Search: 1000 results found for "glia maturation factor"

Description:

Growth and Differentiation Factor 15 Human Recombinant, His Tag

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-691

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Description

Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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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 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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.

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

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

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

What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.

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

What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 HUMAN, 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:

Epidermal Growth Factor Rat Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-669

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Description

Epidermal Growth Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6151 Dalton. The Rat EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Rat EGF was lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.

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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 Rat EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat 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 Rat EGF in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
Background
Pioneering Insights into Epidermal Growth Factor Rat Recombinant: Unraveling Signaling Dynamics and Therapeutic Implications
Abstract:
This research paper delves into the unexplored landscape of Epidermal Growth Factor Rat Recombinant (EGF-RR), delving into its intricate molecular attributes, signaling pathways, and potential therapeutic applications. By employing advanced methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the complex interplay between EGF-RR and cellular responses, offering a new perspective for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) holds a key role in cellular regulation. This paper navigates the intricacies of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and its potential therapeutic implications.
Protein Expression and Purification:
The paper delves into the meticulous engineering of EGF-RR, involving gene optimization for enhanced expression. Protein purification strategies, such as affinity chromatography, are employed to obtain highly purified EGF-RR for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Advanced receptor binding assays elucidate the interaction of EGF-RR with its cognate receptor. By quantifying binding affinities and kinetic rates, the study unveils the nuances of EGF-RR's engagement with its receptor, shedding light on potential structural determinants.
Cellular Signaling Pathways and Functional Responses:
Through in vitro cellular assays, the study unravels the intricate signaling pathways initiated by EGF-RR. Quantitative phosphoproteomic analyses expose the dynamic phosphorylation events triggered by EGF-RR, providing insights into its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Molecular Modeling:
Utilizing advanced bioinformatics tools, molecular dynamics simulations provide a deeper understanding of EGF-RR's interactions with its receptor and potential downstream effectors. Structural modeling unveils the conformational changes driving signaling cascades.
Therapeutic Prospects and Novel Avenues:
The molecular insights into EGF-RR's signaling dynamics open avenues for therapeutic exploration. Targeted interventions harnessing EGF-RR's potential in wound healing and tissue regeneration, as well as its role in modulating cancer microenvironments, emerge as promising prospects.
Challenges and Future Directions:
Despite progress, challenges such as deciphering context-dependent signaling responses remain. Future research should focus on unraveling the intricate cross-talk between different signaling pathways and exploring EGF-RR's role in specific disease contexts.
Conclusion:
In a convergence of advanced methodologies and visionary insights, Epidermal Growth Factor Rat Recombinant emerges as a captivating subject. Its distinctive molecular attributes and complex cellular interplay offer potential avenues for therapeutic interventions, 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 6.1kDa.

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

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

What is the Biological Activity of EGF RAT Protein?
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.

What is the amino acid sequence of EGF RAT Protein?
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.

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:

Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active

Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

Product # :

CYT-1057

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Description

TNFA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235 a.a) and having a molecular mass of 19.9kDa.TNFA Rat is expressed with an 25 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFA Rat protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D.
The ED50 for this effect is ≤ to 0.2 ng/ml.

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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
Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.
Physical Appearance
Sterile Filtered colorless liquid.
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 MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.
Background
Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active: An In-Depth Analysis
Abstract:

Tumor Necrosis Factor-alpha (TNF-α) is a cytokine that plays a significant role in various physiological and pathological processes. This human research paper provides an in-depth analysis of TNF-α Rat Recombinant with a His Tag, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the potential applications of TNF-α Rat Recombinant in human research.
Introduction:

TNF-α is a key mediator of inflammation and immune responses in humans. This research paper aims to provide a comprehensive analysis of TNF-α Rat Recombinant with a His Tag, highlighting its significance in human physiology and its potential applications in human research.
Structure and Function of TNF-α:

TNF-α is a homotrimeric protein that binds to two distinct receptors, TNFR1 and TNFR2, initiating downstream signaling cascades. It regulates immune cell activation, cytokine production, and cellular responses, influencing diverse biological processes.
Signaling Pathways:

Upon binding to its receptors, TNF-α activates various signaling pathways, including the NF-κB pathway, MAPK pathway, and cell death pathways. These pathways regulate gene expression and mediate cellular responses, impacting inflammation, apoptosis, and tissue homeostasis.
Functions of TNF-α:

TNF-α plays a crucial role in immune responses, inflammation, and tissue homeostasis. It regulates the activation and migration of immune cells, promotes cytokine production, and modulates cell survival and death. Dysregulation of TNF-α is implicated in the pathogenesis of various human diseases, making it an attractive target for research and therapeutic interventions.
Applications in Human Research:

TNF-α Rat Recombinant with a His Tag has diverse applications in human research. It can be used to investigate TNF-α signaling pathways, study its effects on immune cell functions, and explore its role in disease pathogenesis. Additionally, this recombinant protein can be utilized for in vitro and in vivo studies aimed at developing novel therapeutic strategies.
Future Directions:

Further research is necessary to unravel the intricate mechanisms of TNF-α signaling and its contributions to human diseases. Continued investigations will enable the development of targeted therapies and personalized medicine approaches. Future studies should also focus on optimizing the use of TNF-α Rat Recombinant in preclinical and clinical research settings.

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 Rabbit Recombinant

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

Product # :

CYT-427

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Description

Insulin-Like Growth Factor-I Rabbit Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 7639 Dalton.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (0.5mg/ml) solution with 0.02% NaHCO3.

Purity

Greater than 98.0% as determined by:(a) Gel-filtration chromatography under non denaturing conditions.(b) Analysis by SDS-PAGE.

Biological Activity

IGF-I is biologically active when compared to human IGF-1. The ED50, calculated by the dose -dependent proliferation of human MCF/7 cells is 5 to 25ng/ml in the cell culture mixture dependent on culture conditions. Its activity consists of 30-40 % compared to human IGF-1.

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Introduction
The 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. 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'. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A, and somatomedin B. IGF-1 is a small protein secreted mostly but not exclusively by the liver and circulating in blood mostly as a complex with several IGF binding proteins. It has growth-regulating, insulin-like, and mitogenic functions and it is secreted in response to growth hormone stimulation.
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Insulin-Like Growth Factor-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 rbIGF-I in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MTAGPETLCG AELVDALQFV CGDRGFYFNK PTGYGSSSRR APQTGIVDEC CFRSCDLRRL EMYCAPLKP

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 receptor-1 Human Recombinant, HEK Active

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-134

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Description

FLT1 Human Recombinant is a single, glycosylated polypeptide chain containing 535 amino acids (27-328a.a) and having a molecular mass of 60.3kDa (calculated). FLT1 is fused to a 233 amino acid hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293

Formulation

FLT1 protein solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 60ng/ml and is measured by its ability to inhibit proliferation using HUVEC human umbilical vein endothelial cells in the
presence of Human VEGF165.

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Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Physical Appearance
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.Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
SKLKDPELSL KGTQHIMQAG QTLHLQCRGE AAHKWSLPEM VSKESERLSI TKSACGRNGK QFCSTLTLNT AQANHTGFYS CKYLAVPTSK KKETESAIYI FISDTGRPFV EMYSEIPEII HMTEGRELVI PCRVTSPNIT VTLKKFPLDT LIPDGKRIIW DSRKGFIISN ATYKEIGLLT CEATVNGHLY KTNYLTHRQT NTIIDVQIST PRPVKLLRGH TLVLNCTATT PLNTRVQMTW SYPDEKNKRA SVRRRIDQSN SHANIFYSVL TIDKMQNKDK GLYTCRVRSG PSFKSVNTSV HILEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGK.
Background
VEGFR-1 (Vascular Endothelial Growth Factor Receptor-1), also known as Flt-1 (Fms-like tyrosine kinase 1), is a critical receptor involved in angiogenesis and vascular development. This research paper delves into the structure, function, and therapeutic implications of VEGFR-1, shedding light on its multifaceted role in various physiological and pathological processes.
VEGFR-1 is a transmembrane receptor tyrosine kinase belonging to the VEGF receptor family. It is primarily expressed on endothelial cells and plays a pivotal role in mediating the cellular responses to VEGF ligands. Upon ligand binding, VEGFR-1 initiates intracellular signaling cascades that regulate endothelial cell proliferation, migration, and survival, ultimately contributing to the formation of new blood vessels.
The structure of VEGFR-1 comprises distinct domains, including an extracellular ligand-binding domain, a transmembrane domain, and an intracellular tyrosine kinase domain. The extracellular domain facilitates the interaction between VEGF ligands and the receptor, while the intracellular domain transduces downstream signals by phosphorylating specific tyrosine residues.
VEGFR-1 exhibits not only ligand-dependent but also ligand-independent functions. In addition to its role as a VEGF receptor, it can act as a decoy receptor, sequestering VEGF and modulating the bioavailability of VEGF ligands. This unique property allows VEGFR-1 to regulate VEGF signaling and influence angiogenic processes.
The signaling pathways activated by VEGFR-1 are diverse and intricate, involving multiple downstream effectors, such as PI3K/AKT, MAPK/ERK, and STAT proteins. These pathways regulate endothelial cell behaviors, including proliferation, migration, and differentiation, which are crucial for angiogenesis. Perturbations in VEGFR-1 signaling have been implicated in various pathological conditions, including cancer, retinopathy, and inflammatory disorders.
The therapeutic targeting of VEGFR-1 has gained considerable attention for its potential in managing angiogenesis-related diseases. Inhibitors specifically designed to block VEGFR-1 have been developed to suppress aberrant angiogenesis and impede tumor growth. Moreover, VEGFR-1-based therapies have been explored for ocular diseases like wet age-related macular degeneration (AMD) and diabetic retinopathy, aiming to alleviate pathological neovascularization.
The availability of VEGFR-1 human recombinant proteins has facilitated in-depth research and the development of potential therapeutic interventions. Recombinant VEGFR-1 proteins serve as valuable tools for investigating VEGF-VEGFR-1 interactions, screening drug candidates, and elucidating the underlying molecular mechanisms of VEGFR-1-mediated signaling pathways.

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:

CDNF Rat Recombinant

Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.

Product # :

CYT-730

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Description

CDNF Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.8kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

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

Biological Activity

CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the 6-hydroxy (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF 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 CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.
Background
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.8kDa.

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

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

What is the Biological Activity of CDNF Protein?
CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

What is the amino acid sequence of CDNF Protein?
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.

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

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

MYDGF Mouse Recombinant, His Tag

D17Wsu104e, Il25, Ly6elg, MYDGF, Interleukin-25, IL-25, Stromal cell-derived growth factor SF20.

Product # :

CYT-1040

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sds-page

Description

MYDGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (25-166 a.a) and having a molecular mass of 18.1kDa. MYDGF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MYDGF protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

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Introduction
Myeloid-derived growth factor (Mydgf) is a paracrine-acting protein and a bone marrow-derived monocyte which stimulates cardiac myocyte survival and adaptive angiogenesis for cardiac protection and repair after myocardial infarction. Mydgf induces endothelial cell proliferation through a MAPK1/3-, STAT3- and CCND1-mediated signaling lane. When comparing wild-type mice to mice with a Mydgf-deficiency, the later develop larger infarct scars and more acute contractile dysfunction.
Synonyms
D17Wsu104e, Il25, Ly6elg, MYDGF, Interleukin-25, IL-25, Stromal cell-derived growth factor SF20.
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 MGSVSEPTTV PFDVRPGGVV HSFSQDVGPG NKFTCTFTYA SQGGTNEQWQ MSLGTSEDSQ HFTCTIWRPQ GKSYLYFTQF KAELRGAEIE YAMAYSKAAF ERESDVPLKS EEFEVTKTAV SHRPGAFKAE LSKLVIVAKA ARSEL.

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:

Oncostatin-M Mouse Recombinant

Oncostatin-M, OSM, OncoM.

Product # :

CYT-168

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Shipped at Room temp

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Description

OSM Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.4kDa.The OSM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of NIH-3T3 mouse embryonic fibroblast cells is < 1 ng/ml, corresponding to a specific activity of > 1.0×10⁶ units/mg.

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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
Synonyms
Oncostatin-M, OSM, OncoM.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NRGCSNSSSQ LLSQLQNQAN LTGNTESLLE PYIRLQNLNT PDLRAACTQH SVAFPSEDTL RQLSKPHFLS TVYTTLDRVL YQLDALRQKF LKTPAFPKLD SARHNILGIR NNVFCMARLL NHSLEIPEPT QTDSGASRST TTPDVFNTKI GSCGFLWGYH RFMGSVGRVF REWDDGSTRS 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:

Glutamate-Cysteine Ligase, Modifier Subunit Human Recombinant

Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.

Product # :

ENZ-636

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Description

GCLM Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (1-274) and having a molecular mass of 33.3kDa.GCLM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GCLM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Glutamate-cysteine ligase (GCLM) is the first rate limiting enzyme of glutathione synthesis. The GCLM enzyme is comprised of 2 subunits, a heavy catalytic subunit and a light regulatory subunit. GCLM deficiency is associated with some forms of hemolytic anemia.
Synonyms
Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.
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 MGSHMGTDSR AAKALLARAR TLHLQTGNLL NWGRLRKKCP STHSEELHDC IQKTLNEWSS QINPDLVREF PDVLECTVSH AVEKINPDER EEMKVSAKLF IVESNSSSST RSAVDMACSV LGVAQLDSVI IASPPIEDGV NLSLEHLQPY WEELENLVQS KKIVAIGTSD LDKTQLEQLY QWAQVKPNSN QVNLASCCVM PPDLTAFAKQ FDIQLLTHND PKELLSEASF QEALQESIPD IQAHEWVPLW LLRYSVIVKS RGIIKSKGYI LQAKRRGS.

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:

Hypoxia-Inducible Factor-1 Alpha (85 a.a.) Human Recombinant

Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

Product # :

PRO-258

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Description

HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-85 a.a.) and having a molecular mass of 11.8 kDa. The HIF1A is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HIF1A Human (0.25mg/ml) solution containing 20mM Tris buffer(pH 8.0), 20% glycerol, 1mM DTT, 0.2M NaCl and 1mM EDTA.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.
Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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 MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM RLTISYLRVR KLLDAGDLDI EDDMK.

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:

General Transcription Factor IIF, Polypeptide 2 Human Recombinant

General transcription factor IIF subunit 2, ATP-dependent helicase GTF2F2, General transcription factor IIF 30 kDa subunit, Transcription initiation factor IIF subunit beta, TFIIF-beta, Transcription initiation factor RAP30, GTF2F2, RAP30, BTF4, TF2F2, TFIIF.

Product # :

PRO-1093

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Description

GTF2F2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-249 a.a) and having a molecular mass of 30.5kDa (Molecular weight on SDS-PAGE will appear higher).GTF2F2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GTF2F2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.2M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
General Transcription Factor IIF Polypeptide 2 (GTF2F2) is a general transcription initiation factor which binds to RNA polymerase II and helps engage it in the initiation complex in collaboration with TFIIB. GTF2F2 promotes transcription elongation. GTF2F2 shows ATP-dependent DNA-helicase activity.
Synonyms
General transcription factor IIF subunit 2, ATP-dependent helicase GTF2F2, General transcription factor IIF 30 kDa subunit, Transcription initiation factor IIF subunit beta, TFIIF-beta, Transcription initiation factor RAP30, GTF2F2, RAP30, BTF4, TF2F2, TFIIF.
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 MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS SDKLSLEGIV VQRAECRPAA SENYMRLKRL QIEESSKPVR LSQQLDKVVT TNYKPVANHQ
YNIEYERKKK EDGKRARADK QHVLDMLFSA FEKHQYYNLK DLVDITKQPV VYLKEILKEI GVQNVKGIHK NTWELKPEYR HYQGEEKSD.

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 3 Human Recombinant, CHO

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-1259

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Description

TGFB3 Human Recombinant produced in CHO cells is a glycosylated, polypeptide homodimer chain containing 2x112 amino acids and having a total molecular mass of 25.0kDa. The TGFB3 is purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

TGFB3 was lyophilized from a concentrated solution containing 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

Purity

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

Biological Activity

The ED₅₀ as determined by its ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0 × 10⁷ units/mg.

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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Transforming Growth Factor-Beta 3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 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 TGFB3 in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Background
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are 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.

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:

Eukaryotic Translation Initiation Factor 3K (50-94 a.a.) Human Recombinant

PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.

Product # :

PRO-2833

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Description

The EIF3KHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The EIF3KHis-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 45 amino acid residues of the EIF3KHuman, 50-94 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized EIF3Kat -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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Eukaryotic Translation Initiation Factor 3K (EIF3K) is a part of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a few other subunits of the 40S ribosomal subunit and eIF3. EIF3K is found both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4. EIF3K is conserved among high eukaryotes, including mammals, plants and insects and is expressed in human tissues.

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:

Nerve Growth Factor Receptor Human Recombinant

Tumor necrosis factor receptor superfamily member 16, Gp80-LNGFR, Low affinity neurotrophin receptor p75NTR, Low-affinity nerve growth factor receptor, NGF receptor, p75 ICD, CD271.

Product # :

CYT-915

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Description

NGFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 230 amino acids (29-250 a.a.) and having a molecular mass of 24.6kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). NGFR is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Tumor necrosis factor receptor superfamily member 16 (NGFR) BELONGS TO the tumor necrosis factor receptor superfamily with an extensive pattern of expression in tissues such as the brain, liver, lung, and muscle. NGFR has a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, possibly by regulating RAB31 activity, and thus contributes to the regulation of insulin-dependent glucose uptake. NGFRs are low affinity receptors which can bind to NGF, BDNF, NT-3, and NT-4. NGFR mediates cell survival as well as cell death of neural cells.
Synonyms
Tumor necrosis factor receptor superfamily member 16, Gp80-LNGFR, Low affinity neurotrophin receptor p75NTR, Low-affinity nerve growth factor receptor, NGF receptor, p75 ICD, CD271.
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
KEACPTGLYT HSGECCKACN LGEGVAQPCG ANQTVCEPCL DSVTFSDVVS ATEPCKPCTE CVGLQSMSAP CVEADDAVCR CAYGYYQDET TGRCEACRVC EAGSGLVFSC QDKQNTVCEE CPDGTYSDEA NHVDPCLPCT VCEDTERQLR ECTRWADAEC EEIPGRWITR STPPEGSDST APSTQEPEAP PEQDLIASTV AGVVTTVMGS SQPVVTRGTT DNLEHHHHHH.

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:

GM-CSF Receptor Beta Human Recombinant

CSF2RB,Colony Stimulating Factor 2 Receptor, Beta, Low-Affinity (Granulocyte-Macrophage), GM-CSF/IL-3/IL-5 Receptor Common Beta Subunit, CDw131, IL3RB, SMDP5, IL5RB, Interleukin 3 Receptor/Granulocyte-Macrophage Colony Stimulating Factor 3 Receptor, Beta (High Affinity), Colony-Stimulating Factor-2 Receptor, Beta, Low-Affinity, GM-CSF/IL-3/IL-5 Receptor Common Beta-Chain, Cytokine Receptor Common Subunit Beta, CD131 Antigen, CD131.

Product # :

CYT-928

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sds-page

Description

CSF2RB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 435 amino acids (17-443 a.a) and having a molecular mass of 49.7kDa. CSF2RB is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CSF2RB protein solution (0.5mg/ml) containing Phosphate Buffered Saline(pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GM-CSF Receptor Beta, also known as CSF2RB is a member of the type I cytokine receptor family. CSF2RB is a high affinity receptor for interleukin-3, interleukin-5 as well as granulocyte-macrophage colony-stimulating factor. CSF2RB unique form of receptor assembly applies also to IL-3 and IL-5 receptors, providing a structural basis for understanding their activation mechanism which is essential for the development of therapeutics.
Synonyms
CSF2RB,Colony Stimulating Factor 2 Receptor, Beta, Low-Affinity (Granulocyte-Macrophage), GM-CSF/IL-3/IL-5 Receptor Common Beta Subunit, CDw131, IL3RB, SMDP5, IL5RB, Interleukin 3 Receptor/Granulocyte-Macrophage Colony Stimulating Factor 3 Receptor, Beta (High Affinity), Colony-Stimulating Factor-2 Receptor, Beta, Low-Affinity, GM-CSF/IL-3/IL-5 Receptor Common Beta-Chain, Cytokine Receptor Common Subunit Beta, CD131 Antigen, CD131.
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
WERSLAGAEE TIPLQTLRCY NDYTSHITCR WADTQDAQRL VNVTLIRRVN EDLLEPVSCD LSDDMPWSAC PHPRCVPRRC VIPCQSFVVT DVDYFSFQPD RPLGTRLTVT LTQHVQPPEP RDLQISTDQD HFLLTWSVAL GSPQSHWLSP GDLEFEVVYK RLQDSWEDAA ILLSNTSQAT LGPEHLMPSS TYVARVRTRL APGSRLSGRP SKWSPEVCWD SQPGDEAQPQ NLECFFDGAA VLSCSWEVRK EVASSVSFGL FYKPSPDAGE EECSPVLREG LGSLHTRHHC QIPVPDPATH GQYIVSVQPR RAEKHIKSSV NIQMAPPSLN VTKDGDSYSL RWETMKMRYE HIDHTFEIQY RKDTATWKDS KTETLQNAHS MALPALEPST RYWARVRVRT SRTGYNGIWS EWSEARSWDT ESVLPMWLEH HHHHH.
Background
Title: GM-CSF Receptor Beta Human Recombinant: A Key Receptor in Immunological Research
Abstract:

Granulocyte-macrophage colony-stimulating factor receptor beta (GM-CSF Rβ) is a crucial receptor involved in immune cell development and function. This research paper provides a comprehensive analysis of human recombinant GM-CSF Rβ, focusing on its production, characterization, and applications in immunological research. The paper discusses the significance of GM-CSF Rβ in immune cell signaling and its role in various immune-related disorders. Furthermore, it elucidates the potential therapeutic implications of recombinant GM-CSF Rβ in immunotherapy and highlights ongoing research in the field. The information presented in this paper aims to enhance the understanding of human recombinant GM-CSF Rβ and its utility as a research tool in immunological studies.
Introduction:

Granulocyte-macrophage colony-stimulating factor receptor beta (GM-CSF Rβ) is a high-affinity receptor that binds to granulocyte-macrophage colony-stimulating factor (GM-CSF). It plays a critical role in immune cell development, differentiation, and activation. Human recombinant GM-CSF Rβ, produced through genetic engineering techniques, enables researchers to investigate its biological functions and therapeutic potential.
Production and Characterization:

Recombinant GM-CSF Rβ is typically produced using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and binding affinity of the recombinant receptor.
Immunological Significance:

GM-CSF Rβ is expressed on various immune cells, including myeloid cells, dendritic cells, and macrophages. It plays a crucial role in cell signaling pathways, promoting cell proliferation, survival, and activation. The dysregulation of GM-CSF Rβ signaling has been implicated in autoimmune diseases, inflammatory disorders, and hematological malignancies. Recombinant GM-CSF Rβ provides a valuable tool for investigating these immune-related processes and deciphering the underlying mechanisms.
Therapeutic Implications:

The dysregulation of GM-CSF Rβ signaling in immune-related disorders has prompted the exploration of recombinant GM-CSF Rβ as a potential therapeutic target. Targeted therapies, such as monoclonal antibodies and small-molecule inhibitors, are being developed to modulate GM-CSF Rβ signaling and restore immune homeostasis. Ongoing research focuses on optimizing these therapeutic approaches and identifying novel treatment strategies.
Conclusion:

Human recombinant GM-CSF Rβ is a critical research tool in the field of immunology. Its production, characterization, and applications in immune cell signaling contribute to our understanding of immune responses and the development of novel therapeutics. Continued research and advancements in GM-CSF Rβ-based immunotherapy hold promise for improving treatment outcomes in various immune-related disorders.
What is the molecular weight/Mw of CD131 Protein?
CD131 Protein has a total Mw of 49.7kDa.

What is the source or expression system of CD131 Protein?
Sf9, Baculovirus cells.
What is the Purity of CD131 Protein?
CD131 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CD131 Protein?
The biological functionality of CD131 Protein will be determined in the future.

What is the amino acid sequence of CD131 Protein?
WERSLAGAEE TIPLQTLRCY NDYTSHITCR WADTQDAQRL VNVTLIRRVN EDLLEPVSCD LSDDMPWSAC PHPRCVPRRC VIPCQSFVVT DVDYFSFQPD RPLGTRLTVT LTQHVQPPEP RDLQISTDQD HFLLTWSVAL GSPQSHWLSP GDLEFEVVYK RLQDSWEDAA ILLSNTSQAT LGPEHLMPSS TYVARVRTRL APGSRLSGRP SKWSPEVCWD SQPGDEAQPQ NLECFFDGAA VLSCSWEVRK EVASSVSFGL FYKPSPDAGE EECSPVLREG LGSLHTRHHC QIPVPDPATH GQYIVSVQPR RAEKHIKSSV NIQMAPPSLN VTKDGDSYSL RWETMKMRYE HIDHTFEIQY RKDTATWKDS KTETLQNAHS MALPALEPST RYWARVRVRT SRTGYNGIWS EWSEARSWDT ESVLPMWLEH HHHHH.

What applications can CD131 Protein be used in?
CD131 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD131 Protein?
The endotoxin level is minimal, CD131 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:

Granulocyte Chemotactic Protein 2 (CXCL6) Human Recombinant

C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.

Product # :

CHM-025

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Description

GCP-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9kDa.

Source

Escherichia Coli.

Formulation

GCP-2 protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-50 ng/ml corresponding to a specific activity of 20,000-100,000 IU/mg.

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Introduction
Granulocyte Chemotactic Protein 2 (CXCL6), also known as GCP-2, is a Chemotactic for neutrophil granulocytes. GCP-2 signals through binding and activation of its receptors (CXCR1 and CXCR2). GCP-2 has strong antibacterial activity against Gram-positive and Gram-negative bacteria In addition to its chemotactic and angiogenic property.
Synonyms
C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GCP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCP-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 GCP-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VLTELRCTCL RVTLRVNPKT IGKLQVFPAG PQCSKVEVVA SLKNGKQVCL DPEAPFLKKV IQKILDSGNK KN.
Background
What is the molecular weight/Mw of CXCL6 HUMAN Protein?
CXCL6 HUMAN Protein has a total Mw of 7.9kDa.

What is the source or expression system of CXCL6 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL6 HUMAN Protein?
CXCL6 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL6 HUMAN Protein?
Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-50 ng/ml corresponding to a specific activity of 20,000-100,000 IU/mg.

What is the amino acid sequence of CXCL6 HUMAN Protein?
VLTELRCTCL RVTLRVNPKT IGKLQVFPAG PQCSKVEVVA SLKNGKQVCL DPEAPFLKKV IQKILDSGNK KN.

What applications can CXCL6 HUMAN Protein be used in?
CXCL6 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL6 HUMAN Protein?
The endotoxin level is minimal, CXCL6 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-8 Mouse Recombinant

Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.

Product # :

CYT-070

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Description

FGF-8 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids and having a molecular mass of 28.1kDa.The FGF-8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-8 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED50, as determined by the dose-dependent a cell proliferation assay using NR6R-3T3 mouse fibroblast cells is <25 ng/ml in the presence of 0.1 ug/ml heprin, corresponding to a specific activity of > 4.0×10⁴ units/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
Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.
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 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 28.1kDa.

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

What is the Purity of FGF8 Protein?
FGF8 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF8 Protein?
The ED50, as determined by the dose-dependent a cell proliferation assay using NR6R-3T3 mouse fibroblast cells is <25 ng/ml in the presence of 0.1 ug/ml heprin, corresponding to a specific activity of > 4.0×104 units/mg.

What is the amino acid sequence of FGF8 Protein?
QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.

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:

Transforming Growth Factor Beta 2 Human Recombinant

Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

Product # :

CYT-441

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Description

TGFB2 Human Recombinant produced in plants is a homodimeric polypeptide chain containing 2 x 118 amino acids and having a total molecular mass of 27.08kDa. The TGFB2 is fused to 6xHis Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Nicotiana benthamiana.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The biological activity of TGFB2 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 < 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

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Introduction
TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-β (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.
Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB2 Human 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 TGFB2 in sterile 18M-cm H2O not less than 1µg/40µl, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHHALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIH
EPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASAS
PCCVSQDLEPLTI LYYIGKTPKIEQLSNMIVKSCKCS.

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 Human Recombinant, Sf9

Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

Product # :

CYT-365

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Description

Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17353 Dalton.The FGF-basic is purified by proprietary chromatographic techniques.

Source

Baculovirus.

Formulation

The sterile protein solution (0.5mg/ml) contains 20mM Tris pH=7.9, 100mM KCl, 1mM DTT and 20% glycerol.

Purity

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

Biological Activity

The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

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Introduction
Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. 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
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Physical Appearance
Sterile Filtered liquid formulation.
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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ala-Gly-Ser-Ile.
Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.3kDa.

What is the source or expression system of FGF 2 Protein?
Baculovirus.

What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

What is the amino acid sequence of FGF 2 Protein?
FGF 2 Protein is composed from155 amino acids.

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

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

Osteoprotegerin Human Recombinant /Fc Chimera

TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

Product # :

CYT-266

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Description

Recombinant OPG produced in yeast contains 2x412 amino acid residues, including 180 residues from mature OPG (a.a 22-201) and 232 residues from the Fc protein of human IgG1, and has a calculated molecular mass of 109.6kDa.

Source

Pichia Pastoris.

Formulation

OPG was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 6.0, 150mM NaCl and 0.02 % Tween-80.

Purity

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

Biological Activity

The ED₅₀ as determined by neutralizing the stimulation of U937 cells is less tha10ng/ml, corresponding to a specific activity of > 1.0 × 10⁵IU/mg in the presence of 10ng/ml soluble Human RANKL (sRANKL).

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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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 Osteoprotegerin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
OPG 22-201 ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQKCGIDVTL
Fc232EPKSSDKTHT CPPCPAPEFE GAPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPTPIEKTISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK

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:

General Transcription Factor IIE, Polypeptide 2 Human Recombinant

General transcription factor IIE polypeptide 2 beta 34kDa, transcription initiation factor IIE subunit beta, TFIIE-beta, TF2E2, TFIIE-B.

Product # :

PRO-1107

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Description

GTF2E2 Human Recombinant produced in E. coli is a single polypeptide chain containing 315 amino acids (1-291) and having a molecular mass of 35.6kDa.GTF2E2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GTF2E2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 30% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
GTF2E2 is vital for transcription initiation by RNA polymerase II in conjunction with other general factors. General Transcription Factor IIE is a heterotetramer composed of two subunits of relatively high molecular mass 57,000 (GTF2E1) and two of 34,000 (GTF2E2). GTF2E2 is necessary in conjunction with GTF2E1 for transcription initiation. GTF2E2 recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIE and TFIIH are essential for promoter clearance by RNA polymerase.
Synonyms
General transcription factor IIE polypeptide 2 beta 34kDa, transcription initiation factor IIE subunit beta, TFIIE-beta, TF2E2, TFIIE-B.
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 MGSHMDPSLL RERELFKKRA LSTPVVEKRS ASSESSSSSS KKKKTKVEHG GSSGSKQNSD HSNGSFNLKA LSGSSGYKFG VLAKIVNYMK TRHQRGDTHP LTLDEILDET QHLDIGLKQK QWLMTEALVN NPKIEVIDGK YAFKPKYNVR DKKALLRLLD QHDQRGLGGI LLEDIEEALP NSQKAVKALG DQILFVNRPD KKKILFFNDK SCQFSVDEEF QKLWRSVTVD SMDEEKIEEY LKRQGISSMQ ESGPKKVAPI QRRKKPASQK KRRFKTHNEH LAGVLKDYSD ITSSK

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:

GDNF Family Receptor Alpha 1 Rat Recombinant

GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

Product # :

CYT-1012

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Description

GFRA1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 645 amino acids (25-430a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GFRA1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.
Synonyms
GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.
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
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
Background
What is the molecular weight/Mw of GFRA1 RAT Protein?
GFRA1 RAT Protein has a total Mw of 72.3kDa.

What is the source or expression system of GFRA1 RAT Protein?
Sf9, Baculovirus cells.

What is the Purity of GFRA1 RAT Protein?
GFRA1 RAT Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA1 RAT Protein?
The biological functionality of GFRA1 RAT Protein will be determined in the future.

What is the amino acid sequence of GFRA1 RAT Protein?
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

What applications can GFRA1 RAT Protein be used in?
GFRA1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA1 RAT Protein?
The endotoxin level is minimal, GFRA1 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:

Transforming Growth Factor Beta Receptor Associated Protein 1 Human Recombinant

TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.

Product # :

PRO-1890

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Description

TGFBRAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (601-860 a.a) and having a molecular mass of 33kDa.TGFBRAP1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TGFBRAP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
TGF-beta receptor-associated protein 1 also known as TGFBRAP1 takes part in the TGF-beta/activin signaling pathway. TGFBRAP1 is related with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. TGFBRAP1recruits SMAD4 to the vicinity of the receptor complex and smoothes the progress of its interaction with receptor-regulated Smads, such as SMAD2.
Synonyms
TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSKRLQ KEEYHTHLAV LYLEEVLLQR ASASGKGAEA TETQAKLRRL LQKSDLYRVH FLLERLQGAG LPMESAILHG KLGEHEKALH ILVHELQDFA AAEDYCLWCS EGRDPPHRQQ LFHTLLAIYL HAGPTAHELA VAAVDLLNRH ATEFDAAQVL QMLPDTWSVQ LLCPFLMGAM RDSIHARRTM QVALGLARSE NLIYTYDKMK LKGSSIQLSD KKLCQICQNP FCEPVFVRYP NGGLVHTHCA ASRHTNPSSS SPGTRT

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 2 Fusion Protein Human Recombinant

Tumor necrosis factor receptor superfamily member 1B,Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b antigen, Etanercept, TBPII, TNFBR, TNFR80, TNF-R75, p75TNFR, TNF-R-II.

Product # :

CYT-422

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Quantity :

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Description

Recombinant Human Tumor Necrosis Factor Receptor 2 Fusion Protein produced in CHO is a dimeric, glycosylated, polypeptide chain consisting of the extracellular ligand-binding portion of the human 75 kilo Dalton (p75) tumor necrosis factor receptor 2 (TNFR2) linked to the Fc portion of human IgG1. The Fc component of TNFR2 contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. It consists of 934 amino acids and has an apparent molecular weight of approximately 150 kilo Daltons.The TNFR2 is purified by standard chromatographic techniques.

Source

Chinese Hamster Ovarian Cells (CHO).

Formulation

Each mg contains 1.6mg mannitol, 0.4 mg sucrose and 48 µg tromethamine.

Purity

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

Biological Activity

Potency is determined by its ability to neutralize TNF-alpha mediated growth inhibition of A375 cells, corresponding to a Specific Activity of 17,000,000 IU/mg.

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Introduction
TNFR binds specifically to tumor necrosis factor (TNF) and blocks its interaction with cell surface TNF receptors. TNF is a naturally occurring cytokine that is involved in normal inflammatory and immune responses. It plays an important role in the inflammatory processes of rheumatoid arthritis (RA), polyarticular-course juvenile rheumatoid arthritis (JRA), and ankylosing spondylitis and the resulting joint pathology. In addition, TNF plays a role in the inflammatory process of plaque psoriasis. Elevated levels of TNF are found in involved tissues and fluids of patients with RA, psoriatic arthritis, ankylosing spondylitis (AS), and plaque psoriasis. Two distinct receptors for TNF (TNFRs), a 55 kilodalton protein (p55) and a 75 kilodalton protein (p75), exist naturally as monomeric molecules on cell surfaces and in soluble forms. Biological activity of TNF is dependent upon binding to either cell surface TNFR. Recombinant Human TNFR is a dimeric soluble form of the p75 TNF receptor that can bind to two TNF molecules.
It inhibits the activity of TNF in vitro and has been shown to affect several animal models of inflammation, including murine collagen-induced arthritis. TNFR inhibits binding of both TNF? and TNF? (lymphotoxin alpha [LT?]) to cell surface TNFRs, rendering TNF biologically inactive. Cells expressing transmembrane TNF that bind to TNFR are not lysed in vitro in the presence or absence of complement.
TNFR can also modulate biological responses that are induced or regulated by TNF, including expression of adhesion molecules responsible for leukocyte migration (i.e., E-selectin and to a lesser extent intercellular adhesion molecule-1 [ICAM-1]), serum levels of cytokines (e.g., IL-6), and serum levels of matrix metalloproteinase-3 (MMP-3 or stromelysin).
Synonyms
Tumor necrosis factor receptor superfamily member 1B,Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b antigen, Etanercept, TBPII, TNFBR, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor Receptor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFR2 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 TNFR2 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.

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