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1000 results found for “fibroblast growth factor”
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Name :
SF20 HumanDescription:
MYDGF Human Recombinant
C19orf10, Interleukin-25, IL-25, IL25, IL27, IL-27, IL27w, IL-27w, Stromal cell-derived growth factor SF20, UPF0556 protein C19orf10, chromosome 19 open reading frame 10.
Product # :
CYT-622Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
SF20 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 162 amino acids fragment (33-173) and having a total molecular mass of 18 kDa. C9orf10 is fused to 20 amino acids His tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
C9orf10 is supplied in 20mM Tris HCL pH-8 and 20% glycerol.
Purity
Greater than 95.0% by SDS-PAGE.
sds-page
More Info
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Introduction
SF20 plays a role in proliferation of lymphoid cells and is considered an interleukin. SF20 was initially identified as a product of bone marrow-derived stromal cells.
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Synonyms
C19orf10, Interleukin-25, IL-25, IL25, IL27, IL-27, IL27w, IL-27w, Stromal cell-derived growth factor SF20, UPF0556 protein C19orf10, chromosome 19 open reading frame 10.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CNPY1 HumanDescription:
Canopy FGF Signaling Regulator 1 Human Recombinant
Protein canopy homolog 1, CNPY1.
Product # :
PRO-1872Price :
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Description
CNPY1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids (1-92 a.a) and having a molecular mass of 13.3kDa. CNPY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNPY1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Canopy FGF Signaling Regulator 1, also known as CNPY1, is expressed in the midbrain-hindbrain (MHB) boundary in zebrafish. CNPY1, which binds FGFR1, also takes part in FGF signaling.
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Synonyms
Protein canopy homolog 1, CNPY1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNDYKLE EDPVTKERTF KRFAPRKGDK IYQEFKKLYF YSDAYRPLKF ACETIIEEYE DEISSLIAQE THYLADKLCS EKSDLCETSA NHTEL.
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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Name :
CFB Human, Sf9Description:
Complement Factor B Human Recombinant, Sf9
CFB, AHUS4, ARMD14, BF, BFD, CFAB, CFBD, FB, FBI12, GBG, H2-Bf, PBF2, Complement Factor B, B-Factor, Properdin, Properdin Factor B, C3/C5 Convertase, EC 3.4.21.47, PBF2,Glycine-Rich Beta-Glycoprotein, Glycine-Rich Beta Glycoprotein, C3 Proaccelerator, C3 Proactivator , EC 3.4.2, FBI12, H2-Bf.
Product # :
PRO-2403Price :
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Description
CFB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 245 amino acids (26-259a.a.) and having a molecular mass of 27.3kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa). CFB is expressed with a 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CFB protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.
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Synonyms
CFB, AHUS4, ARMD14, BF, BFD, CFAB, CFBD, FB, FBI12, GBG, H2-Bf, PBF2, Complement Factor B, B-Factor, Properdin, Properdin Factor B, C3/C5 Convertase, EC 3.4.21.47, PBF2,Glycine-Rich Beta-Glycoprotein, Glycine-Rich Beta Glycoprotein, C3 Proaccelerator, C3 Proactivator , EC 3.4.2, FBI12, H2-Bf.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPEFTPWSL ARPQGSCSLE GVEIKGGSFR LLQEGQALEY VCPSGFYPYP VQTRTCRSTG SWSTLKTQDQ KTVRKAECRA IHCPRPHDFE NGEYWPRSPY YNVSDEISFH CYDGYTLRGS ANRTCQVNGR WSGQTAICDN GAGYCSNPGI PIGTRKVGSQ YRLEDSVTYH CSRGLTLRGS QRRTCQEGGS WSGTEPSCQD SFMYDTPQEV AEAFLSSLTE TIEGVDAEDG HGPGEQQKRH HHHHH.
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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Name :
FGB HumanDescription:
Fibrinogen Beta Chain Human Recombinant
Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.
Product # :
PRO-2210Price :
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Description
FGB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 351 amino acids (164-491a.a) and having a molecular mass of 40kDa. FGB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FGB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Fibrinogen Beta Chain 9 (FGB) is the beta component of fibrinogen, a blood-borne glycoprotein composed of 3 pairs of nonidentical polypeptide chains. When vascular injury accrues, fibrinogen is cleaved by thrombin to form fibrin which is found in abundance in blood clots.
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Synonyms
Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDNENVVN EYSSELEKHQ LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM SMKIRPFFPQ Q.
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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Name :
IFNG MouseDescription:
IFN-Gamma Mouse Recombinant
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-358Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs. -
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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.
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Solubility
It is recommended to reconstitute the lyophilized IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
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Background
What is the molecular weight/Mw of IFNG MOUSE Protein?
IFNG MOUSE Protein has a total Mw of 15.6kDa.
What is the source or expression system of IFNG MOUSE Protein?
Escherichia Coli.
What is the Purity of IFNG MOUSE Protein?
IFNG MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG MOUSE Protein?
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
What is the amino acid sequence of IFNG MOUSE Protein?
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
What applications can IFNG MOUSE Protein be used in?
IFNG MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG MOUSE Protein?
The endotoxin level is minimal, IFNG 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.
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Name :
LIF HumanDescription:
Leukemia Inhibitory Factor Human Recombinant
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-644Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS 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 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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.
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Solubility
It is recommended to reconstitute the lyophilized Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.
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Background
Leukemia Inhibitory Factor (LIF) Background
Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.
LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.
Function and Applications of LIF
LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.
Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.
Structure and Interactions
LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.
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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Name :
MIF Mouse, HisDescription:
Macrophage Migration Inhibitor Factor Mouse Recombinant, His Tag
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
Product # :
CYT-896Price :
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Shipped with Ice Packs
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Description
MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa. MIF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIF protein solution (0.5mg/ml) containing Phosphate buffered saline , 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPMFIVN TNVPRASVPE GFLSELTQQL AQATGKPAQY IAVHVVPDQL MTFSGTNDPC ALCSLHSIGK IGGAQNRNYS KLLCGLLSDR LHISPDRVYI NYYDMNAANV GWNGSTFA.
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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Name :
FHIT HumanDescription:
Fragile Histidine Triad Human Recombinant
EC 3.6.1.29, Dinucleosidetriphosphatase, Bis (5''-adenosyl)-triphosphatase , AP3Aase, AP3A hydrolase, Diadenosine 5'',5''''''-P1,P3-triphosphate hydrolase, FRA3B.
Product # :
PRO-828Price :
Quantity :
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Shipped with Ice Packs
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Description
FHIT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids (1-147 a.a.) and having a molecular mass of 17.9 kDa. FHIT protein is fused to an 8 amino acid His tag at C-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
FHIT Human solution containing 20mM Tris-HCl pH-8 & 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
FHIT enzyme cleaves adenosine 5'' PPP 5'' A to yield AMP and ADP. FHIT gene includees the regular fragile site FRA3B on chromosome 3. Alterations and deletions of the FHIT gene are highly linked to the genesis and establishment of human tumors of the lung, cervix, breast, colon, stomach and pancreas. In normal cells, FHIT functions as a tumor suppressor and physically relates with ubiquitin conjugating enzyme 9.
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Synonyms
EC 3.6.1.29, Dinucleosidetriphosphatase, Bis (5''-adenosyl)-triphosphatase , AP3Aase, AP3A hydrolase, Diadenosine 5'',5''''''-P1,P3-triphosphate hydrolase, FRA3B.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL RPDEVADLFQ TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL PRKAGDFHRN DSIYEELQKH DKEDFPASWR SEEEMAAEAA ALRVYFQLEH HHHHH.
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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Name :
KIT HumanDescription:
KIT Proto-Oncogene Receptor Tyrosine Human Recombinant
Mast/stem cell growth factor receptor Kit, SCFR, Piebald trait protein, PBT, Proto-oncogene c-Kit, Tyrosine-protein kinase Kit, p145 c-kit, v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog, CD117.
Product # :
PKA-102Price :
Quantity :
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Shipped with Ice Packs
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Description
KIT produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 507 amino acids (26-524 a.a.) and having a molecular mass of 57.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).KIT is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus.
Formulation
KIT protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
KIT, also known as KIT Proto-Oncogene Receptor Tyrosine, is a cytokine receptor which is expressed not only in hematopoietic stem cells but likewise in other cell types. KIT binds to receptor tyrosine kinase type III, which is a stem cell factor, also named a "rigid factor" or "c-kit ligand". Once this receptor binds to stem cell factor (SCF), it forms a dimer which activates intrinsic tyrosine kinase activity, which sequentially phosphorylates & activates signaling molecules which breed signals in cells. This receptor protects vascular smooth muscle cells from apoptosis in addition to restoring cardiac function after myocardial infarction.
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Synonyms
Mast/stem cell growth factor receptor Kit, SCFR, Piebald trait protein, PBT, Proto-oncogene c-Kit, Tyrosine-protein kinase Kit, p145 c-kit, v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog, CD117.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
QPSVSPGEPS PPSIHPGKSD LIVRVGDEIR LLCTDPGFVK WTFEILDETN ENKQNEWITE KAEATNTGKY TCTNKHGLSN SIYVFVRDPA KLFLVDRSLY GKEDNDTLVR CPLTDPEVTN YSLKGCQGKP LPKDLRFIPD PKAGIMIKSV KRAYHRLCLH CSVDQEGKSV LSEKFILKVR PAFKAVPVVS VSKASYLLRE GEEFTVTCTI KDVSSSVYST WKRENSQTKL QEKYNSWHHG DFNYERQATL TISSARVNDS GVFMCYANNT FGSANVTTTL EVVDKGFINI FPMINTTVFV NDGENVDLIV EYEAFPKPEH QQWIYMNRTF TDKWEDYPKS ENESNIRYVS ELHLTRLKGT
EGGTYTFLVS NSDVNAAIAF NVYVNTKPEI LTYDRLVNGM LQCVAAGFPE PTIDWYFCPG TEQRCSASVL PVDVQTLNSS GPPFGKLVVQ SSIDSSAFKH NGTVECKAYN DVGKTSAYFN FAFKGNNKEQ IHPHTLFTPL EHHHHHH.
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.
- View Data Sheet
Name :
OSM Human, 209 a.aDescription:
Oncostatin M Human Recombinant (209 a.a.)
OSM, MGC20461, Oncostatin M.
Product # :
CYT-639Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Oncostatin-M (209 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids and having a molecular mass of 23.9kDa. The Oncostatin-M (209 a.a.) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Oncostatin-M (209 a.a.) was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH-7.4.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
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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.
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Synonyms
OSM, MGC20461, Oncostatin M.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin-M (209 a.a.) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin-M (209 a.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.
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Solubility
It is recommended to reconstitute the lyophilized Oncostatin-M (209 a.a.) in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
AAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPG
AFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDL
EKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQ
RKLEGCRFLHGYHRFMHSVGRVFKWGESPNRSRRHSPHQALRKGVRR.
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.
- View Data Sheet
Name :
CD116 Human, sf9Description:
GM-CSF Receptor Alpha Sf9 Human Recombinant
Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.
Product # :
CYT-1044Price :
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Description
CSF2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (20-320a.a.) and having a molecular mass of 35.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CSF2RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CSF2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.
More Info
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Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
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Synonyms
Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPLIPEKSD LRTVAPASSL NVRFDSRTMN LSWDCQENTT FSKCFLTDKK NRVVEPRLSN NECSCTFREI CLHEGVTFEV HVNTSQRGFQ QKLLYPNSGR EGTAAQNFSC FIYNADLMNC TWARGPTAPR DVQYFLYIRN SKRRREIRCP YYIQDSGTHV GCHLDNLSGL TSRNYFLVNG TSREIGIQFF DSLLDTKKIE RFNPPSNVTV RCNTTHCLVR WKQPRTYQKL SYLDFQYQLD VHRKNTQPGT ENLLINVSGD LENRYNFPSS EPRAKHSVKI RAADVRILNW SSWSEAIEFG SDDGHHHHHH
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Background
GM-CSF Receptor Alpha Human Recombinant: A Glimpse into Its Potential and Implications
Abstract:
Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) receptor alpha, a pivotal component in the GM-CSF signaling pathway, has been the focal point of numerous studies pertaining to hematopoiesis and immune responses. This paper provides an overview of the GM-CSF receptor alpha human recombinant, exploring its characteristics, production techniques, and potential therapeutic applications.
Introduction
GM-CSF, a cytokine responsible for the differentiation and proliferation of white blood cells, functions by binding to its receptor, GM-CSF receptor. The alpha subunit (GM-CSFRα) of this receptor plays a crucial role in ligand binding and is essential for initiating cellular responses. Modern biotechnological advancements have led to the successful production of its human recombinant form, offering new avenues in medical research.
Recombinant GM-CSFRα:
Production and Features Recombinant GM-CSFRα is synthesized using cutting-edge recombinant DNA technologies, predominantly in bacterial or mammalian expression systems. This human recombinant form retains its ability to bind to GM-CSF, maintaining its biological functionality and providing myriad research opportunities.
Therapeutic and Clinical Prospects
- Autoimmune Diseases: GM-CSF is often overexpressed in various autoimmune disorders. By utilizing recombinant GM-CSFRα as a potential decoy receptor, it's feasible to mitigate the effects of excessive GM-CSF, offering a new therapeutic strategy.
- Hematopoietic Disorders: Given its integral role in white blood cell development, recombinant GM-CSFRα might hold promise in treatments or as a diagnostic tool for certain hematological conditions.
- Research Paradigm: Beyond therapeutic applications, the recombinant GM-CSFRα can serve as an invaluable research tool to elucidate the nuances of GM-CSF signaling, aiding in the understanding of immune response mechanisms.
Conclusion:
GM-CSF receptor alpha human recombinant stands at the forefront of exciting research and therapeutic potential. While its full capabilities are yet to be realized, current insights underscore its significance in the realms of immunology and medicine.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 35.9kDa.
What is the source or expression system of CD116 Protein?
Sf9, Baculovirus cells.
What is the Purity of CD116 Protein?
CD116 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CD116 Protein?
Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.
What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 310 amino acids.
What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 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.
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Name :
FASLG HumanDescription:
FAS Ligand Human Recombinant
Tumor necrosis factor ligand superfamily member 6, Apoptosis antigen ligand, APTL, CD95 ligand, CD95-L, Fas antigen ligand, Fas ligand, FasL, CD178, FASLG, APT1LG1, CD95L, TNFSF6, ALPS1B.
Product # :
CYT-031Price :
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- sds-page
Description
FASLG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (130-281 a.a.) and having a molecular mass of 19.6kDa.FASLG is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FASLG protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
The type II transmembrane protein FASLG is a member of the tumor necrosis factor (TNF) superfamily. A fas ligand/receptor interaction has a significant part in the regulation of the immune system and the advancement of cancer. FASLG is expressed on the activated T cell surface as a nondisulfidelinked homotrimer. FASLG binding to Fas/CD95/TNFRSF6 on a nearby cell prompts apoptosis in the Fas expressing cell. FASLG is released from the cell surface by metalloproteinases as a soluble molecule that stays trimeric and is able to bind with Fas, but its capability to activate apoptosis is radically reduced. In addition, FASLG binds to DcR3 - a soluble trap receptor with no signal transduction capabilities. Flawed Fas-mediated apoptosis causes oncogenesis in addition to drug resistance in existing tumors. Constitutive expression of FASLG in a variety of tumors enables their immune evasion. Both mouse and human FASLG are active on mouse and human cells.
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Synonyms
Tumor necrosis factor ligand superfamily member 6, Apoptosis antigen ligand, APTL, CD95 ligand, CD95-L, Fas antigen ligand, Fas ligand, FasL, CD178, FASLG, APT1LG1, CD95L, TNFSF6, ALPS1B.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQIGHPSPPP EKKELRKVAH LTGKSNSRSM PLEWEDTYGI VLLSGVKYKK GGLVINETGL YFVYSKVYFR GQSCNNLPLS HKVYMRNSKY PQDLVMMEGK MMSYCTTGQM WARSSYLGAV FNLTSADHLY VNVSELSLVN FEESQTFFGL YKL.
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Background
What is the molecular weight/Mw of FASL Protein?
FASL Protein has a total Mw of 19.6kDa.
What is the source or expression system of FASL Protein?
Escherichia Coli.
What is the Purity of FASL Protein?
FASL Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of FASL Protein?
The biological functionality of FASL Protein will be determined in the future.
What is the amino acid sequence of FASL Protein?
MGSSHHHHHH SSGLVPRGSH MQIGHPSPPP EKKELRKVAH LTGKSNSRSM PLEWEDTYGI VLLSGVKYKK GGLVINETGL YFVYSKVYFR GQSCNNLPLS HKVYMRNSKY PQDLVMMEGK MMSYCTTGQM WARSSYLGAV FNLTSADHLY VNVSELSLVN FEESQTFFGL YKL.
What applications can FASL Protein be used in?
FASL Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FASL Protein?
The endotoxin level is minimal, FASL 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.
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Name :
OPG MouseDescription:
Osteoprotegerin Mouse Recombinant
Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.
Product # :
CYT-956Price :
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Description
OPG Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 388 amino acids (22-401a.a.) and having a molecular mass of 44.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).OPG is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
OPG protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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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.
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Synonyms
Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
ETLPPKYLHY DPETGHQLLC DKCAPGTYLK QHCTVRRKTL CVPCPDHSYT DSWHTSDECV YCSPVCKELQ SVKQECNRTH NRVCECEEGR YLEIEFCLKH RSCPPGSGVV QAGTPERNTV CKKCPDGFFS GETSSKAPCI KHTNCSTFGL LLIQKGNATH DNVCSGNREA TQKCGIDVTL CEEAFFRFAV PTKIIPNWLS VLVDSLPGTK VNAESVERIK RRHSSQEQTF QLLKLWKHQN RDQEMVKKII QDIDLCESSV QRHLGHSNLT TEQLLALMES LPGKKISPEE IERTRKTCKS SEQLLKLLSL WRIKNGDQDT LKGLMYALKH LKTSHFPKTV THSLRKTMRF LHSFTMYRLY QKLFLEMIGN QVQSVKISCL LEHHHHHH.
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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Name :
FRZB Human, Sf9Description:
Frizzled-Related Protein Human Recombinant, Sf9
Secreted frizzled-related protein 3, sFRP-3, Frezzled, Fritz, Frizzled-related protein 1, FrzB-1, FRZB, FIZ, FRE, FRP, FRZB1, SFRP3, OS1, FZRB, hFIZ, FRP-3, SFRP3, SRFP3, FRZB-PEN.
Product # :
PRO-2551Price :
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Description
FRZB produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 302 amino acids (33-325 a.a.) and having a molecular mass of 34.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).FRZB is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The FRZB solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Frizzled-Related Protein (FRZB) is a secreted protein which is involved in the regulation of bone development. FRZB gene defects cause the female-specific osteoarthritis (OA) susceptibility. sFRPS (Soluble frizzled-related proteins) serve as modulators of Wnt signaling by direct interaction with Wnts. sFRPS have a role in regulating cell growth and differentiation in specific cell types. SFRP3/FRZB is involved in limb skeletogenesis. FRZB regulates chondrocyte maturation and long bone development.
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Synonyms
Secreted frizzled-related protein 3, sFRP-3, Frezzled, Fritz, Frizzled-related protein 1, FrzB-1, FRZB, FIZ, FRE, FRP, FRZB1, SFRP3, OS1, FZRB, hFIZ, FRP-3, SFRP3, SRFP3, FRZB-PEN.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPAACEPVR IPLCKSLPWN MTKMPNHLHH STQANAILAI EQFEGLLGTH CSPDLLFFLC AMYAPICTID FQHEPIKPCK SVCERARQGC EPILIKYRHS WPENLACEEL PVYDRGVCIS PEAIVTADGA DFPMDSSNGN CRGASSERCK CKPIRATQKT YFRNNYNYVI RAKVKEIKTK CHDVTAVVEV KEILKSSLVN IPRDTVNLYT SSGCLCPPLN VNEEYIIMGY EDEERSRLLL VEGSIAEKWK DRLGKKVKRW DMKLRHLGLS KSDSSNSDST QSQKSGRNSN PRQARNHHHH HH.
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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Name :
TSFM HumanDescription:
Ts Translation Elongation Factor Mitochondrial Human Recombinant
Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.
Product # :
PRO-1971Price :
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Description
TSFM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (46-346 a.a) and having a molecular mass of 32.9kDa.TSFM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TSFM protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
TSFM is a mitochondrial translation elongation factor which is linked with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. TSFM stays bound to the aminoacyl-tRNA.EF-Tu.GTP complex until the GTP hydrolysis stage on the ribosome. Mutations in TSFM are related with combined oxidative phosphorylation deficiency-3 syndrome.
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Synonyms
Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MSKELLMKLR RKTGYSFVNC KKALETCGGD LKQAEIWLHK EAQKEGWSKA AKLQGRKTKE GLIGLLQEGN TTVLVEVNCE TDFVSRNLKF QLLVQQVALG TMMHCQTLKD QPSAYSKVQW LTPVNLALWE AEAGGSLEGF LNSSELSGLP AGPDREGSLK DQLALAIGKL GENMILKRAA WVKVPSGFYV GSYVHGAMQS PSLHKLVLGK YGALVICETS EQKTNLEDVG RRLGQHVVGM APLSVGSLDD EPGGEAETKM LSQPYLLDPS ITLGQYVQPQ GVSVVDFVRF ECGEGEEAAE TE.
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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Name :
KLF7 HumanDescription:
Kruppel-Like Factor 7 Human Recombinant
UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.
Product # :
PRO-1527Price :
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Description
KLF7 Human Recombinant produced in E. coli is a single polypeptide chain containing 325 amino acids (1-302) and having a molecular mass of 35.8kDa. KLF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLF7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Kruppel-Like Factor 7 (KLF7) is a part of the Kruppel-like transcriptional regulator family whose members regulate cell proliferation, differentiation and survival and contain 3 C2H2 zinc fingers at the C-terminus that mediate binding to GC-rich sites. KLF7 contributes to the progression of type 2 diabetes by inhibiting hormone expression and secretion in pancreatic beta-cells and also by deregulating adipocytokine secretion in adipocytes.
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Synonyms
UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDVLASY SIFQELQLVH DTGYFSALPS LEETWQQTCL ELERYLQTEP RRISETFGED LDCFLHASPP PCIEESFRRL DPLLLPVEAA ICEKSSAVDI LLSRDKLLSE TCLSLQPASS SLDSYTAVNQ AQLNAVTSLT PPSSPELSRH LVKTSQTLSA VDGTVTLKLV AKKAALSSVK VGGVATAAAA VTAAGAVKSG QSDSDQGGLG AEACPENKKR VHRCQFNGCR KVYTKSSHLK AHQRTHTGEK PYKCSWEGCE WRFARSDELT RHYRKHTGAK PFKCNHCDRC FSRSDHLALH MKRHI.
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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Name :
GRB2 HumanDescription:
Growth Factor Receptor-Bound Protein 2 Human Recombinant
ASH, Grb3-3, MST084, MSTP084, EGFRBP-GRB2, GRB2, Growth factor receptor-bound protein 2, Adapter protein GRB2, SH2/SH3 adapter GRB2, Protein Ash.
Product # :
PRO-678Price :
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Description
GRB2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular mass of 27 kDa.GRB2 is expressed with a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GRB2 protein solution contains 20mM Tris-HCl, pH-8 and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GRB2 is widely expressed and binds the EGFR and contains one SH2 domain and two SH3 domains which form a complex formation with proline-rich regions of other proteins, and its SH2 domain binds tyrosine phosphorylated sequences. GRB2 is related to the Sem5 gene of C.elegans, which is takes part in the signal transduction pathway. GRB2 is an adaptor protein that provides an important link between cell surface growth factor receptors and the Ras signaling pathway. Inhibition of GRB2 activity damages developmental processes in a variety of organisms and blocks transformation and proliferation of different cell types.
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Synonyms
ASH, Grb3-3, MST084, MSTP084, EGFRBP-GRB2, GRB2, Growth factor receptor-bound protein 2, Adapter protein GRB2, SH2/SH3 adapter GRB2, Protein Ash.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEAIAKYDFK ATADDELSFK RGDILKVLNE ECDQNWYKAE LNGKDGFIPK NYIEMKPHPW FFGKIPRAKA EEMLSKQRHD GAFLIRESES APGDFSLSVK FGNDVQHFKV LRDGAGKYFL WVVKFNSLNE LVDYHRSTSV SRNQQIFLRD IEQVPQQPTY VQALFDFDPQ EDGELGFRRG DFIHVMDNSD PNWWKGACHG QTGMFPRNYV TPVNRNV.
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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Name :
KLF6 HumanDescription:
Kruppel-Like Factor 6 Human Recombinant
Krueppel-like factor 6, B-cell-derived protein 1, Core promoter element-binding protein, GC-rich sites-binding factor GBF, Proto-oncogene BCD1, Suppressor of tumorigenicity 12 protein, Transcription factor Zf9, KLF6, BCD1, COPEB, CPBP, ST12.
Product # :
PRO-1864Price :
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Description
KLF6 Human Recombinant produced in E. coli is. a single polypeptide chain containing 306 amino acids (1-283) and having a molecular mass of 34.3kDa. KLF6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLF6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Kruppel-Like Factor 6 (KLF6) is a nuclear protein which has 3 zinc fingers. The zinc fingers of KLF6 are accountable for the specific DNA binding with the guanine-rich core promoter factors. The central region is involved in activation or posttranslational regulatory pathways, and the acidic N terminal domain takes part in the process of transcriptional activation.
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Synonyms
Krueppel-like factor 6, B-cell-derived protein 1, Core promoter element-binding protein, GC-rich sites-binding factor GBF, Proto-oncogene BCD1, Suppressor of tumorigenicity 12 protein, Transcription factor Zf9, KLF6, BCD1, COPEB, CPBP, ST12.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDVLPMC SIFQELQIVH ETGYFSALPS LEEYWQQTCL ELERYLQSEP CYVSASEIKF DSQEDLWTKI ILAREKKEES ELKISSSPPE DTLISPSFCY NLETNSLNSD VSSESSDSSE ELSPTAKFTS DPIGEVLVSS GKLSSSVTST PPSSPELSRE PSQLWGCVPG ELPSPGKVRS GTSGKPGDKG NGDASPDGRR RVHRCHFNGC RKVYTKSSHL KAHQRTHTGE KPYRCSWEGC EWRFARSDEL TRHFRKHTGA KPFKCSHCDR CFSRSDHLAL HMKRHL.
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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Name :
GHBP Human, HisDescription:
Growth Hormone Binding Protein Human Recombinant, His Tag
Growth Hormone Receptor, Growth Hormone Binding Protein, Somatotropin Receptor GH Receptor, Serum Binding Protein, GHBP, GHIP.
Product # :
CYT-921Price :
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Description
GHBP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 254 amino acids (19-264a.a.) and having a molecular mass of 29.4kDa.GHBP is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
GHBP protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 10ng/ml and is measured by ability to inhibit GH-induced proliferation assay using Nb2-11 Rat lymphoma cells in the presence of 1.25ng/ml of human growth hormone.
More Info
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Introduction
Growth hormone receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, growth hormone performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.
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Synonyms
Growth Hormone Receptor, Growth Hormone Binding Protein, Somatotropin Receptor GH Receptor, Serum Binding Protein, GHBP, GHIP.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
FSGSEATAAI LSRAPWSLQS VNPGLKTNSS KEPKFTKCRS PERETFSCHW TDEVHHGTKN LGPIQLFYTR RNTQEWTQEW KECPDYVSAG ENSCYFNSSF TSIWIPYCIK LTSNGGTVDE KCFSVDEIVQ PDPPIALNWT LLNVSLTGIH ADIQVRWEAP RNADIQKGWM VLEYELQYKE
VNETKWKMMD PILTTSVPVY SLKVDKEYEV RVRSKQRNSG NYGEFSEVLY VTLPQMSQFT CEEDFYLEHH HHHH.
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.
- View Data Sheet
Name :
NFATC2 HumanDescription:
Nuclear Factor Of Activated T Cells 2 Human Recombinant
Nuclear Factor Of Activated T Cells 2, Nuclear Factor Of Activated T-Cells, Cytoplasmic, Calcineurin-Dependent 2, Nuclear Factor Of Activated T-Cells 2, NFAT Pre-Existing Subunit, NF-ATc2, NFAT1, NFATP, Nuclear Factor Of Activated T-Cells, Preexisting Component , Nuclear Factor Of Activated T-Cells, Cytoplasmic 2, NFAT Transcription Complex, Preexisting Component, Preexisting Nuclear Factor Of Activated T-Cells 2, T Cell Transcription Factor NFAT1, T-Cell Transcription Factor NFAT1, NF-ATp, NFATc2.
Product # :
PRO-2535Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NFATC2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 290 amino acids (396-678a.a.) and having a molecular mass of 33.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). NFATC2 is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NFATC2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) 40% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NFATC2, also known as nuclear factor of activated T-cells 2, belongs to the nuclear factor of activated T cells family. NFATC2 takes a significant part in the course of T helper cell differentiation, activation, and effector function. Even though KO of an individual NFAT isoform in T cells directs to rather minor effects, T cells lacking for NFATC1 and 2 totally fail to produce T helper cell effector cytokines, for instance the interleukins IL-4 and IL-2. Moreover, NFATC2 is highly phosphorylated and kept in the cytoplasm. Next T cell receptor stimulation, dephosphorylation via calcium-activated calcineurin induces a conformational modification of NFATC2 which reveals a few nuclear localization sequences.
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Synonyms
Nuclear Factor Of Activated T Cells 2, Nuclear Factor Of Activated T-Cells, Cytoplasmic, Calcineurin-Dependent 2, Nuclear Factor Of Activated T-Cells 2, NFAT Pre-Existing Subunit, NF-ATc2, NFAT1, NFATP, Nuclear Factor Of Activated T-Cells, Preexisting Component , Nuclear Factor Of Activated T-Cells, Cytoplasmic 2, NFAT Transcription Complex, Preexisting Component, Preexisting Nuclear Factor Of Activated T-Cells 2, T Cell Transcription Factor NFAT1, T-Cell Transcription Factor NFAT1, NF-ATp, NFATc2.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MPLEWPLSSQ SGSYELRIEV QPKPHHRAHY ETEGSRGAVK APTGGHPVVQ LHGYMENKPL GLQIFIGTAD ERILKPHAFY QVHRITGKTV TTTSYEKIVG NTKVLEIPLE PKNNMRATID CAGILKLRNA DIELRKGETD IGRKNTRVRL VFRVHIPESS GRIVSLQTAS NPIECSQRSA HELPMVERQD TDSCLVYGGQ QMILTGQNFT SESKVVFTEK TTDGQQIWEM EATVDKDKSQ PNMLFVEIPE YRNKHIRTPV KVNFYVINGK RKRSQPQHFT YHPVHHHHHH
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.
- View Data Sheet
Name :
FSTL1 Human, HEKDescription:
Follistatin Like 1 Human Recombinant, HEK
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.
Product # :
CYT-1027Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FSTL1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-308) containing 296 amino acids including a 8 a.a C-terminal His tag. The total molecular mass is 33.8kDa (calculated).
Source
HEK293 cells.
Formulation
FSTL1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline and 5 % (w/v) trehalose, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
FSTL1 protein resembles follistatin, an activin-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.
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Synonyms
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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 one week at 4°C.
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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. FSTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.
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Background
What is the molecular weight/Mw of FSTL1 HUMAN, HEK Protein?
FSTL1 HUMAN, HEK Protein has a total Mw of 33.8kDa.
What is the source or expression system of FSTL1 HUMAN, HEK Protein?
HEK293 cells.
What is the Purity of FSTL1 HUMAN, HEK Protein?
FSTL1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FSTL1 HUMAN, HEK Protein?
The biological functionality of FSTL1 HUMAN, HEK Protein will be determined in the future.
What is the amino acid sequence of FSTL1 HUMAN, HEK Protein?
EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.
What applications can FSTL1 HUMAN, HEK Protein be used in?
FSTL1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FSTL1 HUMAN, HEK Protein?
The endotoxin level is minimal, FSTL1 HUMAN, HEK 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.
- View Data Sheet
Name :
Prolactin Mouse, HisDescription:
Prolactin Mouse Recombinant, His Tag
AV290867, Gha1, Prl1a1, Growth hormone a1, Mammotropin, Luterotropic hormone, Lutetropin, PRL.
Product # :
CYT-1060Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Prolactin Mouse produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (30-228a.a.) and having a molecular mass of 25 kDa. Prolactin Mouse protein is fused to a 23 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
The Prolactin Mouse solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
AV290867, Gha1, Prl1a1, Growth hormone a1, Mammotropin, Luterotropic hormone, Lutetropin, PRL.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQPLPICS AGDCQTSLRE LFDRVVILSH YIHTLYTDMF IEFDKQYVQD REFMVKVIND CPTSSLATPE DKEQALKVPP EVLLNLILSL VQSSSDPLFQ LITGVGGIQE APEYILSRAK EIEEQNKQLL EGVEKIISQA YPEAKGNGIY VWSQLPSLQ GVDEESKILS LRNTIRCLRR DSHKVDNFLK VLRCQIAHQN NC.
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.
- View Data Sheet
Name :
NT 3 HumanDescription:
Neurotrophin-3 Human Recombinant
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
Product # :
CYT-257Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 0.1% TFA.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.
More Info
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Introduction
NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.
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Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-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.
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Solubility
It is recommended to reconstitute the lyophilized Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of NT-3 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.
- View Data Sheet
Name :
EIF3I Human, Sf9Description:
Eukaryotic Translation Initiation Factor 3I Human Recombinant, Sf9
eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiationfactor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta.
Product # :
PRO-2611Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EIF3I Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (1-325 a.a) and having a molecular mass of 37.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).EIF3I is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EIF3I protein solution (0.25mg/ml) 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% Glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Eukaryotic translation initiation factor 3, subunit I (EIF3I) is part of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is essential for numerous steps in the initiation of protein synthesis. The eIF-3 complex links with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2: GTP: methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also essential for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3I are clonorchiasis, and tonsillitis.
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Synonyms
eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiation
factor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta. -
Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA
DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC
FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV
LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN
YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY SSGGEDGYVR IHYFDPQYFE FEFEAHHHHH H.
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.