|


|
GENTAUR
+32
1658 9045
or
0032 (0)16 41 44
07
+32
1650 9045
info@gentaur.com
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l' Armée 68
B-1040
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BELGIUM

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1650 9045

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Other Countries
0032 (0)16 41 44 07
|

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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
|
Download Datasheet:
 |
|
|
|
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.
|
Download Datasheet:
 |
|
|
|
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.
|
Download Datasheet:
 |
|
|
|
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 |
|
|
Download Datasheet:
 |
|
|
|
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.
|
Download Datasheet:
 |
|
|
|
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.
|
Download Datasheet:
 |
|
|
|
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]
|
Download Datasheet:
 |
|
|
|
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 |
| |
|
|
|
|
|
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.
|
Download Datasheet:
 |
|
|
|
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.
|
Download Datasheet:
 |
|
|
|
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. |
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Endostatin monomer, basic amino acid residues shown in
red
1KOE.
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Download Datasheet:
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