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1000 results found for “thymosin”
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Name :
MYL9 MouseDescription:
Myosin Light Chain 9 Mouse Recombinant
Myosin regulatory light polypeptide 9, Myosin regulatory light chain 2, Myosin regulatory light chain 9, Myl9, Myrl2.
Product # :
PRO-2193Price :
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Shipped with Ice Packs
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Description
MYL9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (1-172 a.a) and having a molecular mass of 22.4kDa.MYL9 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYL9 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MYL9 is one of the numerous regulatory myosin light chains. Myosin which is a structural component of the muscle consists of 2 heavy chains and 4 light chains. MYL9 is a myosin light chain regulates muscle contraction by modulating the ATPase activity of myosin heads. MYL9 binds calcium and is activated by myosin light chain kinase. Regulatory myosin light chains regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of regulatory myosin light chains is catalyzed by MLCK in the presence of calcium and calmodulin and it increases the actin-activated myosin ATPase activity, thus regulates the contractile activity.
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Synonyms
Myosin regulatory light polypeptide 9, Myosin regulatory light chain 2, Myosin regulatory light chain 9, Myl9, Myrl2.
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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 MGSHMSSKRA KAKTTKKRPQ RATSNVFAMF DQSQIQEFKE AFNMIDQNRD GFIDKEDLHD MLASLGKNPT DEYLEGMMNE APGPINFTMF LTMFGEKLNG TDPEDVIRNA FACFDEEASG FIHEDHLREL LTTMGDRFTD EEVDEMYREA PIDKKGNFNY VEFTRILKHG AKDKDD
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 :
SERPINA3Description:
Alpha-1 AntiChymotrypsin Human Recombinant
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
Product # :
PRO-750Price :
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Shipped with Ice Packs
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Description
SERPINA3 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 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.The SERPINA3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SERPINA3 solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1-ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT. -
Synonyms
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
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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 MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ 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.
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Name :
IFNW1 Human, HEKDescription:
Interferon-Omega 1 Human Recombinant, HEK
IFN omega-1, IFN alpha-II-1, IFNW1.
Product # :
CYT-1225Price :
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Description
IFNW1 Human Recombinant is a single, glycosylated, polypeptide chain (22-195 a.a) containing a total of 180 amino acids and having a molecular mass of 20.9 kDa. IFNW1 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IFNW1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .
Citations
More Info
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Synonyms
IFN omega-1, IFN alpha-II-1, IFNW1.
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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
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.
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Background
Interferons, a family of signaling proteins, play a pivotal role in the immune system’s defense against viral infections and other threats. Among these, Interferon W1 (IFNW1), a member of the Type I interferon family, has emerged as a key player in orchestrating antiviral responses and modulating immune reactions. This research embarks on a detailed exploration of the IFNW1 protein, unveiling its structural intricacies, signaling pathways, and its broader implications in immune regulation and disease. By delving into IFNW1, scientists aim to comprehend the nuances of its functions, decipher its interactions within the complex interferon network, and explore its potential applications in therapeutic interventions and beyond.
Structural Insights into IFNW1:
IFNW1, like other Type I interferons, exhibits a unique tertiary structure that enables it to interact with specific cell surface receptors. This interaction triggers a cascade of events, leading to the activation of various antiviral genes and immune modulatory pathways. Understanding the structural basis of IFNW1 is crucial for elucidating its binding affinities, biological activities, and its significance in immune responses.
Signaling Pathways and Antiviral Defense:
IFNW1 engages with its cognate receptors, initiating Janus kinase (JAK)-Signal Transducer and Activator of Transcription (STAT) signaling pathways. This activation leads to the transcription of interferon-stimulated genes (ISGs) with potent antiviral properties. IFNW1’s ability to induce an antiviral state in infected and neighboring cells is fundamental for restricting viral replication and curtailing the spread of infections. Additionally, IFNW1 plays a role in modulating adaptive immune responses, contributing to the broader immune defense mechanisms.
IFNW1 in Immunomodulation and Disease:
Beyond its antiviral functions, IFNW1 is implicated in immunomodulation and disease pathogenesis. Dysregulation of IFNW1 signaling is associated with autoimmune disorders, including lupus and rheumatoid arthritis, highlighting its involvement in immune-related diseases. Moreover, IFNW1 is being explored in cancer immunotherapy, where its ability to modulate the tumor microenvironment and enhance immune surveillance presents opportunities for novel treatment strategies.
Therapeutic Potential and Future Prospects:
The unique properties of IFNW1, particularly its role in immune regulation and antiviral defense, position it as a potential therapeutic target. Research efforts are directed towards harnessing its immunomodulatory functions for developing therapies against infectious diseases, autoimmune disorders, and certain cancers. Additionally, understanding IFNW1’s interactions with other components of the immune system opens avenues for innovative approaches in personalized medicine and targeted immunotherapies.
IFNW1 Protein, as an integral component of the interferon network, stands as a sentinel in the body’s defense against viral invasions and immune dysregulations. Its multifaceted roles in antiviral defense, immune modulation, and disease pathogenesis underscore its significance in biology and medicine. As researchers delve deeper into the intricacies of IFNW1, they pave the way for innovative therapies, immunomodulatory interventions, and a deeper understanding of immune responses. This research not only illuminates the pivotal role of IFNW1 but also holds the promise of transformative advancements in medicine, shaping the future of immunology and disease therapeutics.
What is the molecular weight/Mw of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein has a total Mw of 20.9kDa.
What is the source or expression system of IFNW1 HUMAN, HEK Protein?
HEK293 Cells.
What is the Purity of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNW1 HUMAN, HEK Protein?
The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .
What is the amino acid sequence of IFNW1 HUMAN, HEK Protein?
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.
What applications can IFNW1 HUMAN, HEK Protein be used in?
IFNW1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNW1 HUMAN, HEK Protein?
The endotoxin level is minimal, IFNW1 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.
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Name :
NTS HumanDescription:
Neurotensin Human Recombinant
NTS, Neurotensin, NT/N, NMN-125, NTS1, NN, Neurotensin/Neuromedin N, NT.
Product # :
PRO-1311Price :
Quantity :
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Shipped with Ice Packs
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Description
NTS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (24-170 a.a.) and having a molecular mass of 19.9kDa.NTS is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NTS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
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Synonyms
NTS, Neurotensin, NT/N, NMN-125, NTS1, NN, Neurotensin/Neuromedin N, NT.
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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 MGSHMSDSEE EMKALEADFL TNMHTSKISK AHVPSWKMTL LNVCSLVNNL NSPAEETGEV HEEELVARRK LPTALDGFSL EAMLTIYQLH KICHSRAFQH WELIQEDILD TGNDKNGKEE VIKRKIPYIL KRQLYENKPR RPYILKRDSY YY.
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 :
IHH MouseDescription:
Indian Hedgehog Mouse Recombinant
Indian hedgehog protein, IHH, HHG-2, BDA1.
Product # :
CYT-398Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IHH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0μg/ml corresponding to a specific activity of 100-334units/mg.
Citations
More Info
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Introduction
IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.
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Synonyms
Indian hedgehog protein, IHH, HHG-2, BDA1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IHH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IHH 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 IHH 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
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.
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Background
What is the molecular weight/Mw of IHH MOUSE Protein?
IHH MOUSE Protein has a total Mw of 19.8kDa.
What is the source or expression system of IHH MOUSE Protein?
Escherichia Coli.
What is the Purity of IHH MOUSE Protein?
IHH MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IHH MOUSE Protein?
Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0μg/ml corresponding to a specific activity of 100-334units/mg.
What is the amino acid sequence of IHH MOUSE Protein?
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.
What applications can IHH MOUSE Protein be used in?
IHH MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IHH MOUSE Protein?
The endotoxin level is minimal, IHH 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 :
STMN1 HumanDescription:
Stathmin-1 Human Recombinant
Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.
Product # :
PRO-676Price :
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Shipped with Ice Packs
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Description
Recombinant Human Stathmin-1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-149 a.a) and having a molecular mass of 19.4 kDa. STMN1 is fused to 20 amino acid His Tga at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STMN1 protein solution contains 20mM Tris-HCl, pH-8 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
STMN1 takes part in the regulation of the microtubule filament structure by destabilizing microtubules. STMN1 promotes the disassembly of microtubules and prevents assembly. STMN1 is a ubiquitous cytosolic phosphoprotein which functions as an intracellular relay integrating regulatory signals of the cellular environment. Stathmin functions as an Oncoprotein in regulation of the cell cycle. Stathmin mutation results in uncontrolled cell proliferation. Stathmin expression associates with cervical carcinogenesis and tumor progression, thus Stathmin is an important prognostic marker in cervical carcinoma. STMN1, takes part in the prevenative progression of ER-positive primary in breast cancer. Somatic mutation in STMN1 effects cell homeostasis that leads to tumorigenicity.
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Synonyms
Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.
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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 MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL ERLREKDKHI EEVRKNKESK DPADETEAD.
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 :
TBCEL HumanDescription:
Tubulin Folding Cofactor E-Like Human Recombinant
Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
Product # :
PRO-030Price :
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Shipped with Ice Packs
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Description
TBCEL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. The TBCEL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TBCEL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.
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Synonyms
Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
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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 MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.
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 :
TCL1B HumanDescription:
T-cell Leukemia/Lymphoma 1B Human Recombinant
T-Cell Leukemia/Lymphoma 1B, Oncogene TCL-1B, Syncytiotrophoblast-Specific Protein, SYN-1, TML1, T-Cell Leukemia/Lymphoma Protein 1B, T-Cell Lymphoma/Leukemia 1B, TCL1/ MTCP1-Like 1, TCL1, Oncogene TCL1B, TCL1/MTCP1-Like Protein 1.
Product # :
PRO-1749Price :
Quantity :
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Shipped with Ice Packs
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Description
TCL1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (1-128a.a) and having a molecular mass of 17.2kDa. TCL1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TCL1B protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
T-cell leukemia/lymphoma 1B, also known as TCL1B is a member of the TCL1 family. TCL1B is expressed in a variety of tissues as well as the placenta and testis. Moreover, TCL1B enhances the phosphorylation and activation of AKT1 and AKT2.
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Synonyms
T-Cell Leukemia/Lymphoma 1B, Oncogene TCL-1B, Syncytiotrophoblast-Specific Protein, SYN-1, TML1, T-Cell Leukemia/Lymphoma Protein 1B, T-Cell Lymphoma/Leukemia 1B, TCL1/ MTCP1-Like 1, TCL1, Oncogene TCL1B, TCL1/MTCP1-Like Protein 1.
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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
MGSSHHHHHH SSGLVPRGSH MGSMASEASV RLGVPPGRLW IQRPGIYEDE EGRTWVTVVV RFNPSRREWA RASQGSRYEP SITVHLWQMA VHTRELLSSG QMPFSQLPAV WQLYPGRKYR AADSSFWEIA DHGQIDSMEQ LVLTYQPERK D
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 :
TNFRSF10C HumanDescription:
TRAIL Receptor-3 Human Recombinant
Tumor Necrosis Factor Receptor Superfamily, Member 10c, Decoy Without An , Intracellular Domain, TRAILR3, DCR1, TRID, TNF-Related Apoptosis-Inducing Ligand Receptor, Antagonist Decoy Receptor For TRAIL/Apo-2L, Decoy TRAIL Receptor Without Death Domain, Lymphocyte Inhibitor Of TRAIL, Decoy Receptor,TRAIL-R, LIT,Tumor Necrosis Factor Receptor Superfamily Member 10C, TRAIL Receptor Without an Intracellular Domain, Cytotoxic TRAIL Receptor, TRAIL Receptor, CD263 Antigen, DCR1-TNFR, CD263.
Product # :
CYT-889Price :
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Shipped with Ice Packs
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Description
TNFRSF10C Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (26-236 a.a) and having a molecular mass of 24.6 kDa.TNFRSF10C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFRSF10C protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TRAIL Receptor-3, also known as TNFRSF10C belongs to theTNF-receptor super family. TNFRSF10C contains an extracellular TRAIL-binding domain as well as a transmembranedomain, however no cytoplasmic death domain. Furthermore, TNFRSF10C is not capable of inducing apoptosis, and is considered toact as an antagonistic receptor which protects cells from TRAIL-induced apoptosis.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily, Member 10c, Decoy Without An , Intracellular Domain, TRAILR3, DCR1, TRID, TNF-Related Apoptosis-Inducing Ligand Receptor, Antagonist Decoy Receptor For TRAIL/Apo-2L, Decoy TRAIL Receptor Without Death Domain, Lymphocyte Inhibitor Of TRAIL, Decoy Receptor,TRAIL-R, LIT,Tumor Necrosis Factor Receptor Superfamily Member 10C, TRAIL Receptor Without an Intracellular Domain, Cytotoxic TRAIL Receptor, TRAIL Receptor, CD263 Antigen, DCR1-TNFR, CD263.
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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
MGSSHHHHHH SSGLVPRGSH MGSATTARQE EVPQQTVAPQ QQRHSFKGEE CPAGSHRSEH TGACNPCTEG VDYTNASNNE PSCFPCTVCK SDQKHKSSCT MTRDTVCQCK EGTFRNENSP EMCRKCSRCP SGEVQVSNCT SWDDIQCVEE FGANATVETP AAEETMNTSP GTPAPAAEET MNTSPGTPAP AAEETMTTSP GTPAPAAEET MTTSPGTPAP AAEETMTTSP GTPA.
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 :
TNNI1 HumanDescription:
Troponin I Type 1 Human Recombinant
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
Product # :
PRO-1269Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNNI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.8kDa.TNNI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNNI1 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.
Citations
More Info
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Introduction
Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.
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Synonyms
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
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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 MPEVERKPKI TASRKLLLKS LMLAKAKECW EQEHEEREAE KVRYLAERIP TLQTRGLSLS ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK VMDLRGKFKR PPLRRVRVSA DAMLRALLGS KHKVSMDLRA NLKSVKKEDT EKERPVEVGD WRKNVEAMSG MEGRKKMFDA AKSPTSQ
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 :
KRT14 Human, HisDescription:
Cytokeratin 14 Human Recombinant, His Tag
Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.
Product # :
PRO-941Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KRT14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 492 amino acids (1-472 a.a.) and having a molecular mass of 53.8kDa.KRT14 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KRT14 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.
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Synonyms
Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.
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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 MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL SVSSSRFSSG GAYGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGTGLGGGF GGGFAGGDGL LVGSEKVTMQ NLNDRLASYL DKVRALEEAN ADLEVKIRDW YQRQRPAEIK
DYSPYFKTIE DLRNKILTAT VDNANVLLQI DNARLAADDF RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE SLKEELAYLK KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN
LEIELQSQLS MKASLENSLE ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI LLDVKTRLEQ EIATYRRLLE GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT KVMDVHDGKV VSTHEQVLRT KN.
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 :
Leptin tA Rat, PEGDescription:
Leptin Antagonist Triple Mutant Pegylated Rat Recombinant
Product # :
CYT-567Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Rat Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Leptin Antagonist Triple Mutant Rat Recombinant half-life in circulation after SC injection was over 20 hours.
Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Rat Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
TSSC4 HumanDescription:
Tumor Suppressing Subtransferable Candidate 4, Human Recombinant
Tumor suppressing subtransferable candidate 4, Tumor-suppressing STF cDNA 4 protein, Tumor-suppressing subchromosomal transferable fragment candidate gene 4 protein, protein TSSC4.
Product # :
PRO-1021Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TSSC4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 36.8 kDa.TSSC4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TSSC4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TSSC4 is a member of the TSSC4 family. TSSC4 protein is one of quite a few tumor-suppressing subtransferable fragments found in the imprinted gene domain of 11p15.5, a significant tumor-suppressor gene section. Modifications in this section are linked to the Beckwith-Wiedemann syndrome, rhabdomyosarcoma, Wilms tumor, adrenocortical carcinoma, and breast, ovarian, and lung cancer. TSSC4 takes part in malignancies and disease that include this section in addition to hematopoietic cell function. TSSC4 is broadly expressed in virtually all adult tissues, and is found in fetal liver, brain, lung and kidney.
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Synonyms
Tumor suppressing subtransferable candidate 4, Tumor-suppressing STF cDNA 4 protein, Tumor-suppressing subchromosomal transferable fragment candidate gene 4 protein, protein TSSC4.
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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 MGSHMAEAGT GEPSPSVEGE HGTEYDTLPS DTVSLSDSDS DLSLPGGAEV EALSPMGLPG EEDSGPDEPP SPPSGLLPAT VQPFHLRGMS STFSQRSRDI FDCLEGAARR APSSVAHTSM SDNGGFKRPL APSGRSPVEG LGRAHRSPAS PRVPPVPDYV AHPERWTKYS LEDVTEVSEQ SNQATALAFL GSQSLAAPTD CVSSFNQDPS SCGEGRVIFT KPVRGVEARH ERKRVLGKVG EPGRGGLGNP ATDRGEGPVE LAHLAGPGSP EAEEWGSPHG GLQEVEALSG SVHSGSVPGL PPVETVGFHG SRKRSRDHFR NKSSSPEDPG AEV
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 :
CXCL15 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
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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.Citations
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.
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Background
What is the molecular weight/Mw of CXCL15 MOUSE Protein?
CXCL15 MOUSE Protein has a total Mw of 16.4kDa.
What is the source or expression system of CXCL15 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL15 MOUSE Protein?
CXCL15 MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL15 MOUSE Protein?
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.
What is the amino acid sequence of CXCL15 MOUSE Protein?
QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.
What applications can CXCL15 MOUSE Protein be used in?
CXCL15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL15 MOUSE Protein?
The endotoxin level is minimal, CXCL15 MOUSE Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL15 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL15 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
RAC1 Human, HisDescription:
Ras-Related C3 Botulinum Toxin substrate 1 Human Recombinant, His Tag
P21-RAC1, RAC-1, RAC1, RAS-like protein TC25, MIG5, Cell-migration-inducing gene 5 protein,Ras-related C3 botulinum toxin substrate 1, rho family small GTP binding protein Rac1, TC-25, MGC111543.
Product # :
PRO-731Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Ras-Related C3 Botulinum Toxin substrate 1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 23.6 kDa. RAC1 contains a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RAC1 His Tag protein solution contains 20mM Tris-HCl pH7.5, 1mM EDTA, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
RAC1 is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. RAC-1 regulates the actin cytoskeleton but also other cellular processes. RAC1 have been shown to be involved in the regulation of cell-cell adhesion.
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Synonyms
P21-RAC1, RAC-1, RAC1, RAS-like protein TC25, MIG5, Cell-migration-inducing gene 5 protein,Ras-related C3 botulinum toxin substrate 1, rho family small GTP binding protein Rac1, TC-25, MGC111543.
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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).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG QEDYDRLRPLSYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSALTQRGLKTVFD EAIRAVLCPP PVKKRKRKCL LL.
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 :
YWHAH Human, HisDescription:
Tyr-3/Trp-5 Monooxygenase Activation Protein ETA Human Recombinant, His Tag
14-3-3 ETA, YWHAH, YWHA1, Protein AS1, Tyr-3/Trp-5 Monooxygenase Activation Protein ETA.
Product # :
PKA-347Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
YWHAH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 266 amino acids and having a molecular mass of 30.3 kDa. YWHAH is fused to an N-Terminal His Tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
YWHAH solution containing 20mM Tris pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
YWHAH belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. 14-3-3 ETA is found in plants and mammals, and there is 99% identity to the mouse, rat and bovine orthologs. YWHAH gene contains a 7 base pair repeat sequence in its 5' UTR, and changes in the number of this repeat has been associated with early-onset schizophrenia.
14-3-3 eta is specific to the site of joint inflammation.
14-3-3 proteins are colocalized with Lewy bodies in Parkinson disease, though there is no specific staining for the 14-3-3 eta subunit.
There are 3 different isoforms types of 14-3-3: Beta, Gamma and ETA that are DAL-1/Protein 4.1B-binding proteins. -
Synonyms
14-3-3 ETA, YWHAH, YWHA1, Protein AS1, Tyr-3/Trp-5 Monooxygenase Activation Protein ETA.
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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 MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LSLLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEQMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN.
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 :
YWHAZ HumanDescription:
Tyr-3/Trp- 5 Monooxygenase Activation Protein Zeta Human Recombinant
YWHAZ, KCIP-1, MGC111427, MGC126532, MGC138156, 14-3-3 protein zeta/delta, Protein kinase C inhibitor protein 1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Zeta, 14-3-3 Zeta.
Product # :
PKA-257Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
YWHAZ fused to 37 His Tag at N-terminus Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 282 amino acids (1-245) and having a molecular mass of 32kDa.YWHAZ is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
YWHAZ solution containing 1xPBS pH-7.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
YWHAZ accession number NP_ 663723 belongs to the 14-3-3 family of proteins which are in charge for checkpoint control, apoptotic & nutrient sensing pathways as well as signal transduction by binding to phosphoserine-containing proteins. The 14-3-3 protein family is found in both plants and mammals, and KCIP-1 protein is 99% identical to the mouse, rat and sheep orthologs. KCIP-1 interacts with IRS1 protein, signifying a role in regulating insulin. 14-3-3 proteins are highly conserved and ubiquitously expressed. YWHAZ function as an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAZ binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
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Synonyms
YWHAZ, KCIP-1, MGC111427, MGC126532, MGC138156, 14-3-3 protein zeta/delta, Protein kinase C inhibitor protein 1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Zeta, 14-3-3 Zeta.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
YWHAZ Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMDK NELVQKAKLA EQAERYDDMA ACMKSVTEQG AELSNEERNL LSVAYKNVVG ARRSSWRVVS SIEQKTEGAE KKQQMAREYR EKIETELRDI CNDVLSLLEK FLIPNASQAE SKVFYLKMKG DYYRYLAEVA AGDDKKGIVD QSQQAYQEAF EISKKEMQPT HPIRLGLALN FSVFYYEILN SPEKACSLAK TAFDEAIAEL DTLSEESYKD STLIMQLLRD NLTLWTSDTQ GDEAEAGEGG EN.
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 :
IL1B Mouse, His ActiveDescription:
Interleukin-1 beta Human Recombinant, His Tag BioActive
Interleukin 1 beta, IL-1b, IL-1beta, Catabolin, H1, IL 1,IL 1 beta,IL-1 beta, IL1 BETA,IL1B,IL1B_HUMAN,IL1F2, Interleukin 1 beta, Interleukin-1 beta, OAF,OTTHUMP00000162031, Preinterleukin 1 beta,Pro interleukin 1 beta.
Product # :
CYT-1149Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL1B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (118-269 a.a) and having a molecular mass of 21kDa.IL1B is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IL1B protein (1mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED50 range < 0.1 ng/ml.
SDS-PAGE
Citations
More Info
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Introduction
Interleukin-1 beta is a cytokine that causes inflammation and can regulate angiogenesis through interaction with vascular endothelial cells or promoting the creation of proangiogenic modulators through the paracrine system. The cytokine causes migration and proliferation of endothelial cells, creation of mediators to inflammation, expression of adhesion-molecules & recruit of leukocyte cells. Interleukin-1 beta was found crucial for the process of tumors in various organism models.
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Synonyms
Interleukin 1 beta, IL-1b, IL-1beta, Catabolin, H1, IL 1,IL 1 beta,IL-1 beta, IL1 BETA,IL1B,IL1B_HUMAN,IL1F2, Interleukin 1 beta, Interleukin-1 beta, OAF,OTTHUMP00000162031, Preinterleukin 1 beta,Pro interleukin 1 beta.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.
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Background
What is the molecular weight/Mw of IL1B MOUSE, HIS ACTIVE Protein?
IL1B MOUSE, HIS ACTIVE Protein has a total Mw of 21kDa.
What is the source or expression system of IL1B MOUSE, HIS ACTIVE Protein?
Escherichia Coli.
What is the Purity of IL1B MOUSE, HIS ACTIVE Protein?
IL1B MOUSE, HIS ACTIVE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IL1B MOUSE, HIS ACTIVE Protein?
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED50 range < 0.1 ng/ml.
What is the amino acid sequence of IL1B MOUSE, HIS ACTIVE Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.
What applications can IL1B MOUSE, HIS ACTIVE Protein be used in?
IL1B MOUSE, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL1B MOUSE, HIS ACTIVE Protein?
The endotoxin level is minimal, IL1B MOUSE, 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.
- View Data Sheet
Name :
CSK HumanDescription:
C-Src Tyrosine Kinase Human Recombinant
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
Product # :
PKA-062Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CSK Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-450) and having a molecular mass of 53.1 kDa.The CSK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSK protein (0.5mg/ml) is containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
C-Src Tyrosine Kinase, also known as CSK, regulates cell growth, migration, differentiation, and immune response. CSK Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases. CSK is a protein coding gene which suppresses signaling by several surface receptors. Among CSK's related pathways are PI-3K cascade and Signaling by FGFR.
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Synonyms
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
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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 MGSMSAIQAA WPSGTECIAK YNFHGTAEQD LPFCKGDVLT IVAVTKDPNW YKAKNKVGRE GIIPANYVQK REGVKAGTKL SLMPWFHGKI TREQAERLLY PPETGLFLVR ESTNYPGDYT LCVSCDGKVE HYRIMYHASK LSIDEEVYFE NLMQLVEHYT SDADGLCTRL IKPKVMEGTV AAQDEFYRSG WALNMKELKL LQTIGKGEFG DVMLGDYRGN KVAVKCIKND ATAQAFLAEA SVMTQLRHSN LVQLLGVIVE EKGGLYIVTE YMAKGSLVDY LRSRGRSVLG GDCLLKFSLD VCEAMEYLEG NNFVHRDLAA RNVLVSEDNV AKVSDFGLTK EASSTQDTGK LPVKWTAPEA LREKKFSTKS DVWSFGILLW EIYSFGRVPY PRIPLKDVVP RVEKGYKMDA PDGCPPAVYE VMKNCWHLDA AMRPSFLQLR EQLEHIKTHE LHL.
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 :
Activin A Human PlantDescription:
Activin A Human Recombinant, Plant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-052Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
Citations
More Info
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Introduction
Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Activin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin 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 Activin 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
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.
What is the source or expression system of Activin A Protein?
Nicotinia
What is the Purity of Activin A Protein?
Activin A Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological functionality of Activin-A Protein will be determined in the future.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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Serological Identification
The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin 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 :
LGMN MouseDescription:
Legumain Mouse Recombinant
Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.
Product # :
ENZ-933Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (18-435a.a.) and having a molecular mass of 48.6kDa. LGMN is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LGMN 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.
sds-page
Citations
More Info
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Introduction
Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.
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Synonyms
Legumain, Asparaginyl endopeptidase, Protease, cysteine 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
VPVGVDDPED GGKHWVVIVA GSNGWYNYRH QADACHAYQI IHRNGIPDEQ IIVMMYDDIA NSEENPTPGV VINRPNGTDV YKGVLKDYTG EDVTPENFLA VLRGDAEAVK GKGSGKVLKS GPRDHVFIYF TDHGATGILV FPNDDLHVKD LNKTIRYMYE HKMYQKMVFY IEACESGSMM NHLPDDINVY ATTAANPKES SYACYYDEER GTYLGDWYSV NWMEDSDVED LTKETLHKQY HLVKSHTNTS HVMQYGNKSI STMKVMQFQG MKHRASSPIS LPPVTHLDLT PSPDVPLTIL KRKLLRTNDV KESQNLIGQI QQFLDARHVI EKSVHKIVSL LAGFGETAER HLSERTMLTA HDCYQEAVTH FRTHCFNWHS VTYEHALRYL YVLANLCEAP YPIDRIEMAM DKVCLSHYLE HHHHHH.
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 :
IL 17 A/F MouseDescription:
Interleukin-17 A/F Heterodimer Mouse Recombinant
IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.
Product # :
CYT-640Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-17 A/F Mouse Recombinant produced in E.Coli is a heterodimeric, non-glycosylated polypeptide comprised of IL17A monomeric subunit & and IL17F monomeric subunit containing a total of 266 amino acids and having a total molecular mass of 29.8kDa. The IL-17 A/F is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Human IL-17A/F is a 40kDa glycoprotein which is secreted as a disulfide-linked heterodimer. IL-17A/F consists of two proteins of the IL-17 family, IL-17A and IL17F. Proteins of the 6 homodimeric IL17 family show a cysteine knot motif that contains two disulfide-bonds. Human IL17A is produced as a 155 a.a precursor that includes a 23 amino acids signal sequence and a 132 amino acid chain that includes an N-linked glycosylation site. Human IL17F is produced as a 153 amino acid precursor with a 20 amino acid signal sequence and a 133 amino acid region. Similar to IL17A, IL17F also has an N-linked glycosylation site. Both proteins (IL17A & IL17F) share 50% amino acid sequence identity. Human IL17A & IL17F show approximately 60% homology in their amino acid sequence to mouse IL-17A and IL-17F. Interleukin-17A/F and IL17A, IL17F homodimers are manufactured by activted CD4+ T cells, called Th17. IL-23 causes Th17 lymphocytes to manufacture IL-17A/F. IL17RA and IL17RC form a heterodimer for the binding of IL17A and IL17F. IL-17A/F binds IL-17RA. Interleukin-17A/F induces chemokine production and airway neutrophilia with intermediate potency between IL17A (most potent) and IL17F (least potent).
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Synonyms
IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse IL17 A/F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse IL17 A/F 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 Mouse IL17 A/F 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
RKNPKAGVPALQKAGNCPPLEDNTVRVDIRIFNQNQGISVPREFQNRSSSP
WDYNITRDPHRFPSEIAEAQCRHSGCINAQGQEDSTMNSVAIQQEILVLRR
EPQGCSNSFRLEKMLLKVGCTCVKPIVHQAAAAIIPQSSACPNTEAKDFLQ
NVKVNLKVFNSLGAKVSSRRPSDYLNRSTSPWTLHRNEDPDRYPSVIWE
AQCRHQRCVNAEGKLDHHMNSVLIQQEILVLKREPESCPFTFRVEKMLV
GVGCTCVASIVRQAA.
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 :
Recombinant TNF-a AntibodyDescription:
Recombinant Anti Human Tumor Necrosis Factor-Alpha
Product # :
ANT-599Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant TNF-a Antibody is a recombinant human IgG1 monoclonal antibody specific for human tumor necrosis factor (TNF). Recombinant TNF-a Antibody is produced by recombinant DNA technology in a Chinese Hamster Ovary mammalian cell expression system in a serum-free medium and has a molecular weight of approximately 148 kDa.
Source
CHO.
Formulation
The Recombinant TNF-a Antibody 53mg/ml solution contains 6.16 mg/ml of sodium chloride, 0.86 mg/ml of monobasic sodium phosphate dihydrate, 1.53 mg/ml of dibasic sodium phosphate dihydrate, 0.3 mg/ml of sodium citrate, 1.30 mg/ml of citric acidmonohydrate, 12 mg/ml of mannitol, 1mg/ml of polysorbate 80, pH-5.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The EC50 as determined by L929 cell proliferation assay for neutralization reaction between TNF-a Antibody and TNFA, Perform a comparison of a dilution series of the Sample solution with a dilution series of the Standard solution, measured potency was found to be 1.2 X 104EU/mg.Citations
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, tumorigenesisand 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. -
Physical Appearance
Clear and colorless solution.
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Stability
Recombinant TNF-a Antibody should be stored between 2-8°C and should be protected from light. DO NOT FREEZE. DO NOT SHAKE.
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Amino Acid Sequence
LIGHT CHAIN
DIQMTQSPSSLSASVGDRVTITCRASQGIRNYLAWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDF
TLTISSLQPEDVATYYCQRYNRAPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
HEAVY CHAIN
EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYAMHWVRQAPGKGLEWVSAITWNSGHIDYADSVEGRFTISR
DNAKNSLYLQMNSLRAEDTAVYYCAKVSYLSTASSLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTA
ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVD
KKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV
HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRD
ELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM
HEALHNHYTQKSLSLSPGK.
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 :
METRN MouseDescription:
Meteorin Mouse Recombinant
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
Product # :
PRO-2241Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
METRN 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.
Citations
More Info
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Introduction
Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
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Synonyms
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
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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
GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD HHHHHH.
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.