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Description:

Platelet-Derived Growth Factor Receptor, Beta Human Recombinant

Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b AntigenNDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,Platelet-Derived Growth Factor Receptor Beta.

Product # :

CYT-1051

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Description

PDGFRB produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 739 amino acids (33-532a.a.) and having a molecular mass of 83.3kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).PDGFRB is expressed with an 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

PDGFRB protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Platelet-derived growth factor receptor beta (PDGFRB), belongs to the class III subfamily of receptor tyrosine kinases (RTK) which also consist of the receptors for Flt3-ligand, SCF and M-CSF. PDGFRB takes a vital part in blood vessel development by promoting growth, migration as well as recruitment of pericytes and smooth muscle cells to endothelial cells. PDGFRB helps in rearrangement of the actin cytoskeleton in addition the formation of membrane ruffles. PDGFRB phosphorylates, NCK1, PIK3R1, PTPN11, CBL, SHC1, RASA1/GAP and PLCG1.
Synonyms
Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b Antigen
NDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,
Platelet-Derived Growth Factor Receptor Beta.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
LVVTPPGPEL VLNVSSTFVL TCSGSAPVVW ERMSQEPPQE MAKAQDGTFS SVLTLTNLTG LDTGEYFCTH NDSRGLETDE RKRLYIFVPD PTVGFLPNDA EELFIFLTEI TEITIPCRVT DPQLVVTLHE KKGDVALPVP YDHQRGFSGI FEDRSYICKT TIGDREVDSD AYYVYRLQVS SINVSVNAVQ TVVRQGENIT LMCIVIGNEV VNFEWTYPRK ESGRLVEPVT DFLLDMPYHI RSILHIPSAE LEDSGTYTCN VTESVNDHQD EKAINITVVE SGYVRLLGEV GTLQFAELHR SRTLQVVFEA YPPPTVLWFK DNRTLGDSSA GEIALSTRNV SETRYVSELT LVRVKVAEAG HYTMRAFHED AEVQLSFQLQ INVPVRVLEL SESHPDSGEQ TVRCRGRGMP QPNIIWSACR DLKRCPRELP PTLLGNSSEE ESQLETNVTY WEEEQEFEVV STLRLQHVDR PLSVRCTLRN AVGQDTQEVI VVPHSLPFKV LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Insulin Like Growth Factor-1 N15 Labeled Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

CYT-128

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Description

IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N15 is stable isotope labeled. The IGF1 N15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGF1 N15 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg.

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 N15 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IGF1 N15 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Hepatocyte Growth Factor Receptor Mouse Recombinant

hepatocyte growth factor receptor, HGF R/c-MET, Met, AI838057, c-Met, HGF, HGFR, Par4, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met.

Product # :

CYT-1139

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Description

HGF Receptor Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 1146 amino acids (25-931aa) and having a molecular mass of 127.8kDa. HGF is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

HGF Receptor protein (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
HGF, also known as scatter factor (SF) and Hepatocyte growth factor, is secreted from mesenchymal cells, targets and acts mainly on epithelial and endothelial cells. The protein is a paracrine cellular growth, motility and morphogenic factor. HGF can also be part of haemopoietic progenitor cells and T cells. HGF has a crucial role in embryonic organ development, mainly in myogenesis. In adults HGF takes part in organ regeneration and wound healing.
Synonyms
hepatocyte growth factor receptor, HGF R/c-MET, Met, AI838057, c-Met, HGF, HGFR, Par4, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ECKEALVKSE MNVNMKYQLP NFTAETPIQN VVLHGHHIYL GATNYIYVLN DKDLQKVSEF KTGPVLEHPD CLPCRDCSSK ANSSGGVWKD NINMALLVDT YYDDQLISCG SVNRGTCQRH VLPPDNSADI QSEVHCMFSP EEESGQCPDC VVSALGAKVL LSEKDRFINF FVGNTINSSY PPGYSLHSIS VRRLKETQDG FKFLTDQSYI DVLPEFQDSY PIKYIHAFES NHFIYFLTVQ KETLDAQTFH TRIIRFCSVD SGLHSYMEMP LECILTEKRR KRSTREEVFN ILQAAYVSKP GANLAKQIGA SPSDDILFGV FAQSKPDSAE PVNRSAVCAF PIKYVNDFFN KIVNKNNVRC LQHFYGPNHE HCFNRTLLRN SSGCEARSDE YRTEFTTALQ RVDLFMGRLN QVLLTSISTF IKGDLTIANL GTSEGRFMQV VLSRTAHLTP HVNFLLDSHP VSPEVIVEHP SNQNGYTLVV TGKKITKIPL NGLGCGHFQS CSQCLSAPYF IQCGWCHNQC VRFDECPSGT WTQEICLPAV YKVFPTSAPL EGGTVLTICG WDFGFRKNNK FDLRKTKVLL GNESCTLTLS ESTTNTLKCT VGPAMSEHFN VSVIISNSRE TTQYSAFSYV DPVITSISPR YGPQAGGTLL TLTGKYLNSG NSRHISIGGK TCTLKSVSDS ILECYTPAQT TSDEFPVKLK IDLANRETSS FSYREDPVVY EIHPTKSFIS GGSTITGIGK TLNSVSLPKL VIDVHEVGVN YTVACQHRSN SEIICCTTPS LKQLGLQLPL KTKAFFLLDG ILSKHFDLTY VHNPVFEPFE KPVMISIGNE NVVEIKGNNI DPEAVKGEVL KVGNQSCESL HWHSGAVLCT VPSDLLKLNS ELNIEWKQAV SSTVLGKVIV QPDQNFALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
Background
What is the molecular weight/Mw of HGFR MOUSE Protein?
HGFR MOUSE Protein has a total Mw of 127.8kDa.

What is the source or expression system of HGFR MOUSE Protein?
Sf9, Baculovirus cells.

What is the Purity of HGFR MOUSE Protein?
HGFR MOUSE Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of HGFR MOUSE Protein?
The biological functionality of HGFR MOUSE Protein will be determined in the future.

What is the amino acid sequence of HGFR MOUSE Protein?
ECKEALVKSE MNVNMKYQLP NFTAETPIQN VVLHGHHIYL GATNYIYVLN DKDLQKVSEF KTGPVLEHPD CLPCRDCSSK ANSSGGVWKD NINMALLVDT YYDDQLISCG SVNRGTCQRH VLPPDNSADI QSEVHCMFSP EEESGQCPDC VVSALGAKVL LSEKDRFINF FVGNTINSSY PPGYSLHSIS VRRLKETQDG FKFLTDQSYI DVLPEFQDSY PIKYIHAFES NHFIYFLTVQ KETLDAQTFH TRIIRFCSVD SGLHSYMEMP LECILTEKRR KRSTREEVFN ILQAAYVSKP GANLAKQIGA SPSDDILFGV FAQSKPDSAE PVNRSAVCAF PIKYVNDFFN KIVNKNNVRC LQHFYGPNHE HCFNRTLLRN SSGCEARSDE YRTEFTTALQ RVDLFMGRLN QVLLTSISTF IKGDLTIANL GTSEGRFMQV VLSRTAHLTP HVNFLLDSHP VSPEVIVEHP SNQNGYTLVV TGKKITKIPL NGLGCGHFQS CSQCLSAPYF IQCGWCHNQC VRFDECPSGT WTQEICLPAV YKVFPTSAPL EGGTVLTICG WDFGFRKNNK FDLRKTKVLL GNESCTLTLS ESTTNTLKCT VGPAMSEHFN VSVIISNSRE TTQYSAFSYV DPVITSISPR YGPQAGGTLL TLTGKYLNSG NSRHISIGGK TCTLKSVSDS ILECYTPAQT TSDEFPVKLK IDLANRETSS FSYREDPVVY EIHPTKSFIS GGSTITGIGK TLNSVSLPKL VIDVHEVGVN YTVACQHRSN SEIICCTTPS LKQLGLQLPL KTKAFFLLDG ILSKHFDLTY VHNPVFEPFE KPVMISIGNE NVVEIKGNNI DPEAVKGEVL KVGNQSCESL HWHSGAVLCT VPSDLLKLNS ELNIEWKQAV SSTVLGKVIV QPDQNFALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
What applications can HGFR MOUSE Protein be used in?
HGFR MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HGFR MOUSE Protein?
The endotoxin level is minimal, HGFR MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor Rat Recombinant, Yeast

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-1126

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Description

Vascular Endothelial Growth Factor Rat Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x165 amino acid polypeptide chains, having a molecular mass of approximately 25.7kDa each.VEGF is purified by proprietary chromatographic techniques.

Source

Saccharomyces cerevisiae

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 was measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells and was found to be 0.75‑3.75 ng/ml.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both angiogenesis and vasculogenesis.VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of VEGF is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in VEGF have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vascular Endothelial Growth Factor should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPTTEGEQK AHEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNVTMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Transforming Growth Factor-Beta 1 Rat Recombinant

Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.

Product # :

CYT-1265

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Description

Transforming Growth Factor-Beta 1 Rat Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa.
TGFB1 Rat Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

The biological activity was determined by TGFB1 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

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Synonyms
Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 1 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Transforming Growth Factor-Beta 1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSALDTNYC FSSTEKNCCV RQLYIDFRKD LGWKWIHEPK GYHANFCLGP CPYIWSLDTQ YSKVLALYNQ HNPGASASPC CVPQALEPLP IVYYVGRKPK VEQLSNMIVR SCKCS.
Background
Mouse TGF-β1 as an inducer of EMT [epithelial–mesenchymal transition ] therefore used in in fibrosis, wound healing, cancer invasion, and metastasis. Mouse TGF-β1 decreases E-cadherin expression and increases N-cadherin, vimentin and fibronectin.
TGF-β1 is produced by T regulatory cells (Tregs), Macrophages and monocytes, Platelets, Fibroblasts, Epithelial cells, Endothelial cells, Smooth muscle cells, Tumor cells, Activated immune cells
What is the source or expression system of Mouse TGFB1 Protein?
CHO Cells

What is the Purity of Mouse TGFB1 Protein?
Mouse TGFB1 Protein is >97% pure as determined by SDS-PAGE and SEC-HPLC analyses.

What is the molecular weight of Mouse TGFB1 Protein?
Mouse TGFB1 Protein having a total Mw of 25.6kDa.

What is the Biological Activity of Mouse TGFB1 Protein?
The biological functionality of Mouse TGFB1 Protein is determined by mouse HT-2 cells.

What is the endotoxin level for Mouse TGFB1 Protein?
The endotoxin level is minimal, Mouse TGFB1 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of Mouse TGFB1 Protein?
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASASPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.

Is TGFB1 a homodimer / homodimeric protein?
Yes, TGFB1 is homo dimer consisting of 2 identical chains.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Macrophage-Colony Stimulating Factor Mouse Recombinant

CSF-1, Lanimostim, MCSF, M-CSF.

Product # :

CYT-439

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Description

Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5x10⁵ units/mg.

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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
CSF-1, Lanimostim, MCSF, M-CSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized M-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.
Background
Macrophage-Colony Stimulating Factor Mouse Recombinant: An In-Depth Analysis
Abstract:
Macrophage-Colony Stimulating Factor (M-CSF) is a crucial cytokine involved in the regulation of macrophage biology, including their differentiation, survival, and function. This research paper provides an in-depth analysis of M-CSF Mouse Recombinant, focusing on its structure, signaling pathways, and diverse functions in the context of human research. Additionally, the paper explores the therapeutic potential of M-CSF modulation in various diseases.
Introduction:
M-CSF plays a vital role in the development and maintenance of macrophages, key immune cells involved in innate immunity and tissue homeostasis. This paper aims to provide a comprehensive analysis of M-CSF Mouse Recombinant, highlighting its importance in human macrophage biology and its potential therapeutic applications.
Structure and Function of M-CSF:
M-CSF is a homodimeric protein that binds to its receptor, CSF-1R, leading to the activation of downstream signaling pathways. It regulates the proliferation, survival, and activation of macrophages, influencing immune responses and tissue remodeling processes.
Signaling Pathways:
Upon binding to CSF-1R, M-CSF triggers various intracellular signaling pathways, including the MAPK pathway, PI3K/Akt pathway, and JAK/STAT pathway. These pathways regulate gene expression and mediate cellular responses, impacting macrophage functions.
Role in Macrophage Development and Function:
M-CSF is essential for the differentiation and maturation of macrophages from hematopoietic progenitor cells. It promotes the survival, proliferation, and activation of macrophages, enhancing their phagocytic activity, cytokine production, and antigen presentation capabilities.
Therapeutic Potential:
Given its crucial role in macrophage biology, M-CSF modulation has emerged as a potential therapeutic strategy. M-CSF inhibitors and CSF-1R antagonists have shown promise in the treatment of inflammatory and autoimmune diseases, as well as certain cancers. Targeting M-CSF signaling can modulate immune responses and affect disease progression.
Clinical Applications and Future Directions:
The therapeutic potential of M-CSF modulation is being explored in various clinical settings. Clinical trials investigating M-CSF inhibitors as monotherapy or combination therapy are underway in diseases such as rheumatoid arthritis and cancer. Future research should focus on understanding the intricate mechanisms of M-CSF signaling, optimizing therapeutic strategies, and developing personalized treatment approaches.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Canine Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

Product # :

CYT-724

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Description

GMCSF k9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14.2 kDa. GM-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GMCSF was lyophilized after extensive dialysis against 1xPBS pH 7.4.

Purity

Greater than 96.0% as determined by
1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.

Biological Activity

The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF1 erythroleukemic cells is typically 1-4 ng/ml.

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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APTRSPTLVT RPSQHVDAIQ EALSLLNNSN DVTAVMNKAV KVVSEVFDPE
GPTCLETRLQ LYKEGLQGSL TSLKNPLTMM ANHYKQHCPP TPESPCATQN
INFKSFKENL KDFLFNIPFD CWKPVKK.
Background
What is the molecular weight/Mw of GM-CSF K9 Protein?
GM-CSF K9 Protein has a total Mw of 14.2kDa.

What is the source or expression system of GM-CSF K9 Protein?
Escherichia Coli.

What is the Purity of GM-CSF K9 Protein?
GM-CSF K9 Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF K9 Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF1 erythroleukemic cells is typically 1-4 ng/ml.

What is the amino acid sequence of GM-CSF K9 Protein?
APTRSPTLVT RPSQHVDAIQ EALSLLNNSN DVTAVMNKAV KVVSEVFDPE
GPTCLETRLQ LYKEGLQGSL TSLKNPLTMM ANHYKQHCPP TPESPCATQN
INFKSFKENL KDFLFNIPFD CWKPVKK.

What applications can GM-CSF K9 Protein be used in?
GM-CSF K9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF K9 Protein?
The endotoxin level is minimal, GM-CSF K9 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Insulin Like Growth Factor-1, Mutant A70T Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

CYT-1091

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Description

IGF1 A70T Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7kDa. The IGF1 A70T is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGF1 A70T Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM PB and 150 mM NaCl, pH 6.0.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IGF1 A70T in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKST.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Insulin Like Growth Factor Binding Protein-2 Mouse Recombinant

IBP-2, IGF-binding protein 2, IGFBP-2, mIGFBP-2, Igfbp-2, insulin-like growth factor binding protein 2 isoform 1, insulin-like growth factor binding protein 2.

Product # :

CYT-1229

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Description

IGFBP2 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 35-305) containing 277 amino acids and having a molecular mass of 30.3kDa. IGFBP2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

IGFBP2 protein (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range is ≤ 0.7 ug/ml which measured by its ability to inhibit proliferation using MCF-7 human breast cancer cells in the presence of Mouse IGF-2.

More Info

Synonyms
IBP-2, IGF-binding protein 2, IGFBP-2, mIGFBP-2, Igfbp-2, insulin-like growth factor binding protein 2 isoform 1, insulin-like growth factor binding protein 2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
EVLFRCPPCT PERLAACGPP PDAPCAELVR EPGCGCCSVC ARQEGEACGV YIPRCAQTLR CYPNPGSELP LKALVTGAGT CEKRRVGTTP QQVADSDDDH SEGGLVENHV DGTMNMLGGG SSAGRKPLKS GMKELAVFRE KVNEQHRQMG KGAKHLSLEE PKKLRPPPAR TPCQQELDQV LERISTMRLP DDRGPLEHLY SLHIPNCDKH GRYNLKQCKM SLNGQRGECW CVNPNTGKPI QGAPTIRGDP ECHLFYNEQQ ETGGAHAQSV QHHHHHH.
Background
Insulin-like growth factor-binding protein 2 (IGFBP2) is a key regulator of insulin-like growth factor (IGF) signaling pathway, playing crucial roles in cell proliferation, differentiation, and survival. IGFBP2, a member of the IGFBP family, modulates the bioavailability and activity of IGFs by binding to them and regulating their interaction with cell surface receptors. In recent years, IGFBP2 has emerged as a promising target for research due to its involvement in various physiological processes and its implications in several diseases, including cancer, metabolic disorders, and neurodegenerative conditions.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Bone Morphogenetic protein-8b Human Recombinant

Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.

Product # :

CYT-830

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source
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sds-page

Description

BMP8B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (264-402a.a.) and having a molecular mass of 18.1kDa.BMP8B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

BMP8B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
Bone Morphogenetic protein-8b (BMP8B) belongs to a family of secreted signaling molecules which can induce ectopic bone growth. BMP8B is known for having a possible bone inductive activity as it is related to BMP5 and BMP7. BMP8B is the osteoinductive factor accountable for epithelial osteogenesis.
Synonyms
Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAVRPLRR RQPKKSNELP QANRLPGIFD DVHGSHGRQV CRRHELYVSF QDLGWLDWVI APQGYSAYYC EGECSFPLDS CMNATNHAIL QSLVHLMMPD AVPKACCAPT KLSATSVLYY DSSNNVILRK HRNMVVKACG CH.
Background
Bone Morphogenetic Protein-8B Human Recombinant: Unveiling the Potential for Regenerative Medicine and Tissue Engineering
Abstract:
Bone Morphogenetic Protein-8B (BMP-8B) human recombinant is a key member of the bone morphogenetic protein family, renowned for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-8B, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-8B human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine and tissue engineering.
Introduction:
Regenerative medicine and tissue engineering offer promising solutions to address the challenges of tissue repair and regeneration. BMP-8B, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper delves into the distinctive features of BMP-8B and presents novel approaches for the production and optimization of BMP-8B human recombinant, aiming to unleash its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-8B is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, thereby initiating intricate intracellular signaling cascades. BMP-8B signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.
Production of BMP-8B Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-8B human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-8B. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-8B recombinant protein.
Potential Therapeutic Applications:
BMP-8B human recombinant holds immense promise in the field of regenerative medicine and tissue engineering. Its involvement in bone and cartilage formation, muscle regeneration, and wound healing makes it a potential candidate for the treatment of skeletal disorders, muscle injuries, and chronic wounds. Furthermore, the ability of BMP-8B to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.
Conclusion:
BMP-8B human recombinant emerges as a crucial regulator in regenerative medicine and tissue engineering, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. Given its involvement in bone, cartilage, and muscle formation, as well as wound healing, BMP-8B human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.
What is the molecular weight/Mw of BMP8B Protein?
BMP8B Protein has a total Mw of 18.1kDa.

What is the source or expression system of BMP8B Protein?
Escherichia Coli.

What is the Purity of BMP8B Protein?
BMP8B Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP8B Protein?
The biological functionality of BMP8B Protein will be determined in the future.

What is the amino acid sequence of BMP8B Protein?
MGSSHHHHHH SSGLVPRGSH MGSAVRPLRR RQPKKSNELP QANRLPGIFD DVHGSHGRQV CRRHELYVSF QDLGWLDWVI APQGYSAYYC EGECSFPLDS CMNATNHAIL QSLVHLMMPD AVPKACCAPT KLSATSVLYY DSSNNVILRK HRNMVVKACG CH.

What applications can BMP8B Protein be used in?
BMP8B Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP8B Protein?
The endotoxin level is minimal, BMP8B Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Platelet-Derived Growth Factor BB Mouse Recombinant

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

Product # :

CYT-412

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Description

Platelet-Derived Growth Factor BB Mouse Recombinant produced in E.coli, is a homodimeric, non-glycosylated, polypeptide chain containing 2x110 (total of 2 chains 220aa) amino acids and having a total molecular weight of 24.7 kDa.PDGF-BB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 10mM NaCitrate pH-3.0.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity is determined by the dose-dependant stimulation of the proliferation of human umbelical vein endothelial cells (HUVEC) using a concentration range of less than 1.6ng/ml.

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Introduction
PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Platelet-derived Growth Factor BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Platelet-derived Growth Factor-BB in sterile 100mM acetic acid and 0.1% BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSLGSLAAAE PAVIAECKTR TEVFQISRNL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRASQVQMRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETIVTPRPVT
Background
Platelet-Derived Growth Factor BB (PDGF-BB) is one of the isoforms of the PDGF family that plays a significant role in embryonic development, cell proliferation, cell migration, and angiogenesis.
It's also relevant in the context of certain pathologies like cancer or healing processes.
Here's what a research paper on Mouse Recombinant PDGF-BB might involve:
Basic Biology:
It might discuss the basic biology and function of PDGF-BB in the mouse model. This could include its role in various cellular processes like cell growth, division, and survival, as well as in the context of tissue repair or angiogenesis.

Recombinant PDGF-BB Production:
The paper might describe methods for producing recombinant PDGF-BB in laboratory conditions. It might go into detail on the expression system used (e.g., bacterial, yeast, or mammalian cells), the purification process, and how the functionality of the produced PDGF-BB was confirmed.

Applications:
It could also detail the experimental applications of recombinant PDGF-BB in the mouse model. For instance, it could be used to study wound healing processes, tissue regeneration, or the development and progression of certain diseases.
Comparative Analysis:
The research might include a comparison of the recombinant PDGF-BB with its natural counterpart in terms of functionality, structure, or other properties.

Innovation:
If the paper is presenting new research, it might discuss an innovative use of PDGF-BB, a novel production method, or new findings about its function.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.48 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of PDGF-BB as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Transforming Growth Factor-Beta 1 Human Recombinant, His Tag

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.

Product # :

CYT-672

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Description

TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (279-390) having a molecular weight of 17.3kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TGF-b 1 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TGF-b 1 His-Tag protein is supplied in 25mM NaAcetate pH 4.8 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
TGF-b 1 regulates the actions of numerous other growth factors involved in a variety of human diseases including renal disease, hepatic disease, heart failure and cardiomyopathies.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor Human Recombinant, Plant

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-1213

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Description

Vascular Endothelial Growth Factor Human Recombinant produced in Oryza Sativa has a molecular mass of 19.2kDa. The VEGF is purified by proprietary chromatographic techniques.

Source

Rice Grain

Formulation

The VEGF protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 10ng/ml, corresponding to a Specific Activity of 100,000IU/mg

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Introduction
Vascular endothelial growth factor (VEGF) is an important signaling protein involved in vessel formation As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces vasculogenesis and endothelial cell production, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. VEGF is located in normal cartilage though only osteoarthritic cartilage expresses the VEGF receptors, NP1, VEGFR1 and VEGFR2. The VEGF level in the culture media from OA chondrocytes was more than 3 folds higher than in media from normal chondrocytes
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized VEGF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant, His Tag

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim

Product # :

CYT-1160

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Description

GMCSF Poricne Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (18-144a.a.) and having a molecular mass of 16.6kDa.GMCSF is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GMCSF protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

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Introduction
The hematopoietic growth factor GM-CSF or granulocyte macrophage colony-stimulating factor, stimulates the development of neutrophils & macrophages, enhance proliferation and development of early erythroid megakaryocytic & eosinophilic progenitor cells. GM-CSF is secreted from the fibroblasts, monocytes, T-lymphocytes & endothelial cells. This protein blocks the migration of neutrophils & induces the biological activity of mature end-cells.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK
Background
What is the molecular weight/Mw of GM-CSF PORCINE, HIS Protein?
GM-CSF PORCINE, HIS Protein has a total Mw of 16.6kDa.

What is the source or expression system of GM-CSF PORCINE, HIS Protein?
Escherichia Coli.

What is the Purity of GM-CSF PORCINE, HIS Protein?
GM-CSF PORCINE, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF PORCINE, HIS Protein?
The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

What is the amino acid sequence of GM-CSF PORCINE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK

What applications can GM-CSF PORCINE, HIS Protein be used in?
GM-CSF PORCINE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF PORCINE, HIS Protein?
The endotoxin level is minimal, GM-CSF PORCINE, HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

RANK Ligand Soluble Human Recombinant

Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

Product # :

CYT-334

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source
formulation
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HPLC, SDS-PAGE

Description

sRANKL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19.7kDa.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Sodium phosphate, pH-7.5.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Biological Activity

The activity of RAW-Blue was measured to be 46.96 ng/ml, corresponding to a specific activity of 2.1x10⁴units/mg.

HPLC, SDS-PAGE

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Introduction
RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.
Synonyms
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFSF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANKL should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized sRANKL in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EKAMVDGSW LDLAKRSKLE AQPFAHLTIN ATDIPSGSHK VSLSSWYHDR GWAKISNMTF SNGKLIVNQD GFYYLYANIC FRHHETSGDL ATEYLQLMVY VTKTSIKIPS SHTLMKGGST KYWSGNSEFH FYSINVGGFF KLRSGEEISI EVSNPSLLDP DQDATYFGAF KVRDID.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Cell Growth Factor, Mouse Anti-Human

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

ANT-125

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Shipped at Room temp

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Introduction
Vascular endothelial growth factoris an important signaling proteininvolved in both vasculogenesisand angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.HumanVEGF.
Ig Subclass
Mouse IgM.
Clone
NYRhVEGF.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.15 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Boric acid precipitation Protein concentration1mg/ml in PBS (after reconstitution).

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor (121) Human Recombinant, HEK

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-116

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Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Recombinant Human VEGF 121 amino acids, produced in HEK cells is a glycosylated 37kDa homodimer and 50kDa homotrimer.The VEGF is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

VEGF was lyophilized from a 0.2µm filtered solution containing 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of HUVEC cells (Human Umbilical Vein Endothelial Cells), the ED₅₀ is 3ng/ml.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized VEGF in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth Hormone Human Recombinant

GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

CYT-202

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
purity
biological activity
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Description

GH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids and having a molecular mass of 22kDa. Growth Hormone is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GH protein lyophilized from a 0.2µm filtered concentrated solution containing mannitol, and glycine.

Purity

Greater than 96.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ was determined by the proliferation assay of rat lymphoma NB2-11 cells and was found to be less than 0.1ng/ml.

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGH should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized HGH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FPTIPLSRLF DNAMLRAHRL HQLAFDTYQE FEEAYIPKEQ KYSFLQNPQT SLCFSESIPT PSNREETQQK SNLELLRISL LLIQSWLEPV QFLRSVFANS LVYGASDSNV YDLLKDLEEG IQTLMGRLED GSPRTGQIFK QTYSKFDTNS HNDDALLKNY GLLYCFRKDM DKVETFLRIV QCRSVEGSCG F.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor Human Recombinant, Yeast

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-577

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
biological activity
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Description

Vascular Endothelial Growth Factor Human Recombinant produced in Yeast is a double, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 42 kDa.

Source

Pichia Pastoris.

Formulation

The protein contains 20mM Phosphate- Buffered Saline, pH 7.4.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Determined by its ability to stimulate 3H-Thymidine incorporation in human umbilical vein endothelial cells, the ED50 for this effect was found to be 2-6ng/ml.

More Info

Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered colorless liquid formulation.
Stability
Vascular Endothelial Growth Factor Human although stable at 15°C for 2 weeks, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glia Maturation Factor Beta Human Recombinant

Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

Product # :

CYT-565

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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purity
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Description

Glia Maturation Factor-Beta (GMF-Beta) Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.5 kDa. Glia Maturation Factor-Beta, GMF-Beta, Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GMF-beta protein was lyophilized after dialysis against 20mM PBS pH=7.4 and 130mM NaCl.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines.
Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMF-B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMF-beta should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GMFB in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.
Background
What is the molecular weight/Mw of GMFB HUMAN Protein?
GMFB HUMAN Protein has a total Mw of 16.5kDa.

What is the source or expression system of GMFB HUMAN Protein?
Escherichia Coli.

What is the Purity of GMFB HUMAN Protein?
GMFB HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GMFB HUMAN Protein?
The biological functionality of GMFB HUMAN Protein will be determined in the future.

What is the amino acid sequence of GMFB HUMAN Protein?
SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.

What applications can GMFB HUMAN Protein be used in?
GMFB HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GMFB HUMAN Protein?
The endotoxin level is minimal, GMFB HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor-E Recombinant (Orf Virus)

Product # :

CYT-263

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

A DNA sequence encoding the mature variant of ovVEGF-E isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020) was expressed in E. coli as a 132 amino acid residue fusion protein with an N-terminal His-tag sequence and a thrombin cleavage site. Recombinant VEGF-E homodimer was dimerized in vitro and has a predicted mass of approximately 35 kDa.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing PBS.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The biological activity was determined (1) by the ability to induce VEGFR-2/KDR receptor phosphorylation in PAE/KDR cells and (2) in a cell proliferation assay using primary HUVECs. The ED₅₀ for this effect is typically 1-5ng/ml.

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Introduction
Based on sequence similarity to VEGF-A, a gene encoding a VEGF homologue has recently been discovered in the genome of Orf virus (OV) (Lyttle et al., 1994). Different isolates of Orf virus show significant amino acid sequence similarity to VEGF-A and described as a viral virulence factor that appears to be derived from captured host genes. All eight cysteine residues of the central cysteine knot motif characteristic of members of the VEGF family are conserved among other residues in the VEGF-E proteins (Dehio et al., 1999; Wise et al., 1999). Alignment of all mammalian VEGF sequences indicated that VEGF-E is distinct from the previously described VEGFs but most closely related to VEGF-A. Like VEGF-A, VEGF-E was found to bind with high affinity to VEGF receptor-2 (KDR) resulting in receptor autophosphorylation, whilst in contrast to VEGF-A, VEGF-E can not bind to VEGF receptor-1 (Flt-1). Furthermore VEGF-E can also not bind to VEGF receptor-3 (FLT-4). Therefore VEGF-E is a potent angiog
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vascular Endothelial Growth Factor-E Orf Virus although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF E -OV should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
The lyophilized oVEGF-E Orf Virus should be reconstituted in water or medium to a concentration not lower than 50µg/ml. For long term storage we would recommend to add at least 0.1% human or bovine serum albumin.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH DSTKTWSEVF ENSGCKPRPM VFRVHDEHPE LTSQRFNPPC VTLMRCGGCC NDESLECVPT EEANVTMQLM GASVSGGNGM QHLSFVEHKK CDCKPPLTTT PPTTTRPPRR RR

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth and Differentiation Factor 15 Human Recombinant

GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

Product # :

CYT-335

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa. The GDF15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF15 is lyophilized from a sterile filtered solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GDF15 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
Background
What is the molecular weight/Mw of GDF15 HUMAN Protein?
GDF15 HUMAN Protein has a total Mw of 24.8kDa.

What is the source or expression system of GDF15 HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF15 HUMAN Protein?
GDF15 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 HUMAN Protein?
The biological functionality of GDF15 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GDF15 HUMAN Protein?
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.

What applications can GDF15 HUMAN Protein be used in?
GDF15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF15 HUMAN Protein?
The endotoxin level is minimal, GDF15 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor (120a.a.) Rat Recombinant, Yeast

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-1127

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Vascular Endothelial Growth Factor(120a.a.) Rat Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x121 amino acid polypeptide chains, having a molecular mass of approximately 18.5kDa each.VEGF is purified by proprietary chromatographic techniques.

Source

Saccharomyces cerevisiae

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 was measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells and was found to be 2‑10 ng/ml.

More Info

Introduction
Vascular endothelial growth factor is an important signaling protein involved in both angiogenesis and vasculogenesis.VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of VEGF is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in VEGF have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vascular Endothelial Growth Factor should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPTTEGEQK AHEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNVTMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKPR R.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Pro-Insulin Like Growth Factor-2 Human Recombinant

Pro-Insulin Like Growth Factor-2, pro-IGF2.

Product # :

CYT-110

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Pro-IGF2 Human Recombinant produced in HEK cells is a glycosylated monomer, contains 157 a.a. (24-180) having a total molecular weight of 25kDa.The Pro-IGF2 contains a C-terminal propeptide (E peptide) Arg92 to Lys180 and is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The Pro-IGF2 was lyophilized in 50mM Sodium Acetate pH 4.5 and 350mM NaCl.

Purity

Greater than 90% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of MCF-7 cells (human breast cancer cell line) and is typically 2-8ng/ml.

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Introduction
IGF-2 is a member of the insulin family of polypeptide growth factors that is involved in development and growth. It is an imprinted gene and is expressed only from the paternally inherited allele. It is a candidate gene for eating disorders. There is a read-through, INS-IGF2, which aligns to this gene at the 3' region and to the upstream INS gene at the 5' region. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.
Synonyms
Pro-Insulin Like Growth Factor-2, pro-IGF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Pro-IGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pro-IGF2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Pro-IGF2 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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