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Name :
IFNG Human, His ActiveDescription:
Interferon-gamma Human Recombinant, His Tag Active
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-1053Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
IFNG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (24-161 a.a) and having a molecular mass of 18.4kDa. IFNG is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IFNG protein solution (1mg/ml) containing Phosphate buffered saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cytotoxicity assay using WiDr cells. The ED50 for this effect is ≤ 5 ng/ml.
SDS-PAGE
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 interferons. -
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
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Physical Appearance
Sterile Filtered colorless liquid.
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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 MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
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Background
What is the molecular weight/Mw of IFNG HUMAN, HIS ACTIVE Protein?
IFNG HUMAN, HIS ACTIVE Protein has a total Mw of 18.4kDa.
What is the source or expression system of IFNG HUMAN, HIS ACTIVE Protein?
Escherichia Coli.
What is the Purity of IFNG HUMAN, HIS ACTIVE Protein?
IFNG HUMAN, HIS ACTIVE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG HUMAN, HIS ACTIVE Protein?
Measured in a cytotoxicity assay using WiDr cells. The ED50 for this effect is ≤ 5 ng/ml.
What is the amino acid sequence of IFNG HUMAN, HIS ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
What applications can IFNG HUMAN, HIS ACTIVE Protein be used in?
IFNG HUMAN, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG HUMAN, HIS ACTIVE Protein?
The endotoxin level is minimal, IFNG HUMAN, HIS ACTIVE 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 :
SPINK7 HumanDescription:
Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant
Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.
Product # :
PRO-1507Price :
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Shipped with Ice Packs
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Description
SPINK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 89 amino acids (20-85) and having a molecular mass of 9.6 kDa.SPINK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPINK7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Serine peptidase inhibitor Kazal type 7 (SPINK7) which includes one Kazal-like domain is most likely serine protease inhibitor. Diseases linked with SPINK7 include esophageal cancer, and oral squamous cell carcinoma
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Synonyms
Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.
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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 MGSSEAASLS PKKVDCSIYK KYPVVAIPCP ITYLPVCGSD YITYGNECHL CTESLKSNGR VQFLHDGSC.
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 :
TNFA Mouse, Sf9Description:
Tumor Necrosis Factor-alpha Mouse Recombinant, Sf9
Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2.
Product # :
CYT-912Price :
Quantity :
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Shipped with Ice Packs
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Description
TNFA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 162 amino acids (80-235 a.a.) and having a molecular mass of 18kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).TNFA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFA protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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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
Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2.
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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
LRSSSQNSSD KPVAHVVANH QVEEQLEWLS QRANALLANG MDLKDNQLVV PADGLYLVYS QVLFKGQGCP DYVLLTHTVS RFAISYQEKV NLLSAVKSPC PKDTPEGAEL KPWYEPIYLG GVFQLEKGDQ LSAEVNLPKY LDFAESGQVY FGVIALHHHH 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 :
GADD45GIP1 HumanDescription:
Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant
Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.
Product # :
PRO-972Price :
Quantity :
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Shipped with Ice Packs
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Description
GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GADD45GIP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.
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Synonyms
Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.
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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 MPRWQLGPRY AAKQFARYGA ASGVVPGSLW PSPEQLRELE AEEREWYPSL ATMQESLRVK QLAEEQKRRE REQHIAECMA KMPQMIVNWQ QQQRENWEKA QADKERRARL QAEAQELLGY QVDPRSARFQ ELLQDLEKKE RKRLKEEKQK RKKEARAAAL AAAVAQDPAA SGAPSS
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 :
CHGA Human, HisDescription:
Chromogranin-A Human Recombinant, His Tag
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-699Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (19-457 a.a) and having a molecular mass of 51.2kDa (Molecular weight on SDS-PAGE will appear higher). Chromgranin-A is fused to 21 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein (0.5mg/ml) contains 20mM Tris-HCl buffer pH-7.5, 2mM EDTA, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 80.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
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Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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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 MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVMEKREDSK EAEKSGEATD GARPQALPEP MQESKAEGNN QAPGEEEEEE EEATNTHPPA SLPSQKYPGP QAEGDSEGLS QGLVDREKGL SAEPGWQAKR EEEEEEEEEA EAGEEAVPEE EGPTVVLNPH PSLGYKEIRK GESRSEALAV DGAGKPGAEE AQDPEGKGEQ EHSQQKEEEE EMAVVPQGLF RGGKSGELEQ EEERLSKEWE DSKRWSKMDQ LAKELTAEKR LEGQEEEEDN RDSSMKLSFR ARAYGFRGPG PQLRRGWRPS SREDSLEAGL PLQVRGYPEE KKEEEGSANR RPEDQELESL SAIEAELEKV AHQLQALRRG.
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 :
p16-INK4a HumanDescription:
Cyclin-Dependent Kinase Inhibitor 2A Human Recombinant
Cyclin-dependent kinase 4 inhibitor A, CDK4I, p16-INK4, p16-INK4a, p16INK4A, CDKN-2A, CDKN2, Multiple tumor suppressor 1, MTS1, CMM2, MLM, TP16, p16(INK4), p19.
Product # :
PKA-341Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CDKN2A Human Recombinant produced in E.Coli, it's a single non-glycosylated polypeptide chain containing 156 amino acids, approximately 16.5 kDa.CDKN2A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDKN2A was lyophilized from a concentrated (1mg/ml) sterile solution containing 1x PBS pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Cyclin-dependent kinase inhibitors (CDKIs) are proteins that bind to and inhibit the activity of CDKs. Two major classes of CDK inhibitors have been identified. The p16 family (p15, p16, p18 and p19) binds to and inhibits the activities of CDK4 and CDK6. The p21 family (p21, p27, p28 and p57) can bind to broad range of CDK-cyclin complexes and inhibit their activities. CDKIs are capable of suppressing growth, and several lines of evidence strongly suggest that at least some CDKIs may be tumor suppressor proteins.
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Synonyms
Cyclin-dependent kinase 4 inhibitor A, CDK4I, p16-INK4, p16-INK4a, p16INK4A, CDKN-2A, CDKN2, Multiple tumor suppressor 1, MTS1, CMM2, MLM, TP16, p16(INK4), p19.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cyclin-dependent kinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cyclin-dependent kinase 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 Cyclin-dependent kinase 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
MEPAAGSSMEPSADWLATAAARGRVEEVRALLEAGALPNAPNSYGRRPIQVM
MMGSARVAELLLLHGAEPNCADPATLTRPVHDAAREGFLDTLVVLHRAGARL
DVRDAWGRLPVDLAEELGHRDVARYLRAAAGGTRGSNHARIDAAEGPSDIPD.
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 :
MIP 1a Mouse, HisDescription:
Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3), His Tag
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, Heparin-binding chemotaxis protein, L2G25B.
Product # :
CHM-008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MIP-1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (24-92 a.a.) and having a molecular mass of 10.4kDa.MIP-1a is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP-1a protein solution (0.5mg/ml) containing 20mM Sodium citrate buffer (pH 3.5) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, Heparin-binding chemotaxis protein, L2G25B.
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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 MGSMAPYGAD TPTACCFSYS RKIPRQFIVD YFETSSLCSQ PGVIFLTKRN RQICADSKET WVQEYITDLE LNA.
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Background
What is the molecular weight/Mw of MIP 1A MOUSE, HIS Protein?
MIP 1A MOUSE, HIS Protein has a total Mw of 10.4kDa.
What is the source or expression system of MIP 1A MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of MIP 1A MOUSE, HIS Protein?
MIP 1A MOUSE, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A MOUSE, HIS Protein?
The biological functionality of MIP 1A MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of MIP 1A MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAPYGAD TPTACCFSYS RKIPRQFIVD YFETSSLCSQ PGVIFLTKRN RQICADSKET WVQEYITDLE LNA..
What applications can MIP 1A MOUSE, HIS Protein be used in?
MIP 1A MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A MOUSE, HIS Protein?
The endotoxin level is minimal, MIP 1A MOUSE, 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.
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Name :
TINAGL1 Human, Sf9Description:
Tubulointerstitial Nephritis Antigen Like 1 Human Recombinant, Sf9
Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.
Product # :
PRO-2422Price :
Quantity :
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Shipped with Ice Packs
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Description
TINAGL1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 455 amino acids (22-467a.a.) and having a molecular mass of 51.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). TINAGL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TINAGL1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Tubulointerstitial Nephritis Antigen Like 1 also known as TINAGL1 is similar in sequence to tubulointerstitial nephritis antigen, a secreted glycoprotein which is identified by antibodies in several types of immune-related tubulointerstitial nephritis. Three transcript variants encoding different isoforms are known for TINAGL1.
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Synonyms
Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.
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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
ADLAQQGRGR RELAPGLHLR GIRDAGGRYC QEQDLCCRGR ADDCALPYLG AICYCDLFCN RTVSDCCPDF WDFCLGVPPP FPPIQGCMHG GRIYPVLGTY WDNCNRCTCQ ENRQWQCDQE PCLVDPDMIK AINQGNYGWQ AGNHSAFWGM TLDEGIRYRL GTIRPSSSVM NMHEIYTVLN PGEVLPTAFE ASEKWPNLIH EPLDQGNCAG SWAFSTAAVA SDRVSIHSLG HMTPVLSPQN LLSCDTHQQQ GCRGGRLDGA WWFLRRRGVV SDHCYPFSGR ERDEAGPAPP CMMHSRAMGR GKRQATAHCP NSYVNNNDIY QVTPVYRLGS NDKEIMKELM ENGPVQALME VHEDFFLYKG GIYSHTPVSL GRPERYRRHG THSVKITGWG EETLPDGRTL KYWTAANSWG PAWGERGHFR IVRGVNECDI ESFVLGVWGR VGMEDMGHHH 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 :
TNIP1 HumanDescription:
TNFAIP3 Interacting Protein 1 Human Recombinant
TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-1.
Product # :
PRO-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNIP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 458 amino acids (94-530 a.a.) and having a molecular mass of 51.8kDa. The TNIP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TNIP1 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol, 5mM DTT and 200mM NaCl.
Purity
Greater than 75.0% as determined by SDS-PAGE.
More Info
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Introduction
TNFAIP3-interacting protein 1 (TNIP1) interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with a RIP- or TRAF2-mediated transactivation signal. Furthermore, TNIP1 interacts with HIV-1 matrix protein and is packaged into virions and its overexpression can inhibit viral replication. TNIP1 can regulate matrix nuclear localization, both nuclear import of Preintegration complex (PIC) and export of GAG polyprotein and viral genomic RNA during virion production.
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Synonyms
TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-1.
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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 MSNVTASPTA PACPSDKPAP VQKPPSSGTS SEFEVVTPEE QNSPESSSHA NAMALGPLPR EDGNLMLHLQ RLETTLSVCA EEPDHGQLFT HLGRMALEFN RLASKVHKNE QRTSILQTLC EQLRKENEAL KAKLDKGLEQ RDQAAERLRE ENLELKKLLM SNGNKEGASG RPGSPKMEGT GKKAVAGQQQ ASVTAGKVPE VVALGAAEKK VKMLEQQRSE LLEVNKQWDQ HFRSMKQQYE QKITELRQKL ADLQKQVTDL EAEREQKQRD FDRKLLLAKS KIEMEETDKE QLTAEAKELR QKVKYLQDQL SPLTRQREYQ EKEIQRLNKA LEEALSIQTP PSSPPTAFGS PEGAGALLRK QELVTQNELL KQQVKIFEED FQRERSDRER MNEEKEELKK QVEKLQAQVT LSNAQLKAFK DEEKAREALR QQKRKAKA.
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 :
p59-Fyn HumanDescription:
p59-Fyn Human Recombinant
Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.
Product # :
PRO-506Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
p59-Fyn Human Recombinant (a.a. 23-216) expressed in E.coli, shows a 50 kDa SDS-PAGE (Including GST tag).The p59-Fyn is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
p59-Fyn in 50mM Tris-Acetate, pH7.5, 1mM EDTA and 20% Glycerol.
More Info
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Introduction
p59-Fyn is a member of the protein-tyrosine kinase oncogene family. p59fyn is a membrane-associated non-receptor protein tyrosine kinase that belongs to the Src-family of kinases. p59-Fyn encodes a membrane-associated tyrosine kinase which is implicated in the control of cell growth. p59-Fyn associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. The unique N-terminal domain of p59fyn interacts with the CD3 and eta chains of the TcR. p59fyn can bind other proteins (p82 and p116) through its SH2 and SH3 domains, which may act as substrates or regulators of fyn activity. p59fyn is highly expressed in brain suggesting that it may have a role in the sensory nervous network and in myelination at early stages of CNS formation. Distinct isoforms exist due to alternative splicing.
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Synonyms
Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
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Applications
• ELISA
• Inhibition Assays
• Western Blotting.
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 :
Lungkine MouseDescription:
Lungkine (CXCL15) Mouse Recombinant
C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.
Product # :
CHM-286Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Recombinant Mouse Lungkine produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids and having a molecular mass of 16.4kDa.The CXCL15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Lungkine protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 0.02% Tween-20.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.More Info
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Introduction
Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.
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Synonyms
C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Lungkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL15 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 Lungkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.
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 :
IFNG Human, HisDescription:
Interferon-Gamma Human Recombinant, His Tag
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-478Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- SDS-PAGE
Description
IFN-Gamma Human Recombinant produced in E.Coli is a single, glycosylated polypeptide chain containing 159 amino acids (24-161 a.a) without cysteine residues and having a molecular mass of 18.5kDa (confirmed by MALDI-TOF). IFN-Gamma is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interferon-g is supplied in phosphate-buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
SDS-PAGE
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 interferons. -
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
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Background
What is the molecular weight/Mw of IFNG HUMAN, HIS Protein?
IFNG HUMAN, HIS Protein has a total Mw of 18.5kDa.
What is the source or expression system of IFNG HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of IFNG HUMAN, HIS Protein?
IFNG HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG HUMAN, HIS Protein?
The biological functionality of IFNG HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of IFNG HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
What applications can IFNG HUMAN, HIS Protein be used in?
IFNG HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG HUMAN, HIS Protein?
The endotoxin level is minimal, IFNG 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.
- View Data Sheet
Name :
HCV NS5, BiotinDescription:
Hepatitis C Virus NS5, Biotin Recombinant
Product # :
HCV-236Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- formulation
- purity
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Description
The E.coli derived Biotin Labeled recombinant protein contains the HCV NS5 immunodominant regions. HCV NS5 antigen (recombinant) a.a 2061 to a.a 2302 of HCV polyprotein. The protein is fused to a GST tag at N-terminus.
Formulation
1.5M urea, 25mM Tris-HCl pH 8.0, 0.2% Triton-X and 50% Glycerol.
Purity
HCV NS5 Biotin protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6). -
Stability
HCV NS5 Biotin although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HCV NS5 Biotin antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
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Specificity
Immunoreactive with sera of HCV-infected individuals.
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Purification Method
HCV NS5 Biotin protein was purified by proprietary chromatographic technique.
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 :
GM-CSF MouseDescription:
Granulocyte Macrophage-Colony Stimulating Factor Mouse Recombinant
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF
Product # :
CYT-222Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Granulocyte Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14285.35 Dalton.GM-CSF Mouse is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GM-CSF Mouse was lyophilized with no additives.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.More Info
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GM-CSF 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 Granulocyte Macrophage Colony Stimulating Factor in sterile 20mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.
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Background
What is the molecular weight/Mw of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein has a total Mw of 14.28kDa.
What is the source or expression system of GM-CSF MOUSE Protein?
Escherichia Coli.
What is the Purity of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.
What is the amino acid sequence of GM-CSF MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.
What applications can GM-CSF MOUSE Protein be used in?
GM-CSF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF MOUSE Protein?
The endotoxin level is minimal, GM-CSF MOUSE Protein was purified using conventional chromatography techniques.
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Protein content
GM-CSF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.765 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GM-CSF 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 :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
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Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.
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 :
SNCA Delta-NAC HumanDescription:
Alpha Synuclein Delta-NAC Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-161Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
A-Synuclein Delta-NAC Human Recombinant which is a deletion mutant of the a-synuclein that lacks the NAC region (amino acid 61-95), produced in E.Coli is a single, non-glycosylated polypeptide chain of 111 amino acids having a molecular mass of 11.9kDa (molecular size on SDS-PAGE will appear higher), with 6 amino acids added as a linker. The Recombinant Human a-Synuclein Delta-NAC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA Delta-NAC protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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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.
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Amino Acid Sequence
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK GTEIWMKKDQ LGKNEEGAPQ EGILEDMPVD PDNEAYEMPS EEGYQDYEPE A.
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 :
PPIF HumanDescription:
Cyclophilin-F Human Recombinant
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
Product # :
ENZ-385Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- biological activity
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Description
PPIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids (30-207) and having a molecular mass of 21 kDa. The PPIF is fused to a 20 amino acid His tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PPIF solution containing 20mM Tris-HCl pH-7.5, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 250 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
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Synonyms
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH CSKGSGDPSS SSSSGNPLVY LDVDANGKPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FTLKHVGPGV LSMANAGPNT NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGRTSKKIV ITDCGQLS.
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 :
GNLY HumanDescription:
Granulysin Human Recombinant
LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.
Product # :
PRO-852Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
GNLY Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and fused to a double His Tag (N+C terminus) and having a total molecular mass of 18.1 kDa.The GNLY is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Granulysin protein was lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.
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Synonyms
LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulysin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulysin 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 Granulysin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MGSSHHHHHHSSGLVPRGSHMMEGLVFSRLSPEYYD
LARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYR
TCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWR
DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPS
TGPLGSHHHHHH.
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 :
RCVRN MouseDescription:
Recoverin Mouse Recombinant
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.
Product # :
PRO-2547Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recoverin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202a.a.) and having a molecular mass of 25.8kDa. Recoverin Mouse is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Recoverin is a member of the recoverin family of neuronal calcium sensors. Recoverin is a heterogeneously acylated calcium-binding and intracellular signal transduction 23kDa protein in the photoreceptor cells of retina. Recoverin contains four EF-hands, of which two bind Ca. Ca-induced extrusion of the acyl group from a hydrophobic cleft in the protein drives the translocation of recoverin from solution to the disc membrane. Recoverin may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin plays a key role in the inhibition of rhodopsin kinase, a molecule that regulates the phosphorylation of rhodopsin. This in due course controls the ability of the eye to adapt to, and recover from, exposure to the presence of light. Recoverin is a detectable serologic protein that is expressed in patients with cancer-associated retinopathy, a paraneoplastic syndrome.
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Synonyms
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGNSKSG ALSKEILEEL QLNTKFTEEE LSAWYQSFLK ECPSGRITRQ EFESIYSKFF PDSDPKAYAQ HVFRSFDANS DGTLDFKEYV IALHMTTAGK PTQKLEWAFS LYDVDGNGTI SKNEVLEIVM AIFKMIKPED VKLLPDDENT PEKRAEKIWA FFGKKEDDKL TEEEFIEGTL ANKEILRLIQ FEPQKVKERI KEKKQ.
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 :
CTSZ MouseDescription:
Cathepsin-Z Mouse Recombinant
Cathepsin Z, CTSZ.
Product # :
ENZ-934Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (23-306a.a.) and having a molecular mass of 32.8kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTSZ protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.
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Synonyms
Cathepsin Z, CTSZ.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH 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 :
GDF5 Mouse, HisDescription:
Growth differentiation factor 5 Mouse Recombinant, His Tag
Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.
Product # :
CYT-852Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- sds-page
Description
GDF5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (376-495 a.a) and having a molecular mass of 16kDa.GDF5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
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Synonyms
Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.
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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 MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.
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Background
What is the molecular weight/Mw of GDF5 MOUSE Protein?
GDF5 MOUSE Protein has a total Mw of 16kDa.
What is the source or expression system of GDF5 MOUSE Protein?
Escherichia Coli.
What is the Purity of GDF5 MOUSE Protein?
GDF5 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF5 MOUSE Protein?
The biological functionality of GDF5 MOUSE Protein will be determined in the future.
What is the amino acid sequence of GDF5 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.
What applications can GDF5 MOUSE Protein be used in?
GDF5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF5 MOUSE Protein?
The endotoxin level is minimal, GDF5 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.
- View Data Sheet
Name :
IFNG HumanDescription:
IFN-Gamma Human Recombinant
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-206Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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- formulation
- purity
- biological activity
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- sds-page
Description
IFN-gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 17kDa.The IFN-gamma is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 4.6.
Purity
Greater than 98.0% 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 < 0.05 ng/ml, corresponding to a specific activity of 2.0 x 10,000,000 IU/mg.sds-page
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 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFQGR RASQ.
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Background
IFN-gamma Human
About IFN-gamma Human:
IFN-gamma, often known as interferon gamma (and originally known as immune interferon), is a soluble, dimerized cytokine that is the only interferon in the type II class. Besides its primary function in preventing the spread of the vesicular stomatitis virus, interferon gamma release assays are extensively employed in the diagnosis of tuberculosis. IFN-gamma, encoded by the IFNG gene in humans, controls immunological responses by cell signaling, particularly through the JAK-STAT pathway. Subsequently, interferon gamma plays a crucial role in cancer immunotherapy by preventing tumor growth, managing immune defenses against pathogens and monitoring cells activity. In this article we will delve into the science behind IFN-gamma and explain its significance in biomedical research.
Description:
IFN-gamma Human Recombinant is a single non-glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 17kDa that its original source is Escherichia Coli. This product appears as a sterile-filtered white lyophilized powder, ensuring purity and stability. Its formulation involves lyophilization from a filtered concentrated solution in PBS (pH 4.6). Its purity is determined both by analysis by RP-HPLC and SDS-PAGE and is therefore greater than 98%. In terms of stability, lyophilized IFN gamma is stable at room temperature for three weeks. However, it is preferable to store it desiccated below -18°C. In any case, you should prevent freeze thaw cycles. Additionally, reconstitution of IFN-gamma is recommended in sterile distilled water or 20mM AcOH, maintaining a concentration of at least 100µg/ml.
Protein Function:
Interferon gamma is a key player in immune control. It is a protein that plays a major role in complex cell signaling networks. The JAK-STAT pathway, which is essential for immunological regulation, is triggered by IFN-gamma through its interaction with the heterodimeric receptor. IFN-gamma's ability to regulate inflammation, apoptosis, cytokine signaling, and cell proliferation through protein mediated signaling skills is crucial for maintaining immune vigilance and response mechanisms. The incorporation of IFN-gamma into our product is validated by protein quantitation using two independent methods: UV spectroscopy and RP-HPLC.
Applications and Usage:
IFN-gamma Human is tailored for laboratory research, serving as a vital tool in elucidating immune mechanisms, exploring antiviral features, and unraveling tumor suppressor functions.
Safety Information:
IFN-gamma Human is only intended to be used in laboratory research, in line with safety protocols. It emphasizes adherence to ethical and regulatory norms and is not designed for use as household chemicals, pharmaceuticals, agricultural goods, or food additives.
What is the molecular weight/Mw of IFNG HUMAN Protein?
IFNG HUMAN Protein has a total Mw of 17kDa.
What is the source or expression system of IFNG HUMAN Protein?
Escherichia Coli.
What is the Purity of IFNG HUMAN Protein?
IFNG HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG HUMAN Protein?
The specific activity as determined in a viral resistance assay is < 0.05 ng/ml, corresponding to a specific activity of 2.0 x 10,000,000 IU/mg.
What is the amino acid sequence of IFNG HUMAN Protein?
MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFQGR RASQ.
What applications can IFNG HUMAN Protein be used in?
IFNG HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG HUMAN Protein?
The endotoxin level is minimal, IFNG HUMAN Protein was purified using conventional chromatography techniques.
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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 0.640 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IFN-g 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 :
TNFR2 MouseDescription:
Tumor Necrosis Factor Receptor Type 2 Mouse Recombinant
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, CD120b, Tnfrsf1b, Tnfr-2, Tnfr2, TNFBR, TNFR80, TNFRII, TNF-R75, TNF-R-II, TNF-alphaR2, TNFalpha-R2.
Product # :
CYT-770Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
TNFR2 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 236 amino acids and having a molecular mass of 25.3kDa.The TNFR2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFR2 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to inhibit the TNF-a mediated cytotoxicity in the L-929 cells is less than 2µg/ml, corresponding to a specific activity of > 500IU/mg in the presence of 0.1ng/mL of rHuTNF-a.
More Info
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Introduction
TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury. -
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, CD120b, Tnfrsf1b, Tnfr-2, Tnfr2, TNFBR, TNFR80, TNFRII, TNF-R75, TNF-R-II, TNF-alphaR2, TNFalpha-R2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNFR2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TNFR2 should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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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.
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Amino Acid Sequence
VPAQVVLTPY KPEPGYECQI SQEYYDRKAQ MCCAKCPPGQ YVKHFCNKTS DTVCADCEAS MYTQVWNQFR TCLSCSSSCT TDQVEIRACT KQQNRVCACE AGRYCALKTH SGSCRQCMRL SKCGPGFGVA SSRAPNGNVL CKACAPGTFS DTTSSTDVCR PHRICSILAI PGNASTDAVC APESPTLSAI PRTLYVSQPE PTRSQPLDQE PGPSQTPSIL TSLGSTPIIE QSTKGG.
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 :
PSPN MouseDescription:
Persephin Mouse Recombinant
Persephin, PSPN.
Product # :
CYT-802Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.More Info
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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
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Synonyms
Persephin, PSPN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN 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 PSPN 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
ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG
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.