Search: 1000 results found for "Neurotrophic factors"

Description:

TRAF Family Member-Associated NFKB Activator Human Recombinant

TRAF, TRAF2, TRAF-interacting protein, ITRAF.

Product # :

PRO-1348

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Description

TANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 448 amino acids (1-425a.a) and having a molecular mass of 50.2kDa. TANK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TANK protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
TRAF Family Member-Associated NFKB Activator (TANK) is located in the cytoplasm and binds Either TRAF1, TRAF2 or TRAF3. TANK is an inhibitor of TRAF function which regulates TRAF protein activity via sequestering TRAFs in a dormant position in the cytoplasm. Overexpression of TANK, inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and also inhibits LMP1-mediated NFkappa-B activation by blocking the connection of TRAF2 with LMP1.
Synonyms
TRAF, TRAF2, TRAF-interacting protein, ITRAF.
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 MGSMDKNIGE QLNKAYEAFR QACMDRDSAV KELQQKTENY EQRIREQQEQ LSLQQTIIDK LKSQLLLVNS TQDNNYGCVP LLEDSETRKN NLTLDQPQDK VISGIAREKL PKVRRQEVSS PRKETSARSL GSPLLHERGN IEKTFWDLKE EFHKICMLAK AQKDHLSKLN IPDTATETQC SVPIQCTDKT DKQEALFKPQ AKDDINRGAP SITSVTPRGL CRDEEDTSFE SLSKFNVKFP PMDNDSTFLH STPERPGILS PATSEAVCQE KFNMEFRDNP GNFVKTEETL FEIQGIDPIA SAIQNLKTTD KTKPSNLVNT CIRTTLDRAA CLPPGDHNAL YVNSFPLLDP SDAPFPSLDS PGKAIRGPQQ PIWKPFPNQD SDSVVLSGTD SELHIPRVCE FCQAVFPPSI TSRGDFLRHL NSHFNGET.

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 Related Protein Rat Recombinant

VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L.

Product # :

CYT-262

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Description

Vascular Endothelial Growth Factor C Rat Recombinant contains 127 amino acids residues and was fused to a His- tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 15-20 kDa protein in SDS-PAGE under reducing conditions.

Source

Sf9, Insect Cells.

Formulation

Each mg of VEGF-C Rat contains 50mg BSA and PBS as buffer.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to stimulate phosphorylation of the VEGFR-3/FLT-4 receptor in porcine aortic endothelial cells. The ED50 for this effect is typically 200-300ng/ml corresponding to a Specific Activity of 3,334-5,000IU/mg.

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Introduction
VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. The rat VEGFC cDNA encodes a pre-pro-protein of 416 amino acids residues.
It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant rat VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT -4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant rat VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.
Synonyms
VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vascular Endothelial Growth Factor-C although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-C 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 C in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DTVKLAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGAATNTFFKP PCVSVYRCGGCCNSEGLQCMNTSTGYLSKTLFEITVPLSQGPKPVTISFA NHTSCRCMSKLDVYRQVHSIIHHHHHH.

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:

Stem Cell Factor Rat Recombinant

Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.

Product # :

CYT-323

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Description

Stem cell factor Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (26-189) and having a molecular mass of 18.4 kDa.The Rat SCF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.

Purity

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

Biological Activity

The ED50 is determined by the dose-dependant stimulation of the proliferation of human TF-1 cells which is < 10 ng/ml, corresponding to a specific activity of 100,000units/mg.

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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117 (c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized rat SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 SCF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQEICRNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV THLSVSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVAC MEENAPKNVK ESLKKPETRN FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.

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:

NTF2-like Export Factor 1 Human Recombinant

NTF2-like export factor 1, MTR2, Protein P15, NTF2-related export protein 1, NUTF-like export factor 1, NTX2-like export factor1.

Product # :

PRO-218

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Description

NXT1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140a.a.) and having a molecular mass of 18.0kDa. The NXT1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NXT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol and 0.1M NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
NXT1 operates as a nuclear export factor in both RAN and CRM1 dependent pathways. NXT1 is known to stimulate the export of U1 snRNA in RAN (Ras-related nuclear protein) and CRM1 (chromosome region maintenance) dependent pathways and the export of tRNA and mRNA in a CRM1-independent pathway. This protein heterodimerizes with Tap protein and regulates the ability of Tap protein to intermediate nuclear mRNA export.
Synonyms
NTF2-like export factor 1, MTR2, Protein P15, NTF2-related export protein 1, NUTF-like export factor 1, NTX2-like export factor1.
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 MASVDFKTYV DQACRAAEEF VNVYYTTMDK RRRLLSRLYM GTATLVWNGN AVSGQESLSE FFEMLPSSEF QISVVDCQPV HDEATPSQTT VLVVICGSVK FEGNKQRDFN QNFILTAQAS PSNTVWKIAS DCFRFQDWAS.

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

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

Product # :

CYT-392

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Description

Vascular Endothelial Growth Factor Rat Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38,750 Dalton. The VEGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 10mM NaP, pH 7.5.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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 4.0-8.0 ng/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 Vascular Endothelial Growth Factor 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 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:

Neuropilin 1 Human Recombinant

Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.

Product # :

CYT-1059

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Description

NRP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856a.a.) and having a molecular mass of 94.8kDa. (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NRP1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
NRP1 is a coreceptor bound on membranes to tyrosine kinase receptors for semaphorin family proteins and endothelial growth factors, it is a type one transmembrane protein. Neuropilin-1 takes part in cell survival, angiogenesis, invasion, migration, and axon guidance. the protein is a potential target for cancer therapies as it interacts with VEGF (co-receptor).
Synonyms
Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.
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
FRNDKCGDTI KIESPGYLTS PGYPHSYHPS EKCEWLIQAP DPYQRIMINF NPHFDLEDRD CKYDYVEVFD GENENGHFRG KFCGKIAPPP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TTPSGVIKSP GFPEKYPNSL ECTYIVFAPK MSEIILEFES FDLEPDSNPP
GGMFCRYDRL EIWDGFPDVG PHIGRYCGQK TPGRIRSSSG ILSMVFYTDS AIAKEGFSAN YSVLQSSVSE DFKCMEALGM ESGEIHSDQI TASSQYSTNW SAERSRLNYP ENGWTPGEDS YREWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYKID VSSNGEDWIT IKEGNKPVLF
QGNTNPTDVV VAVFPKPLIT RFVRIKPATW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITSSN QGDRNWMPEN IRLVTSRSGW ALPPAPHSYI NEWLQIDLGE EKIVRGIIIQ GGKHRENKVF MRKFKIGYSN NGSDWKMIMD DSKRKAKSFE GNNNYDTPEL RTFPALSTRF
IRIYPERATH GGLGLRMELL GCEVEAPTAG PTTPNGNLVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTVIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDNHVQL KWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQNSAHC MTFWYHMSGS HVGTLRVKLR
YQKPEEYDQL VWMAIGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PADLDKKNPE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH.

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:

Epidermal Growth Factor Rat

Urogastrone, URG, EGF.

Product # :

CYT-556

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Description

Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Adult Male Rat Submandibular Glands.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

Purity

Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential
Abstract:
This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.
Protein Expression and Purification:
The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.
Cellular Signaling Pathways and Responses:
In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Structural Modeling:
Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.
Therapeutic Implications and Future Prospects:
EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.
Challenges and Future Directions:
Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.
Conclusion:
A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.15kDa.

What is the source or expression system of EGF RAT Protein?
Adult Male Rat Submandibular Glands.

What is the Purity of EGF RAT Protein?
EGF RAT Protein is >99% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of EGF RAT Protein?
EGF RAT Protein is composed from 53 amino acids.

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

What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT 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:

Neuronal Regeneration Related Protein Human Recombinant

Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.

Product # :

PRO-1780

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Description

NREP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (1-68) and having a molecular mass of 10.3kDa.NREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NREP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Neuronal Regeneration Related Protein (NREP) has roles in neural function. NREP promotes axonal regeneration. In addition, NREP has functions in cellular differentiation. NREP protein induces differentiation of fibroblast into myofibroblast and increases retinoic-acid regulation of lipid-droplet biogenesis. NREP down-regulates the expression of TGFB1 and TGFB2 but not of TGFB3. NREP has a role in the regulation of alveolar generation.
Synonyms
Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.
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 MGSMVYYPEL FVWVSQEPFP NKDMEGRLPK GRLPVPKEVN RKKNDETNAA SLTPLGSSEL RSPRISYLHF 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:

Cardiotrophin-1 Rat Recombinant

Cardiotrophin-1, CT-1, Ctf1.

Product # :

CYT-199

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Description

Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×10⁶ units/mg.

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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat 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 CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.

What is the source or expression system of CTF1 Protein?
Escherichia Coli.

What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.

What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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:

TRAF Family Member-Associated NFKB Activator Human Recombinant (1-119 a.a.)

TRAF2, I-TRAF, TANK, TRAF family member-associated NF-kappa-B activator, TRAF-interacting protein, ITRAF.

Product # :

PRO-685

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Description

TANK produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (1-119 a.a.) and having a molecular mass of 13.6 kDa.TANK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TANK protein solution contains 20mM Tris, pH-8.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TRAF2 protein is related with transduce signals from members of the TNFR superfamily. TRAF2 is located in the cytoplasm binds to TRAF1, TRAF2, or TRAF3, thus inhibiting TRAF function by sequestering the TRAFs in a suppressed state in the cytoplasm. Overexpression of TANK inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and inhibits LMP1-mediated NF-kappa-B activation by blocking the association of TRAF2 with LMP1. TRAF2 is necessary for the cellular response to TNF-alpha by connecting upstream signalling molecules to the IKKs and p65.
Synonyms
TRAF2, I-TRAF, TANK, TRAF family member-associated NF-kappa-B activator, TRAF-interacting protein, ITRAF.
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
MDKNIGEQLN KAYEAFRQAC MDRDSAVKEL QQKTENYEQR IREQQEQLSL QQTIIDKLKS QLLLVNSTQD NNYGCVPLLE DSETRKNNLT LDQPQDKVIS GIAREKLPKV DIASAESSI.

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:

HVEM Mouse Recombinant

Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

Product # :

CYT-1145

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Description

TNFRSF14 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 407 amino acids (39-206 aa) and having a molecular mass of 45.3kDa.TNFRSF14 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The TNFRSF14 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Herpesvirus entry mediator or HVEM or tumour necrosis factor receptor superfamily member 14 or TNFRSF14, is part of the TNF receptors family that is a receptor located on the cell surface. The cytoplasmic area of this receptor can bind all sorts of TNF receptor associated factor (TRAF) protein. Those proteins can mediate pathways activating an immune response. The MITF is regulating TNFRSF14 gene expression.
Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
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
QPSCRQEEFL VGDECCPMCN PGYHVKQVCS EHTGTVCAPC PPQTYTAHAN GLSKCLPCGV
CDPDMGLLTW QECSSWKDTV CRCIPGYFCE NQDGSHCSTC LQHTTCPPGQ RVEKRGTHDQ
DTVCADCLTG TFSLGGTQEE CLPWTNCSAF QQEVRRGTNS TDTTCSSQLE PKSCDKTHTC
PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN
AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP
QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL
YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH

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:

Chromosome 19 Open Reading Frame 80 Mouse Recombinant

Betatrophin, Angiopoietin-like protein 8, Lipasin, Refeeding-induced fat and liver protein, Gm6484, Angptl8, Rifl, EG624219.

Product # :

PRO-1576

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Quantity :

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Description

C19ORF80 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 16-198) containing 193 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 21.8kDa (calculated).

Source

Escherichia Coli.

Formulation

C19ORF80 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer, pH-4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.
Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, Refeeding-induced fat and liver protein, Gm6484, Angptl8, Rifl, EG624219.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASVRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYRA TEARLTEAGH SLGLYDRALE FLGTEVRQGQ DATQELRTSL SEIQVEEDAL HLRAEATARS LGEVARAQQA LRDTVRRLQV QLRGAWLGQA HQEFETLKAR ADKQSHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHTAA LPA.

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:

Neurexophilin 1 Human Recombinant

Nbla00697, NPH1, Neurexophilin-1, NXPH1.

Product # :

PRO-1859

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Description

NXPH1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 273 amino acids (22-271) and having a molecular mass of 31kDa. NXPH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NXPH1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Neurexophilin 1 (NXPH1) is a part of the neurexophilin family which encodes a secreted protein with a variable N terminal domain, an extremely conserved, N-glycosylated central domain, a short linker region, and a cysteine-rich Cterminal domain. NXPH1 shapes a very tight complex with alpha neurexins, a group of proteins which promote adhesion among dendrites and axons.
Synonyms
Nbla00697, NPH1, Neurexophilin-1, NXPH1.
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. 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 MGSANLTNGG KSELLKSGSS KSTLKHIWTE SSKDLSISRL LSQTFRGKEN DTDLDLRYDT PEPYSEQDLW DWLRNSTDLQ EPRPRAKRRP IVKTGKFKKM FGWGDFHSNI KTVKLNLLIT GKIVDHGNGT FSVYFRHNST GQGNVSVSLV PPTKIVEFDL AQQTVIDAKD SKSFNCRIEY EKVDKATKNT LCNYDPSKTC YQEQTQSHVS WLCSKPFKVI CIYISFYSTD YKLVQKVCPD YNYHSDTPYF PSG.

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:

Multiple Coagulation Factor Deficiency 2 Human Recombinant

SDNSF, LMAN1IP, Multiple coagulation factor deficiency protein 2, Neural stem cell-derived neuronal survival protein, MCFD2, F5F8D, DKFZp686G21263.

Product # :

PRO-769

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Description

MCFD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (27-146 a.a.) and having a molecular wieght of 15.1kDa. The MCFD2 is is fused to 16 a.a. T7-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MCFD2 protein solution contains 20mM Tris-HCl, pH-7.5, 100mM NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The MCFD2-LMAN1 complex forms an explicit cargo receptor for the ER-to-Golgi transport of selected proteins. MCFD2 is involved in the secretion of coagulation factors. MCFD2 is expressed by neural stem/progenitor cells of the hippocampus, and localized to region where neurogenesis persists throughout life. MCFD2 prevents NSC cell death and maintains stem cell characteristics. MCFD2 forms a complex with LAMN1 that facilitates the transport of coagulation factors V and VIII from the endoplasmic reticulum to the Golgi apparatus through an endoplasmic reticulum Golgi intermediate compartment. Mutations in the MCFD2 cause Factor V and Factor VIII combined deficiency.
Synonyms
SDNSF, LMAN1IP, Multiple coagulation factor deficiency protein 2, Neural stem cell-derived neuronal survival protein, MCFD2, F5F8D, DKFZp686G21263.
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
MASMTGGQQM GRGSHMEEPA ASFSQPGSMG LDKNTVHDQE HIMEHLEGVI NKPEAEMSPQ ELQLHYFKMH DYDGNNLLDG LELSTAITHV HKEEGSEQAP LMSEDELINI IDGVLRDDDK NNDGYIDYAE FAKSLQ.

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:

Hepatoma-Derived Growth Factor (32-285 a.a) Human Recombinant

Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.

Product # :

CYT-294

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SDS-PAGE

Description

HGF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (32-285 a.a.) and having a molecular mass of 29.8kDa. HGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HGF protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.
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
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein has a total Mw of 29.8kDa.

What is the source or expression system of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
Escherichia Coli.

What is the Purity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
What is the molecular weight/Mw of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein has a total Mw of 29.8kDa. What is the source or expression system of HGF (32-285) HUMAN Protein? Escherichia Coli. What is the Purity of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE. What is the Biological Activity of HGF (32-285) HUMAN Protein? The biological functionality of HGF (32-285) HUMAN Protein will be determined in the future. What is the amino acid sequence of HGF (32-285) HUMAN Protein? MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET. What applications can HGF (32-285) HUMAN Protein be used in? HGF (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for HGF (32-285) HUMAN Protein? The endotoxin level is minimal, HGF (32-285) HUMAN Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.

What applications can HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein be used in?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR (32-285) 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:

Fibroblast Growth Factor-basic Rat Recombinant

HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b, Fibroblast Growth Factor-basic, Basic fibroblast growth factor, bFGF, Heparin-binding growth factor 2.

Product # :

CYT-608

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Description

bFGF Rat Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.4 kDa.The bFGF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-b was lyophilized from 1mg/ml solution after extensive dialysis against 10mM Na2PO4, pH 7.5 and 50mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ range as determined by the dose-dependant proliferation of NR6R-3T3 cells was found to be 0.903ng/ml, corresponding to a specific activity of 1.1x10⁷units/mg.

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Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG (CUG) initiation codons resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. there are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b, Fibroblast Growth Factor-basic, Basic fibroblast growth factor, bFGF, Heparin-binding growth factor 2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat bFGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat FGF-2 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 Rat bFGF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPALPEDGGGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHV KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTEE CFFFERLESN NYNTYRSRKY SSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS.
Background
What is the molecular weight/Mw of FGF 2 RAT Protein?
FGF 2 RAT Protein has a total Mw of 16.4kDa.

What is the source or expression system of FGF 2 RAT Protein?
Escherichia Coli.

What is the Purity of FGF 2 RAT Protein?
FGF 2 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 2 RAT Protein?
The ED50 range as determined by the dose-dependant proliferation of NR6R-3T3 cells was found to be 0.903ng/ml, corresponding to a specific activity of 1.1x107 units/mg.

What is the amino acid sequence of FGF 2 RAT Protein?
MPALPEDGGGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHV KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTEE CFFFERLESN NYNTYRSRKY SSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS.

What applications can FGF 2 RAT Protein be used in?
FGF 2 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 2 RAT Protein?
The endotoxin level is minimal, FGF 2 RAT 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:

Tumor Necrosis Factor Receptor Type 2 Human Recombinant

Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, TNFRSF1B, TNFBR, TNFR2.

Product # :

CYT-769

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Description

TNFR2 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 20kDa. The TNFR2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFR2 was Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by its ability to inhibit the TNF-a mediated cytotoxicity in the L-929 cells is less than 0.2µg/ml, corresponding to a specific activity of > 5000IU/mg in the presence of 0.25ng/mL of rHuTNF-a.

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Introduction
TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, TNFRSF1B, TNFBR, TNFR2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFR2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TNFR2 should be stored at 4C between 2-7 days and for future use below -18C. 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 TNFR2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPAQVAFTPY APEPGSTCRL REYYDQTAQM CCSKCSPGQH AKVFCTKTSD TVCDSCEDST YTQLWNWVPE CLSCGSRCSS DQVETQACTR EQNRICTCRP GWYCALSKQE GCRLCAPLRK CRPGFGVARP GTETSDVVCK PCAPGTFSNT TSSTDICRPH QICNVVAIPG NASMDAVCTS TSPT.

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:

Neuroglobin Human Recombinant, His Tag

NGB.

Product # :

CYT-1030

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Description

Neuroglobin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (1-151a.a) and having a molecular mass of 18kDa. NGB is fused to 10 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NGB is Filtered (0.4μm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Neuroglobin, 151 amino acid residue protein, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O (2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. Moreover, neuroglobin may be a novel oxidative stress-responsive sensor for signal transduction in the brain. Neuroglobin expression is increased by neuronal hypoxia in vitro and focal cerebral ischemia in vivo, and neuronal survival after hypoxia is reduced by inhibiting neuroglobin expression with an antisense oligodeoxynucleotide and enhanced by neuroglobin overexpression.
Synonyms
NGB.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Neuroglobin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS MERPEPELIR QSWRAVSRSP LEHGTVLFAR LFALEPDLLP LFQYNCRQFS SPEDCLSSPE FLDHIRKVML VIDAAVTNVE DLSSLEEYLA SLGRKHRAVG VKLSSFSTVG ESLLYMLEKC LGPAFTPATR AAWSQLYGAV VQAMSRGWDG E.

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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SDS-PAGE

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:

Trefoil Factor-3 Rat Recombinant

Trefoil factor 3, Intestinal trefoil factor, rITF, Polypeptide P1.B, rP1.B, Tff3, Itf.

Product # :

CYT-781

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Description

The Trefoil Factor-3 Rat was constructed as a recombinant protein with a 9 a.a C-terminal fusion of Flag-Tag (1 aa N-terminal+8 aa C-terminal). The TFF3 Rat produced in E.coli, is 7.7kDa protein containing a total of 68 amino acid residues.

Source

Escherichia Coli.

Formulation

TFF3 protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM TRIS and 50mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains. TFF3 induces ciliogenesis and promotes airway epithelial ciliated cell differentiation, relatively through an epidermal growth factor receptor-dependent pathway. TFF3 overexpression is crucial for progression in mouse and human hepatocellular carcinogenesis. TFF-3 is normally expressed in hepatocellular carcinoma and its expression associates with tumor grade.
Synonyms
Trefoil factor 3, Intestinal trefoil factor, rITF, Polypeptide P1.B, rP1.B, Tff3, Itf.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MQEFVGLSPS QCMVPANVRV DCGYPTVTSE QCNNRGCCFD SSIPNVPWCF KPLQETECT F DYKDDDDK.

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 Human Recombinant

TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265

Product # :

CYT-734

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Quantity :

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Shipped at Room temp

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Description

RANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.1kDa. The RANK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH 8.0 and 150mM NaCl.

Purity

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

Biological Activity

The ED₅₀ as determined by its ability to inhibit sRANK Ligand induced nuclear factor kappa B (NFkappaB) in RAW 264.7 cells is less than 50 ng/ml, corresponding to a specific activity of
> 2.0 × 10⁴ IU/mg in the presence of 15 ng/ml of recombinant sRANK Ligand.

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Introduction
sRANK Receptor is a part of of the TNF superfamily of ligands and receptors which participates in the regulation of specific immunity and bone turnover. sRANK Receptor was originally acknowledged as a dendritic-cell-membrane protein, which by interacting with RANKL augments the capacity of dendritic cells to stimulate naive T cell proliferation and to endorse the survival of RANK and T cells. The full length human RANK cDNA encodes a type I transmembrane protein of 616 amino acids with a predicted 183 amino acid extracellular domain and a 383 amino acid cytoplasmic domain. sRANK Receptor is also expressed in a various tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.
Synonyms
TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized RANK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANK Receptor 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 RANK in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QIAPPCTSEK HYEHLGRCCN KCEPGKYMSS KCTTTSDSVC LPCGPDEYLD SWNEEDKCLL HKVCDTGKAL VAVVAGNSTT PRRCACTAGY HWSQDCECCR RNTECAPGLG AQHPLQLNKD TVCKPCLAGY FSDAFSSTDK CRPWTNCTFL GKRVEHHGTE KSDAVCSSSL PARK.

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:

Fibroblast Growth Factor-8 Mouse Recombinant, 194 a.a.

FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

Product # :

CYT-840

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

FGF 8 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 5mM Na3PO4 and 50 mM NaCl, pH 7.5.

Purity

Greater than 97.0% as determined by analysis by SDS-PAGE.

Biological Activity

The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

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Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF 8 although stable at room temperature for 3 weeks, should be stored desiccated below -18?C. Upon reconstitution FGF 8 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 FGF 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 22.5kDa.

What is the source or expression system of FGF8 Protein?
Escherichia Coli.

What is the Purity of FGF8 Protein?
FGF8 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF8 Protein?
The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

What is the amino acid sequence of FGF8 Protein?
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR

What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 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:

Macrophage-Colony Stimulating Factor Mouse Recombinant

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

Product # :

CYT-439

Price :

Quantity :

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Shipped at Room temp

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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:

Tumor Necrosis Factor-Alpha Mouse Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-252

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

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.
(c) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000Units/mg.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 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 calibrated solution of TNF-a 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.

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Formulation

Purity

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Formulation

Purity

Biological Activity

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Formulation

Purity

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Source

Formulation

Purity

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Source

Formulation

Purity

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