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Name :
RXRA HumanDescription:
Retinoid X Receptor Alpha Human Recombinant
Retinoic acid receptor RXR-alpha, Retinoid X receptor alpha, Nuclear receptor subfamily 2 group B member 1, RXRA, NR2B1, FLJ00280, FLJ00318, FLJ16020, FLJ16733, MGC102720, RXR Alpha, RXR-a.
Product # :
PRO-437Price :
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Shipped with Ice Packs
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Description
RXRA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (111-228) & having a molecular mass of 13.6 kDa.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) containing 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM ?-Mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The retinoid X receptor (RXR) is a pleiotropic nuclear receptor transcription factor that interacts with a variety of nuclear receptor dimeric partner. RXR binds cognate response elements as a homodimer in the presence of its ligand, 9-cis retinoic acid, or as a heterodimer with other members of the nuclear hormone receptor superfamily including retinoic acid receptors (RAR), thyroid hormone receptors (TR), vitamin D receptors and peroxisome proliferators-activated receptors (PPAR). The RXR family includes three different isoforms; RXR a, b, g . Human RXR a gene is localized on 9q34.9 and encodes two major isoforms (RXR a1, RXR a2). The DNA binding domain of RXR (111-228aa) was purified by using conventional column chromatography techniques.
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Synonyms
Retinoic acid receptor RXR-alpha, Retinoid X receptor alpha, Nuclear receptor subfamily 2 group B member 1, RXRA, NR2B1, FLJ00280, FLJ00318, FLJ16020, FLJ16733, MGC102720, RXR Alpha, RXR-a.
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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
MLGLNGVLKV PAHPSGNMAS FTKHICAICG DRSSGKHYGV YSCEGCKGFF KRTVRKDLTY TCRDNKDCLI DKRQRNRCQY CRYQKCLAMG MKREAVQEER QRGKDRNENE VESTSSANE.
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 :
MMADHC HumanDescription:
Methylmalonic Aciduria cblD type, with Homocystinuria Human Recombinant
Chromosome 2 Open Reading Frame 25, Methylmalonic Aciduria (Cobalamin Deficiency) CblD Type With Homocystinuria, Methylmalonic Aciduria And Homocystinuria Type D Protein Mitochondrial, Protein C2orf25 Mitochondrial, CL25022, C2orf25, cblD.
Product # :
PRO-1850Price :
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Description
MMADHC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (39-296) and having a molecular mass of 31.0 kDa. MMADHC is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The MMADHC solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MMADHC is a mitochondrial protein which takes part in an early step of vitamin B1 2 metabolism. Vitamin B12 (cobalamin) is vital for regular development and existence in humans. Mutations in MMADHC can result in methylmalonic aciduria and homocystinuria type cblD, a cobalamin metabolism syndrome which is characterized by decreased levels of the coenzymes methylcobalamin and adenosylcobalamin.
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Synonyms
Chromosome 2 Open Reading Frame 25, Methylmalonic Aciduria (Cobalamin Deficiency) CblD Type With Homocystinuria, Methylmalonic Aciduria And Homocystinuria Type D Protein Mitochondrial, Protein C2orf25 Mitochondrial, CL25022, C2orf25, cblD.
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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 MGSSDESHVA AAPPDICSRT VWPDETMGPF GPQDQRFQLP GNIGFDCHLN GTASQKKSLV HKTLPDVLAE PLSSERHEFV MAQYVNEFQG NDAPVEQEIN SAETYFESAR VECAIQTCPE LLRKDFESLF PEVANGKLMI LTVTQKTKND MTVWSEEVEI EREVLLEKFI NGAKEICYAL RAEGYWADFI DPSSGLAFFG PYTNNTLFET DERYRHLGFS VDDLGCCKVI RHSLWGTHVV VGSIFTNATP DSHIMKKLSG N
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 :
ADPRH HumanDescription:
ADP-Ribosylarginine Hydrolase Human Recombinant
[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.
Product # :
ENZ-631Price :
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Description
ADPRH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 42.1kDa.ADPRH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ADPRH solution (0.5mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ADP-ribosylarginine hydrolase (ADPRH) is a member of the ADP-ribosylglycohydrolase family. ADPRH catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. The human ADPRH enzyme is DTT-independent as opposed to the rat and mouse enzymes, which require DTT for maximal activity.
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Synonyms
[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.
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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 MGSHMEKYVA AMVLSAAGDA LGYYNGKWEF LQDGEKIHRQ LAQLGGLDAL DVGRWRVSDD TVMHLATAEA LVEAGKAPKL TQLYYLLAKH YQDCMEDMDG RAPGGASVHN AMQLKPGKPN GWRIPFNSHE GGCGAAMRAM CIGLRFPHHS QLDTLIQVSI ESGRMTHHHP TGYLGALASA LFTAYAVNSR PPLQWGKGLM ELLPEAKKYI VQSGYFVEEN LQHWSYFQTK WENYLKLRGI LDGESAPTFP ESFGVKERDQ FYTSLSYSGW GGSSGHDAPM IAYDAVLAAG DSWKELAHRA FFHGGDSDST AAIAGCWWGV MYGFKGVSPS NYEKLEYRNR
LEETARALYS LGSKEDTVIS L.
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 :
AGRP HumanDescription:
Agouti–Related Protein Human Recombinant
ART, AGRT, ASIP2, MGC118963, AGRP.
Product # :
HOR-283Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Human Agouti-related protein is created as a recombinant protein with N-terminal fusion of His Tag.The Human Agouti-related protein His-Tagged Fusion Protein, produced in E. coli, is 14.4 kDa (calculated) protein containing 112 amino acid residues of the human AGRP and 16 additional amino acid residues - His Tag, thrombin cleavage site (highlighted).The AGRP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AGRP protein was lyophilized from 0.5mg/ml in 5mM TRIS, 25mM NaCl, pH 7.5.
Purity
Purity of Agouti–related protein recombinant human is >95% as determined by SDS-PAGE.
More Info
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Introduction
Agouti-related protein is an endogenous antagonist of hypothalamic alpha-melanocortin receptors MC3R and MC4R with potent orexigenic activity. Although a complete deletion of the AGRP gene does not produce any significant metabolic phenotypes, reduction in AGRP expression by RNA interference is associated with increased metabolic rate along with reduced weight gain. In hypothalamus, it is produced by neurons in the medial portion of arcuate nucleus, which produce also the potent orexigenic peptide Neuropeptide Y (NP-Y). Another site of central AGRP production is the hypothalamic nucleus. AGRP encompasses 132 amino acid residues and its alpha-melanocortin inhibiting activity results in a 34 amino acid cystine knot domain within the C-terminal (87-132) portion of the protein. Both AGRP and NP-Y expression was shown to be suppressed by leptin. Central administration of AGRP induces hyperphagia and increased gain in body weight in rodents, but may also exert metabolic effects even when hyperphagia is prevented. In the absence of hyperphagia, intracerebralventricular administration of AGRP caused significant increases in plasma leptin and insulin concentrations (twofold and 1.5-fold, respectively) and fat pad mass.
In the periphery, AGRP mRNA was found in adrenal glands, lung, testis, ovary, skeletal muscle and adipose tissue in humans or rodents. In the adrenals, it was shown that AGRP antagonizes glucosteroid production mediated by MC4R. AGRP could then modulate locally the functions of some peripheral tissues such as adrenals.
In human and rat serum, detectable levels of AGRP-like activity were reported in the lower picogram range. The serum AGRP levels were elevated in obese humans compared to lean controls and increased with fasting in rats. -
Synonyms
ART, AGRT, ASIP2, MGC118963, AGRP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized AGRP protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MKHHHHHHHM LVPRGSAQMG LAPMEGIRRP DQALLPELPG LGLRAPLKKT TAEQAEEDLL QEAQALAEVL DLQDREPRSS RRCVRLHESC LGQQVPCCDP CATCYCRFFN AFCYCRKLGT AMNPCSRT.
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 :
HLA-C HumanDescription:
Major Histocompatibility Complex Class I C Human Recombinant
Major Histocompatibility Complex Class I- C, D6S204, HLA-JY3, PSORS1, HLC-C, HLA Class I Histocompatibility Antigen C Alpha Chain, Human Leukocyte Antigen-C Alpha Chain, Major Histocompatibility Antigen HLA-C, MHC Class I Antigen Heavy Chain HLA-C.
Product # :
PRO-1562Price :
Quantity :
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Shipped with Ice Packs
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Description
HLA-C Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (25-308) and having a molecular mass of 34.9kDa.HLA-C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HLA-C solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Major Histocompatibility Complex Class I C (HLA-C) belongs to the HLA class I heavy chain paralogues. The HLA-C (class I molecule) is a heterodimer comprised of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules have a key role in the immune system by presenting peptides derived from endoplasmic reticulum lumen. Class I molecules are expressed in virtually all cells.
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Synonyms
Major Histocompatibility Complex Class I- C, D6S204, HLA-JY3, PSORS1, HLC-C, HLA Class I Histocompatibility Antigen C Alpha Chain, Human Leukocyte Antigen-C Alpha Chain, Major Histocompatibility Antigen HLA-C, MHC Class I Antigen Heavy Chain HLA-C.
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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 MGSCSHSMRY FDTAVSRPGR GEPRFISVGY VDDTQFVRFD SDAASPRGEP RAPWVEQEGP EYWDRETQKY KRQAQADRVS LRNLRGYYNQ SEDGSHTLQR MSGCDLGPDG RLLRGYDQSA YDGKDYIALN EDLRSWTAAD TAAQITQRKL EAARAAEQLR AYLEGTCVEW LRRYLENGKE TLQRAEPPKT HVTHHPLSDH EATLRCWALG FYPAEITLTW QRDGEDQTQD TELVETRPAG DGTFQKWAAV VVPSGQEQRY TCHMQHEGLQ EPLTLSWEPS SQPTIPI
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 :
DEFB118 HumanDescription:
Beta Defensin 118 Human Recombinant
Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.
Product # :
CYT-714Price :
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- sds-page
Description
DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.
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Synonyms
Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.
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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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.
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Background
Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications
Abstract:
Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.Production and Characterization:
Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD118.Role in Innate Immunity:
BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.Therapeutic Implications:
Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.Conclusion:
Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.What is the molecular weight/Mw of DEFB118 Protein?
DEFB118 Protein has a total Mw of 13.8kDa.
What is the source or expression system of DEFB118 Protein?
Escherichia Coli.
What is the Purity of DEFB118 Protein?
DEFB118 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of DEFB118 Protein?
The biological functionality of DEFB118 Protein will be determined in the future.
What is the amino acid sequence of DEFB118 Protein?
MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.
What applications can DEFB118 Protein be used in?
DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DEFB118 Protein?
The endotoxin level is minimal, DEFB118 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 :
ATP1B1 HumanDescription:
ATPase Transporting Beta 1 Human Recombinant
Sodium/potassium-transporting ATPase subunit beta-1, ATPase, Na+/K+ transporting, beta 1 polypeptide, ATP1B, ATPBS, Sodium/potassium-dependent ATPase subunit beta-1, ATP1B1, ATPaseTransporting Beta 1.
Product # :
PRO-1665Price :
Quantity :
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Shipped with Ice Packs
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Description
ATP1B1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (63-303) and having a molecular mass of 30.4 kDa.ATP1B1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ATP1B1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ATPaseTransporting Beta 1 (ATP1B1) is a part of the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an essential membrane protein accountable for establishing and maintaining the electrochemical gradients of Na and K ions over the plasma membrane. These gradients are vital for osmoregulation, for sodium-coupled transport of a range of organic and inorganic molecules, and for electrical excitability of muscle and nerve. ATP1B1is combined of 2 subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates the number of sodium pumps transported to the plasma membrane through assembly of alpha/beta heterodimers. ATP1B1 is a beta 1 subunit.
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Synonyms
Sodium/potassium-transporting ATPase subunit beta-1, ATPase, Na+/K+ transporting, beta 1 polypeptide, ATP1B, ATPBS, Sodium/potassium-dependent ATPase subunit beta-1, ATP1B1, ATPaseTransporting Beta 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 MGSEFKPTYQ DRVAPPGLTQ IPQIQKTEIS FRPNDPKSYE AYVLNIVRFL EKYKDSAQRD DMIFEDCGDV PSEPKERGDF NHERGERKVC RFKLEWLGNC SGLNDETYGY KEGKPCIIIK LNRVLGFKPK PPKNESLETY PVMKYNPNVL PVQCTGKRDE DKDKVGNVEY FGLGNSPGFP LQYYPYYGKL LQPKYLQPLL AVQFTNLTMD TEIRIECKAY GENIGYSEKD RFQGRFDVKI EVKS.
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 :
ATPIF1 HumanDescription:
ATPase Inhibitory Factor 1 Human Recombinant
ATPase inhibitor mitochondrial, Inhibitor of F(1)F(o)-ATPase, IF(1), IF1, ATPIF1, ATPI, IP, ATPIP.
Product # :
PRO-1154Price :
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Shipped with Ice Packs
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Description
ATPIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (26-106 a.a) and having a molecular mass of 12.2kDa.ATPIF1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ATPIF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ATPase inhibitory factor 1 (ATPIF1) attaches to the C-terminal region of a beta subunit of the F1-ATPase at low pH values and, through interference of the beta and gamma subunit interaction, ATPIF1 controls the activity of the F1 (the hydrophilic catalytic core), F0 (the membrane embedded protein channel) ATPase. ATPIF1 overexpression in a number of human carcinomas additionally reinforces its participation in oncogenesis and offers insight into the transformed metabolism of cancer cells, including the reprogramming of energy metabolism in relation to glycolysis. Endogenous F1F(o)-ATPase inhibitor curbing ATP depletion when the mitochondrial membrane potential drops below a threshold and the F1F(o)-ATP synthase begins hydrolyzing ATP to pump protons out of the mitochondrial matrix.
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Synonyms
ATPase inhibitor mitochondrial, Inhibitor of F(1)F(o)-ATPase, IF(1), IF1, ATPIF1, ATPI, IP, ATPIP.
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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 MGSHMGSDQS ENVDRGAGSI REAGGAFGKR EQAEEERYFR AQSREQLAAL KKHHEEEIVH HKKEIERLQK EIERHKQKIK MLKHDD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IFNG MonkeyDescription:
Interferon-gamma Recombinant Rhesus Macaque
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-1122Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interferon-gamma Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 142 amino acid and having a molecular mass of approximately 16.8kDa.IFNG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens / mitogens.
IFN-gamma, on top of 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 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 IFNG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interferon-gamma Rhesus Macaque should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interferon-gamma Rhesus Macaque 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
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.
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Background
What is the molecular weight/Mw of IFNG MONKEY Protein?
IFNG MONKEY Protein has a total Mw of 16.8kDa.
What is the source or expression system of IFNG MONKEY Protein?
Escherichia Coli.
What is the Purity of IFNG MONKEY Protein?
IFNG MONKEY Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG MONKEY Protein?
The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.
What is the amino acid sequence of IFNG MONKEY Protein?
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.
What applications can IFNG MONKEY Protein be used in?
IFNG MONKEY Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG MONKEY Protein?
The endotoxin level is minimal, IFNG MONKEY 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 :
ST13 HumanDescription:
HSP70 Interacting Protein Human Recombinant
AAG2, SNC6, HSPABP, FAM10A1, FAM10A4, HSPABP1, ST-13, Hsc70-interacting protein, Suppression of tumorigenicity protein 13, Putative tumor suppressor ST13, Protein FAM10A1, Progesterone receptor-associated p48 protein, Renal carcinoma antigen NY-REN-33, ST13, HIP, HOP, P48, PRO0786, FLJ27260, MGC129952.
Product # :
HSP-130Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
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Description
Recombinant Human ST13 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 369 amino acids (12-369 a.a.) and having a molecular mass of 41.3kDa.ST13 human recombinant is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The ST13 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT, 0.1M NaCl & 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
ST13 is an adaptor protein (co-chaperone) that mediates the association of HSP70 & HSP90 and appears in early receptor complexes. ST13 plays a role in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. The expression of ST13 is downregulated in colorectal carcinoma tissue signifying that is candidate tumor suppressor gene. Through common binding to both Hsp70 and Hsp90, ST13 functions as an adaptor that can integrate Hsp70 and Hsp90 interactions. The expression of ST13 decreases in colorectal cancer tissue compared with that in adjacent normal tissue. ST13 is mostly expressed in colorectal epithelia and adenocarcinoma cells. ST13 functions to promote the efficiency of glucocorticoid receptor maturation in cells. The expression levels of the ST13 gene were significantly decreased in primary tumors compared with adjacent mucosa.
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Synonyms
AAG2, SNC6, HSPABP, FAM10A1, FAM10A4, HSPABP1, ST-13, Hsc70-interacting protein, Suppression of tumorigenicity protein 13, Putative tumor suppressor ST13, Protein FAM10A1, Progesterone receptor-associated p48 protein, Renal carcinoma antigen NY-REN-33, ST13, HIP, HOP, P48, PRO0786, FLJ27260, MGC129952.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP DSKKVEEDLK ADEPSSEESD LEIDKEGVIEPDTDAPQEMG DENAEITEEM MDQANDKKVA AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER KREEREIKER IERVKKAREE HERAQREEEA
RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK LSAKFGGQA.
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 :
SULT1C2 HumanDescription:
Sulfotransferase Family, Cytosolic 1C, Member 2 Human Recombinant
Sulfotransferase 1C2, ST1C2, Sulfotransferase 1C1, SULT1C#1, humSULTC2, SULT1C2, SULT1C1, ST1C1.
Product # :
ENZ-047Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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Description
SULT1C2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296a.a.) and having a molecular mass of 37.0kDa. SULT1C2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SULT1C2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Sulfotransferase 1C2 (SULT1C2) is a member the sulfotransferase1 superfamily. SULT1C2 catalyzes the transfer of sulfate from PAPS (3’-phosphoadenosine-5’-phosphosulfate) to phenol-containing compounds, including hormones and neurotransmitters. A short and a long isoform of SULT1C2 exist as a result of alternative splicing events. Sulfotransferase enzymes catalyze the sulfate conjugation of various hormones, neurotransmitters, drugs, and xenobiotic compounds.
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Synonyms
Sulfotransferase 1C2, ST1C2, Sulfotransferase 1C1, SULT1C#1, humSULTC2, SULT1C2, SULT1C1, ST1C1.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MALTSDLGKQ IKLKEVEGTL LQPATVDNWS QIQSFEAKPD DLLICTYPKA GTTWIQEIVD MIEQNGDVEK CQRAIIQHRH PFIEWARPPQ PSGVEKAKAM PSPRILKTHL STQLLPPSFW ENNCKFLYVA RNAKDCMVSY YHFQRMNHML PDPGTWEEYF ETFINGKVVW GSWFDHVKGW WEMKDRHQIL FLFYEDIKRD PKHEIRKVMQ FMGKKVDETV LDKIVQETSF EKMKENPMTN RSTVSKSILD QSISSFMRKG TVGDWKNHFT VAQNERFDEI YRRKMEGTSI NFCMEL.
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 :
TCEAL1 HumanDescription:
Transcription Elongation Factor A (SII)-Like 1 Human Recombinant
Transcription elongation factor A protein-like 1, TCEA-like protein 1, Nuclear phosphoprotein p21/SIIR, Transcription elongation factor S-II protein-like 1, TCEAL1, SIIR, p21, pp21.
Product # :
PRO-507Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TCEAL1 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-159 a.a.) and having a molecular mass of 19.7kDa. The TCEAL1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TCEAL1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Transcription elongation factor A protein-like 1 (TCEAL1) is a member of the transcription elongation factor A (SII)-like (TCEAL) family, which may function as nuclear phosphoproteins that modulate transcription in a promoter context-dependent manner. TCEAL1 is involved in transcriptional regulation. TCEAL1 is expressed in all tissues, especially highly expressed in the heart, ovary, prostate and skeletal muscle.
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Synonyms
Transcription elongation factor A protein-like 1, TCEA-like protein 1, Nuclear phosphoprotein p21/SIIR, Transcription elongation factor S-II protein-like 1, TCEAL1, SIIR, p21, pp21.
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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
MDKPRKENEE EPQSAPKTDE ERPPVEHSPE KQSPEEQSSE EQSSEEEFFP EELLPELLPE MLLSEERPPQ EGLSRKDLFE GRPPMEQPPC GVGKHKLEEG SFKERLARSR PQFRGDIHGR NLSNEEMIQA ADELEEMKRV RNKLMIMHWK AKRSRPYPIL EHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TCL1A HumanDescription:
T-cell Leukemia/Lymphoma 1A Human Recombinant
T-cell leukemia/lymphoma protein 1A, Protein p14 TCL1, Oncogene TCL-1, Oncogene TCL1, TCL1A, TCL1.
Product # :
PRO-726Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
TCL1A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids (1-114 a.a.) and having a molecular mass of 13.4kDa.The TCL1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TCL1A protein solution contains 50mM Tris-HCl buffer (pH7.5) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
TCL1A (T-cell leukemia/lymphoma 1A) is a protein with a possible role in intracellular regulation of T cell signaling. TCL1A enhances cell proliferation, stabilizes mitochondrial membrane potential and promotes cell survival. TCL1A is restricted in the T-cell lineage to immature thymocytes and activated peripheral lymphocytes. TCL1A is preferentially expressed early in T and B-lymphocyte differentiation. Chromosomal anomalies activating TCL1A are found in chronic T-cell leukemias (T-CLL).
TCL1A enhances the phosphorylation and activation of AKT1, AKT2 and AKT3. TCL1A promotes nuclear translocation of AKT1. TCL1A binds to the pleckstrin homology domain of Akt (protein kinase B) family proteins, which facilitates Akt dimerization and activity. By increasing Akt activity, TCL1A can enhance the serine/threonine phosphorylation of major Akt signaling substrates, for example Ikk complex, mTOR, BAD, p70S6 kinase, FOXO transcription factors and GSK3b. These substrates regulate cellular differentiation, growth, survival, and metabolism. -
Synonyms
T-cell leukemia/lymphoma protein 1A, Protein p14 TCL1, Oncogene TCL-1, Oncogene TCL1, TCL1A, TCL1.
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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.
-
Amino Acid Sequence
MAECPTLGEA VTDHPDRLWA WEKFVYLDEK QHAWLPLTIE IKDRLQLRVL LRREDVVLGR PMTPTQIGPS LLPIMWQLYP DGRYRSSDSS FWRLVYHIKI DGVEDMLLEL LPDD.
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 :
Platelet Factor 4 HumanDescription:
Platelet Factor-4 Human Recombinant (CXCL4)
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-350Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CXCL4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.8 kDa.
Source
Escherichia Coli.
Formulation
The CXCL4 protein was filtered (0.2µm) and lyophilized from a concentrated solution containing 20mM PB and 1.5M NaCl, pH 7.4.
Purity
Greater than 97.0% 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 fibroblasts is in a concentration of 1.0-10 ng/ml.
More Info
-
Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
-
Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized CXCL4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL4 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 CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
EAEEDGDLQC LCVKTTSQVR PRHITSLEVI KAGPHCPTAQ LIATLKNGRK ICLDLQAPLY KKIIKKLLES.
-
Background
What is the molecular weight/Mw of PLATELET FACTOR 4 HUMAN Protein?
PLATELET FACTOR 4 HUMAN Protein has a total Mw of 7.8kDa.
What is the source or expression system of PLATELET FACTOR 4 HUMAN Protein?
Escherichia Coli.
What is the Purity of PLATELET FACTOR 4 HUMAN Protein?
PLATELET FACTOR 4 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of PLATELET FACTOR 4 HUMAN Protein?
The biological activity determined by a chemotaxis bioassay using human fibroblasts is in a concentration of 1.0-10 ng/ml.
What is the amino acid sequence of PLATELET FACTOR 4 HUMAN Protein?
EAEEDGDLQC LCVKTTSQVR PRHITSLEVI KAGPHCPTAQ LIATLKNGRK ICLDLQAPLY KKIIKKLLES.
What applications can PLATELET FACTOR 4 HUMAN Protein be used in?
PLATELET FACTOR 4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for PLATELET FACTOR 4 HUMAN Protein?
The endotoxin level is minimal, PLATELET FACTOR 4 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Platelet Factor 4 MouseDescription:
Platelet Factor-4 Mouse Recombinant (CXCL4)
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-245Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CXCL4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 8.2kDa.
Source
Escherichia Coli.
Formulation
The Mouse CXCL4 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 1.5M NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human neutrophils using a concentration range of 10-100ng/ml.
More Info
-
Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily.
-
Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized CXCL4 Mouse Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CXCL4 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 CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VTSAGPEESD GDLSCVCVKT ISSGIHLKHI TSLEVIKAGR HCAVPQLIAT LKNGRKICLD RQAPLYKKVI KKILES.
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Background
What is the molecular weight/Mw of PLATELET FACTOR 4 MOUSE Protein?
PLATELET FACTOR 4 MOUSE Protein has a total Mw of 8.2kDa.
What is the source or expression system of PLATELET FACTOR 4 MOUSE Protein?
Escherichia Coli.
What is the Purity of PLATELET FACTOR 4 MOUSE Protein?
PLATELET FACTOR 4 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of PLATELET FACTOR 4 MOUSE Protein?
Determined by its ability to chemoattract human neutrophils using a concentration range of 10-100ng/ml.
What is the amino acid sequence of PLATELET FACTOR 4 MOUSE Protein?
VTSAGPEESD GDLSCVCVKT ISSGIHLKHI TSLEVIKAGR HCAVPQLIAT LKNGRKICLD RQAPLYKKVI KKILES.
What applications can PLATELET FACTOR 4 MOUSE Protein be used in?
PLATELET FACTOR 4 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for PLATELET FACTOR 4 MOUSE Protein?
The endotoxin level is minimal, PLATELET FACTOR 4 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 :
FGF13 HumanDescription:
Fibroblast Growth Factor 13 Human Recombinant
Fibroblast growth factor 13, FGF-13, Fibroblast growth factor homologous factor 2, FHF-2, FGF13, FHF2.
Product # :
CYT-121Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
FGF13 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.6kDa.The FGF-13 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FGF13 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 0.5M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Fibroblast growth factor 13 (FGF-13) is a member of the large FGF family which has at least 23 members. Most of its members are binding growth factors with a core 120 amino acid (aa) FGF domain which allows for a mutual tertiary structure. Human and mouse FGF13 are 245 aa proteins which arise from genes that show N-terminal alternative splicing. Transcripts for 245 aa, 199 aa, 226 aa, 192 aa and 255 aa have been identified in human and mouse, with almost complete cross-species aa identity among all splice forms (greater than 98%). FGF13 is identified in the fetal ependyma, dorsal root and cranial ganglia, both atrial and ventricular myocardium, and in renal collecting duct-associated mesenchyme.
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Synonyms
Fibroblast growth factor 13, FGF-13, Fibroblast growth factor homologous factor 2, FHF-2, FGF13, FHF2.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FGF13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-13 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized FGF-13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK LYLAMNSEGY LYTSELFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS HNEST.
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Background
What is the molecular weight/Mw of FGF13 Protein?
FGF13 Protein has a total Mw of 27.6kDa.
What is the source or expression system of FGF13 Protein?
Escherichia Coli.
What is the Purity of FGF13 Protein?
FGF13 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF13 Protein?
The biological functionality of FGF13 Protein will be determined in the future.
What is the amino acid sequence of FGF13 Protein?
MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK LYLAMNSEGY LYTSELFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS HNEST.
What applications can FGF13 Protein be used in?
FGF13 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF13 Protein?
The endotoxin level is minimal, FGF13 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 :
ING1 HumanDescription:
Inhibitor of Growth Family, Member 1 Human Recombinant
Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .
Product # :
PRO-2130Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279 a.a) and having a molecular mass of 34.3kDa.ING1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ING1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Inhibitor of Growth Family Member 1, also known as ING1 is a tumor suppressor protein which is able to induce cell growth arrest and apoptosis. ING1 is a nuclear protein which physically act together with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. In addition, Reduced expression and rearrangement of ING1 have been identified in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described for ING1.
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Synonyms
Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLSPANG EQLHLVNYVE DYLDSIESLP FDLQRNVSLM REIDAKYQEI LKELDECYER FSRETDGAQK RRMLHCVQRA LIRSQELGDE KIQIVSQMVE LVENRTRQVD SHVELFEAQQ ELGDTAGNSG KAGADRPKGE AAAQADKPNS KRSRRQRNNE NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE ASPADLPIDP NEPTYCLCNQ VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR GENEKTMDKA LEKSKKERAY NR.
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 :
GAMT HumanDescription:
Guanidinoacetate N-Methyltransferase Human Recombinant
PIG2, TP53I2, GAMT, Guanidinoacetate N-methyltransferase.
Product # :
ENZ-460Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human GAMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (1-236 a.a) and having a molecular mass of 28.4 kDa. GAMT is fused to a 20 amino acids His-Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The GAMT protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GAMT is a methyltransferase that transfers guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects GAMT gene result in neurologic syndromes and muscular hypotonia, probably due to creatine deficiency and accumulation of guanidinoacetate in the brain of affected individuals. GAMT take parts in the two-step synthesis of creatine from the protein building blocks glycine, arginine, and methionine. GAMT takes part in supplying the energy for muscle contraction, and is in addition a significant player in nervous system functioning. GAMT is active in the liver, pancreas, and kidne.
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Synonyms
PIG2, TP53I2, GAMT, Guanidinoacetate N-methyltransferase.
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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 MSAPSATPIF APGENCSPAW GAAPAAYDAA DTHLRILGKP VMERWETPYM HALAAAASSK GGRVLEVGFG MAIAASKVQE APIDEHWIIE CNDGVFQRLR DWAPRQTHKV IPLKGLWEDV APTLPDGHFD GILYDTYPLS EETWHTHQFN FIKNHAFRLL KPGGVLTYCN LTSWGELMKS KYSDITIMFE ETQVPALLEA GFRRENIRTE VMALVPPADC RYYAFPQMIT PLVTKG.
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 :
GET4 HumanDescription:
Golgi To ER Traffic Protein 4 Human Recombinant
Golgi to ER traffic protein 4 homolog (S. cerevisiae), C7orf20, CEE, CGI-20, TRC35, Golgi to ER traffic protein 4 homolog, Conserved edge-expressed protein, Transmembrane domain recognition complex 35 kDa subunit, GET4.
Product # :
PRO-1868Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GET4 Human Recombinant produced in E. coli is. a single polypeptide chain containing 350 amino acids (1-327) and having a molecular mass of 38.9kDa. GET4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GET4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
BAT3 complex is a multiprotein complex which takes part in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. Golgi To ER Traffic Protein 4 (GET4) is a part of the BAT3 complex. The complex functions by helping TA proteins (which contain a single C-terminal transmembrane region) which are captured by ASNA1/TRC40. BAT3 complex synthesizes membrane proteins, interacts with the transmembrane area of recently released TA proteins, and transfers them to ASNA1/TRC40 for targeting.
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Synonyms
Golgi to ER traffic protein 4 homolog (S. cerevisiae), C7orf20, CEE, CGI-20, TRC35, Golgi to ER traffic protein 4 homolog, Conserved edge-expressed protein, Transmembrane domain recognition complex 35 kDa subunit, GET4.
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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 MGSMAAAAAM AEQESARNGG RNRGGVQRVE GKLRASVEKG DYYEAHQMYR TLFFRYMSQS KHTEARELMY SGALLFFSHG QQNSAADLSM LVLESLEKAE VEVADELLEN LAKVFSLMDP NSPERVTFVS RALKWSSGGS GKLGHPRLHQ LLALTLWKEQ NYCESRYHFL HSADGEGCAN MLVEYSTSRG FRSEVDMFVA QAVLQFLCLK NKSSASVVFT TYTQKHPSIE DGPPFVEPLL NFIWFLLLAV DGGKLTVFTV LCEQYQPSLR RDPMYNEYLD RIGQLFFGVP PKQTSSYGGL LGNLLTSLMG SSEQEDGEES PSDGSPIELD.
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 :
Troponin-C ProteinDescription:
Cardiac Troponin-C Human
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Product # :
PRO-2571Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Troponin-C Human produced from Human Cardiac Tissue, having a molecular mass of 18kDa. The Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.
Source
Human cardiac tissue
Formulation
The protein solution contains 150 mM NaCl, 10 mM sodium phosphate and 0.05% NaN3, (pH 7.0).
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.
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Synonyms
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
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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.
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 :
COQ9 HumanDescription:
Coenzyme Q9 Human Recombinant
Ubiquinone biosynthesis protein COQ9, mitochondrial, C16orf49, COQ10D5, C16orf49, HSPC326, PSEC0129.
Product # :
ENZ-898Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
COQ9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (45-318 a.a) and having a molecular mass of 33.3kDa.COQ9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
COQ9 protein solution (1mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquinone biosynthesis protein COQ9 (COQ9) represents a mitochondrial ubiquinone biosynthesis gene. The COQ9 protein is likely required for biosynthesis of coenzyme Q10, since mutations at this locus have been linked with autosomal-recessive neonatal-onset primary coenzyme Q10 deficiency.
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Synonyms
Ubiquinone biosynthesis protein COQ9, mitochondrial, C16orf49, COQ10D5, C16orf49, HSPC326, PSEC0129.
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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 MGSRSSDEQK QQPPNSFSQQ HSETQGAEKP DPESSHSPPR YTDQGGEEEE DYESEEQLQH RILTAALEFV PAHGWTAEAI AEGAQSLGLS SAAASMFGKD GSELILHFVT QCNTRLTRVL EEEQKLVQLG QAEKRKTDQF LRDAVETRLR MLIPYIEHWP RALSILMLPH NIPSSLSLLT SMVDDMWHYA GDQSTDFNWY TRRAMLAAIY NTTELVMMQD SSPDFEDTWR FLENRVNDAM NMGHTAKQVK STGEALVQGL MGAAVTLKNL TGLNQRR.
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 :
SARS MERS, Sf9Description:
SARS MERS Spike Recombinant
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein
Product # :
SARS-051Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SARS MERS Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1285 amino acids (18-1296aa) and having a molecular mass of 141.6kDa.SARS MERS is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The SARS MERS solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.
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Synonyms
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein
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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
YVDVGPDSVK SACIEVDIQQ TFFDKTWPRP IDVSKADGII YPQGRTYSNI TITYQGLFPY QGDHGDMYVY SAGHATGTTP QKLFVANYSQ DVKQFANGFV VRIGAAANST GTVIISPSTS ATIRKIYPAF MLGSSVGNFS DGKMGRFFNH TLVLLPDGCG TLLRAFYCIL EPRSGNHCPA GNSYTSFATY HTPATDCSDG NYNRNASLNS FKEYFNLRNC TFMYTYNITE DEILEWFGIT QTAQGVHLFS SRYVDLYGGN MFQFATLPVY DTIKYYSIIP HSIRSIQSDR KAWAAFYVYK LQPLTFLLDF SVDGYIRRAI DCGFNDLSQL HCSYESFDVE SGVYSVSSFE AKPSGSVVEQ AEGVECDFSP LLSGTPPQVY NFKRLVFTNC NYNLTKLLSL FSVNDFTCSQ ISPAAIASNC YSSLILDYFS YPLSMKSDLS VSSAGPISQF NYKQSFSNPT CLILATVPHN LTTITKPLKY SYINKCSRLL SDDRTEVPQL VNANQYSPCV SIVPSTVWED GDYYRKQLSP LEGGGWLVAS GSTVAMTEQL QMGFGITVQY GTDTNSVCPK LEFANDTKIA SQLGNCVEYS LYGVSGRGVF QNCTAVGVRQ QRFVYDAYQN LVGYYSDDGN YYCLRACVSV PVSVIYDKET KTHATLFGSV ACEHISSTMS QYSRSTRSML KRRDSTYGPL QTPVGCVLGL VNSSLFVEDC KLPLGQSLCA LPDTPSTLTP RSVRSVPGEM RLASIAFNHP IQVDQLNSSY FKLSIPTNFS FGVTQEYIQT TIQKVTVDCK QYVCNGFQKC EQLLREYGQF CSKINQALHG ANLRQDDSVR NLFASVKSSQ SSPIIPGFGG DFNLTLLEPV SISTGSRSAR SAIEDLLFDK VTIADPGYMQ GYDDCMQQGP ASARDLICAQ YVAGYKVLPP LMDVNMEAAY TSSLLGSIAG VGWTAGLSSF AAIPFAQSIF YRLNGVGITQ QVLSENQKLI ANKFNQALGA MQTGFTTTNE AFQKVQDAVN NNAQALSKLA SELSNTFGAI SASIGDIIQR LDVLEQDAQI DRLINGRLTT LNAFVAQQLV RSESAALSAQ LAKDKVNECV KAQSKRSGFC GQGTHIVSFV VNAPNGLYFM HVGYYPSNHI EVVSAYGLCD AANPTNCIAP VNGYFIKTNN TRIVDEWSYT GSSFYAPEPI TSLNTKYVAP QVTYQNISTN LPPPLLGNST GIDFQDELDE FFKNVSTSIP NFGSLTQINT TLLDLTYEML SLQQVVKALN ESYIDLKELG NYTYYNKWPH 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 :
EIF3K (50-94) HumanDescription:
Eukaryotic Translation Initiation Factor 3K (50-94 a.a.) Human Recombinant
PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.
Product # :
PRO-2833Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The EIF3KHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The EIF3KHis-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 45 amino acid residues of the EIF3KHuman, 50-94 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized EIF3Kat -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Eukaryotic Translation Initiation Factor 3K (EIF3K) is a part of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a few other subunits of the 40S ribosomal subunit and eIF3. EIF3K is found both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4. EIF3K is conserved among high eukaryotes, including mammals, plants and insects and is expressed in human tissues.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ctxBDescription:
Cholera Toxin B subunit Recombinant
Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.
Product # :
PRO-2605Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Cholera Toxin B subunit Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 103 amino acids and having a molecular mass of 11.6kDa.ctxB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ctxB is supplied as a 0.2 μm filtered solution conteining 5mM PB, pH 7.0, 75mM NaCl, and 50 % glycerol.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Cholera Toxin B subunit (ctxB) Cholera is a protein complex secreted by the bacterium Vibrio cholerae. ctxB is responsible for the massive, watery diarrhea characteristic of cholera infection. The cholera toxin is an oligomeric complex made up of 6 protein subunits: a single copy of the A subunit and5 copies of the B subunit, denoted as AB5. Subunit B binds while subunit A activates the G protein which activates adenylate cyclase. The five B subunits form a five-membered ring. The A subunit has 2 important segments. The A1 portion of the chain (CTA1) is a globular enzyme payload that ADP-ribosylates G proteins, while the A2 chain (CTA2) forms an extended alpha helix which sits snugly in the central pore of the B subunit ring.
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Synonyms
Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.
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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
TPQNITDLCA EYHNTQIYTL NDKIFSYTES LAGKREMAII TFKNGAIFQV EVPGSQHIDS QKKAIERMKD TLRIAYLTEA KVEKLCVWNN KTPHAIAAIS MAN.
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.