Activity

0.55×105 Units/mg by Anti-migration Assay.The activity is assayed on anti-proliferation and anti-migration of endothelial cells in vitro and anti-angiogenesis in vivo.

PI

7.8 by Isoelectricfocusing

concentration

1.1 mg / ml by BCA

Endotoxin

less than 10EU/mg as determined by LAL method

Storage Buffer  

PBS Buffer.

Storage

At 4℃ for 6 months and -80℃ for 2 years




 

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Chaperonin 10 

Cat. No.

CCT05

Product Overview

Recombinant Human Chaperonin 10 produced in E. coli has a molecular mass of approximately 11 KDa.

Description

Chaperonin 60 (GroEL) and chaperonin 10 (GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles. The chaperonins assist the folding of nascent, organelle-imported or stress-destabilized polypeptides. In vitro, purified GroEL together with purified GroES in the presence of Mg-ATP facilitate refolding and reactivation of denaturedproteins. Chaperonin 10 (GroES) is expressed in E. coli.

Purity

>95% as determined by SDS-PAGE.

Storagee

Liquid. In Tris-HCl Buffer (pH 7.4).

Gene Information

Gene Name

HSPE1

Synonyms

CPN10; GROES; HSP10; EPF; HSP10; Hsp10; 10 kDa chaperonin; 10 kDa heat shock protein; mitochondrial; Early-pregnancy factor; chaperonin 10; heat shock 10kD protein 1

GeneID

3336

mRNA Refseq

NM_002157.1

Protein Refseq

NP_002148.1

MIM

600141

UniProt ID

P61604

Chromosome Location

2q33.1

Pathway

ATP binding, chaperone binding, unfold protein binding

Function

caspase activation,  protein folding, response to unfolded protein

 



A chaperonin called GroEL-GroES complex (from Escherichia coli) (PDB code=1aon). Two rings of 7x2GroEL proteins (shown in blue and green) with a cap (just on one side) of GroES proteins (red and yellow). Unfolded proteins enter that cavity (which is protein sized) to be protected during folding.
 

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Chaperonin 60  

Cat. No.

CCT06

Product Overview

Recombinant Human Chaperonin 60 produced in E. coli has a molecular mass of approximately 60 KDa.

Description

Chaperonin 60(GroEL) and chaperonin 10(GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles. The chaperonins assist the folding of nascent, organelle-imported or stress-destabilized polypeptides. In vitro, purified GroEL together with purified GroES in the presence of Mg- ATP facilitate refolding and reactivation of denatured proteins. Chaperonin 60(GroEL) is expressed in E. coli.

Purity

>95% as determined by SDS-PAGE.

Storagee buffer

Liquid. In Tris-HCl Buffer (pH 7.4).

Gene Information

Gene Name

HSPD1

Synonyms

CPN60; GROEL; HSP-60; HSP60; HSP65; Hsp60; HuCHA60; SPG13; chaperonin; 60 kDa chaperonin; 60 kDa heat shock protein; mitochondrial precursor; Heat shock protein 60; Mitochondrial matrix protein P1; P60 lymphocyte protein; heat shock 60kD protein 1 (chaperonin); heat shock protein 65; short heat shock protein 60 Hsp60s1; spastic paraplegia 13 (autosomal dominant)

GeneID

3329

mRNA Refseq

NM_002156.4

Protein Refseq

NP_002147.2

MIM

118190

UniProt ID

P10809

Chromosome Location

2q33.1

Pathway

Prion disease, Type I diabetes mellitus

Function

ATP binding, chaperone binding, unfold protein binding

Process

caspase activation,  protein folding, response to unfolded protein

 



A chaperonin called GroEL-GroES complex (from Escherichia coli) (PDB code=1aon). Two rings of 7x2GroEL proteins (shown in blue and green) with a cap (just on one side) of GroES proteins (red and yellow). Unfolded proteins enter that cavity (which is protein sized) to be protected during folding.
 

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Myoglobin  

Cat. No.

CCT11

Product Overview

Recombinant Sperm whale myoglobin produced in E. coli has a molecular mass of approximately 17 KDa.

Description

Myoglobin contains an intracellular heme that facilitates the transport of molecular oxygen by combining with molecular oxygen to form oxymyoglobins. Measurement of myoglobin levels is useful in the diagnosis of skeletal and cardiac muscle damage. Sperm whale myoglobin is expressed in E. coli.

Purity

>95% as determined by SDS-PAGE.

Storagee buffer

Liquid. In PBS Buffer.

Gene Information

Gene Name

MB

Synonyms

MGC13548; PVALB; Myoglobin; myoglobin

GeneID

4151

mRNA Refseq

NM_005368.2

Protein Refseq

NP_005359.1

MIM

160000

UniProt ID

P02144 

Function

heme binding, iron ion binding, metal ion binding, oxygen binding, oxygen transporter activity.

Process

enuclease erythrocyte differentiation, heart development, oxygen transport, response to hypoxia, transport.

 



Model of helical domains in myoglobin.[1]
 

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PEX, His tagged  

Cat. No.

CCT14

Product Overview

Recombinant Human PEX produced in E. coli has a molecular mass of approximately 23 KDa.

Description

PEX is the C-terminal hemopexin domain of Matrix Metalloproteinase-2. It has the activity of anti-angiogenesis, and a naturally occurring form of PEX can be detected in vivo. PEX can block angiogenesis and tumor growth in vivo, providing a potentially novel therapeutic approach for diseases associated with neovascularization. The appearance of PEX at sites of neovascularization may not only control normal angiogenesis, but when administered in sufficient quantities, may provide a naturally-occurring therapeutic inhibitor of diseases associated with angiogenesis.

Purity

>95% as determined by SDS-PAGE.

Specific Activity

Measured by its ability of suppressing angiogenesis in vitro.

Formulation

The protein (1mg/ml) was lyophilized with 2mM Tris pH-7.4.

Storage Buffer

Liquid. In PBS Buffer.

Storagee

Lyophilized rHuPEX although stable at room temperature for 3 weeks, should be stored desiccated below -18oC. Upon reconstitution rHuPEX should be stored at 4oC between 2-7 days and for future use below -18oC.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

Gene Information

Gene Name

MMP2

Synonyms

CLG4; MONA; CLG4A; TBE-1; MMP-II; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); MMP2_HUMAN; 72 kDa type IV collagenase [Precursor]; EC 3.4.24.24.; 72 kDa gelatinase; 72kD type IV collagenase; Gelatinase A; Matrix metalloproteinase-2; collagenase type IV-A; matrix metalloproteinase 2 (gelatinase A, 72kD gelatinase, 72kD typeIV collagenase); matrix metalloproteinase-II; neutrophil gelatinase.

GeneID

4313

mRNA Refseq

NM_001127891

Protein Refseq

NP_001121363

MIM

120360

UniProt ID

P08253

Chromosome Location

16q13-q21

Pathway

GnRH signaling pathway; Leukocyte transendothelial migration.

Function

calcium ion binding; catalytic activity; metal ion binding; metalloendopeptidase activity; protein binding; zinc ion binding

 



PDB rendering based on 1ck7.
Available structures: 1ck7, 1cxw, 1eak, 1gen,
1gxd, 1j7m, 1ks0, 1rtg
 

Download Datasheet::

 

beta-Defensin 1 

Cat. No.

CCT17

Product Overview

Recombinant Human beta-Defensin 1 produced in E. coli is a single non-glycosylated polypeptide chain containing 47 amino acids and having a molecular mass of approximately 5.0 KDa,

Description

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, four human β-defensins have been identified; BD-1, BD-2, BD-3 and BD-4. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. β-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

Purity

>98% by SDS-PAGE and HPLC analyses.

Formulation

Lyophilized from a 0.2mm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 130mM NaCl.

Biological Activity

Fully biologically active when compared to standard. Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

Endotoxin

Less than 1EU/mg of rHuBD-1 as determined by LAL method.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-20oC. Further dilutions should be made in appropriate buffered solutions.

Storage

This lyophilized preparation is stable for several weeks at 2-8oC, but should be kept at -20oC for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8oC. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20oC to -70oC. Avoid repeated freeze/thaw cycles.

Gene Information

Gene Name

DEFB1

Synonyms

BD1, DEFB-1, DEFB101, HBD1, hBD-1,beta-defensin-1, defensin beta 1, MGC51822, Beta-defensin 1 precursor, BD-1

GeneID

1672

mRNA Refseq

NM_005218.3

Protein Refseq

NP_005209.1

MIM

602056

UniProt ID

P60022

Chromosome Location

8p23.2-p23.1

Process

G-protein coupled receptor protein signaling pathway, chemotaxis, defense response to bacterium, innate immune response.

 



PDB rendering based on 1e4s.
 

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beta-Defensin 2  

Cat. No.

CCT18

Product Overview

Recombinant Human beta-Defensin 2 produced in E. coli is a single non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of  4.3 kDa.

Description

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, four human β-defensins have been identified; BD-1, BD-2, BD-3 and BD-4. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. β-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

Purity

>98% by SDS-PAGE and HPLC analyses.

Formulation

Lyophilized from a 0.2mm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 130mM NaCl.

Biological Activity

Fully biologically active when compared to standard. Determined by its ability to chemoattract immature human dendritic cells using a concentration range of 10-100 ng/ml.

Endotoxin

Less than 1EU/mg of rHuBD-2 as determined by LAL method.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-20oC. Further dilutions should be made in appropriate buffered solutions.

Storagee

This lyophilized preparation is stable for several weeks at 2-8oC, but should be kept at -20oC for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8oC. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20oC to -70oC. Avoid repeated freeze/thaw cycles.

Gene Information

Gene Name

DEFB4

Synonyms

DEFB-2; DEFB102; DEFB2; HBD-2; SAP1; defensin, beta 4; defensin, beta 2; skin-antimicrobial peptide 1; Beta-defensin 2 precursor; Defensin β2; H.sapiens mRNA for skin-antimicrobial-peptide 1 (SAP1); defensin β4

GeneID

1673

mRNA Refseq

NM_004942.2

Protein Refseq

NP_004933.1

MIM

602215

UniProt ID

O15263

Chromosome Location

8p23.1-p22

Process

G-protein  coupled receptor protein signaling pathway; chemotaxis; defense response to bacterium; immune response.

 



PDB rendering based on 1e4q.
 

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Endostatin  

Cat. No.

CCT19

Product Overview

Recombinant Human Endostatin produced in Pichia P. is a single glycosylated polypeptide having a total molecular mass of 20 kDa.

Description

Endostatin has been identified as a C-terminal fragment of Collagen type 18, a recently identified member of a family of collagen-like proteins referred to as multiplexin familyEndostatin specifically inhibits proliferation of endothelial cells although it does not affect the proliferation of EOMA cells. Endostatin also potently inhibits angiogenesis and tumor growth. Endostatin has an important role in endothelial cell adhesion and cytoskeletal organization. Endostatin can be found in vessel walls (elastic fibers) and basement membranes. Recombinant Endosatin expressed in yeast causes G1 arrest of endothelial cells, and endostatin treatment results in apoptosis of HUVE and HMVE cells.

Purity

>96% by SDS-PAGE and HPLC analyses.

Formulation

Lyophilized from a 0.2μm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

Biological Activity

Fully biologically active when compared to standard. The activity calculated by ECE migration inhibition was found to be 50,000IU/mg.

Endotoxin

Less than 1EU/μg of rHuEndostatin as determined by LAL method.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20oC. Further dilutions should be made in appropriate buffered solutions.

Storagee

This lyophilized preparation is stable at 2-8oC, but should be kept at -20oC for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8oC. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20oC to -70oC. Avoid repeated freeze/thaw cycles.

Gene Information

Gene Name

COL18A1

Synonyms

FLJ27325; KNO; KNO1; MGC74745; OTTHUMP00000115472; OTTHUMP00000115473; alpha 1 type XVIII collagen; antiangiogenic agent; endostatin; multi-functional protein MFP; XVIII chain precursor; Collagen alpha-1; XVIIIchain precursor; collagen, type XVIII, alpha 1; human type XVIII collagen

GeneID

80781

mRNA Refseq

NM_030582.3

Protein Refseq

NP_085059.2

MIM

120328

UniProt ID

P39060

Chromosome Location

21q22.3

Process

binding, extracellular matrix structural constituent, metal ion binding, protein binding, structural molecular activity, zinc ion binding.

 



Endostatin monomer, basic amino acid residues shown in red 1KOE.
 

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Last modified: 05/13/09