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1000 results found for “prefoldin”
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Name :
LCAT Human, HEKDescription:
Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Product # :
ENZ-254Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LCAT Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 429 amino acids (25-440) which includes a 13 amino acid Flag Tag fused at N-terminus and having a total molecular mass of 48.5 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.
Source
Human Embryonic Kidney 293 cells
Formulation
The LCAT protein was lyophilized from 0.4um filtered solution at a concentration of 0.5mg/ml containing 20mM Tris buffer, and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
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Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LCAT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCAT 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
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. LCAT HEK is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
HVDYKDDDDK PAGFWLLNVL FPPHTTPKAE LSNHTRPVIL VPGCLGNQLE AKLDKPDVVN WMCYRKTEDF FTIWLDLNMF LPLGVDCWID NTRVVYNRSS GLVSNAPGVQ IRVPGFGKTY SVEYLDSSKL AGYLHTLVQN LVNNGYVRDE TVRAAPYDWR LEPGQQEEYY RKLAGLVEEM HAAYGKPVFL IGHSLGCLHL LYFLLRQPQA WKDRFIDGFI SLGAPWGGSI KPMLVLASGD NQGIPIMSSI KLKEEQRITT TSPWMFPSRM AWPEDHVFIS TPSFNYTGRD FQRFFADLHF EEGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPRTYIY DHGFPYTDPV GVLYEDGDDT VATRSTELCG LWQGRQPQPV HLLPLHGIQH LNMVFSNLTL EHINAILLGA YRQGPPASPT ASPEPPPPE
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 :
PRLR Human, AntagonistDescription:
Prolactin Receptor Antagonist Human Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-1254Price :
Quantity :
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Description
Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.
Biological Activity
fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).
More Info
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PRLR in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr
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Background
Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
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 :
FGF 2 Human, sf9Description:
Fibroblast Growth Factor-Basic Human Recombinant, Sf9
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Product # :
CYT-365Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17353 Dalton.The FGF-basic is purified by proprietary chromatographic techniques.
Source
Baculovirus.
Formulation
The sterile protein solution (0.5mg/ml) contains 20mM Tris pH=7.9, 100mM KCl, 1mM DTT and 20% glycerol.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.More Info
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Introduction
Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
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Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
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Physical Appearance
Sterile Filtered liquid formulation.
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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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ala-Gly-Ser-Ile.
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Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.3kDa.
What is the source or expression system of FGF 2 Protein?
Baculovirus.
What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.
What is the amino acid sequence of FGF 2 Protein?
FGF 2 Protein is composed from155 amino acids.
What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CRYBB1 HumanDescription:
Crystallin Beta B1 Human Recombinant
EC 1.17.4.1, RR2M, Beta-B1 crystallin, CATCN3.
Product # :
HSP-033Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRYBB1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (1-252 a.a.) and having a molecular mass of 29.1 kDa. The CRYBB1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYBB1 solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Crystallins are the main structural proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into 3 fprotein families, α, β, & γ families. Because lens central fiber cells lose their nuclei during development, these crystallins are prepared and then retained throughout life, making them extremely stable proteins. CRYBB1 is a beta basic group member and undergoes extensive cleavage at its N-terminal extension during lens maturation.
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Synonyms
EC 1.17.4.1, RR2M, Beta-B1 crystallin, CATCN3.
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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
MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE GSFPVLATEP PKRSHHHHHH.
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 :
Leptin qA Ovine, PEGDescription:
Leptin Quadruple Antagonist Pegylated Ovine Recombinant
Product # :
CYT-1246Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM 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 Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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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.
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Name :
Activin-A RatDescription:
Activin-A Rat Recombinant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-147Price :
Quantity :
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Shipped at Room temp
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Description
Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/mlMore Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). 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
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
Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.
What is the source or expression system of Activin A Protein?
Ecoli
What is the Purity of Activin A Protein?
Activin A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.
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?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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 :
ACVRL1 HumanDescription:
Activin A Receptor Type II-Like 1 Human Recombinant
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
Product # :
CYT-920Price :
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Shipped with Ice Packs
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Description
ACVRL1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids (22-118a.a.) and having a molecular mass of 11.5kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).ACVRL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
ACVRL1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
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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
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
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Background
The Physiological Implications and Therapeutic Potential of Activin A Receptor Type II-Like 1 Human Recombinant
1. Abstract
This research paper investigates the Activin A Receptor Type II-Like 1 Human Recombinant (ACVRL1), a significant protein involved in the TGF-beta superfamily signaling pathway. We provide an extensive understanding of ACVRL1’s structure, signaling mechanism, biological functions, and implications in disease pathology. Additionally, we explore the therapeutic potential of ACVRL1 in various pathological conditions.
2. Introduction
ACVRL1, also known as ALK1, plays an essential role in the TGF-beta signaling pathway, which has implications in cellular proliferation, differentiation, and apoptosis. Understanding ACVRL1 and its signaling mechanisms could provide insights into its potential therapeutic applications in various diseases.
3. Structure and Signaling of ACVRL1
ACVRL1 is a type I receptor protein involved in the TGF-beta signaling pathway. It is a transmembrane protein that consists of a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Binding of ligands to ACVRL1 triggers phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVRL1
ACVRL1 plays pivotal roles in multiple biological processes, including vascular development, angiogenesis, and maintenance of vascular integrity. It is known to influence cellular processes such as proliferation, differentiation, and apoptosis, thereby implicating it in organogenesis and homeostasis.
5. ACVRL1 in Disease Pathology
Mutations in the ACVRL1 gene have been associated with hereditary hemorrhagic telangiectasia (HHT), a genetic disorder characterized by abnormal blood vessel formation. This link underscores the critical role of ACVRL1 in vascular biology and disease.
6. Therapeutic Potential of ACVRL1
Given its crucial role in vascular biology and its link to HHT, ACVRL1 presents a promising target for therapeutic interventions. Modulation of ACVRL1 signaling could potentially provide treatment options for pathological conditions related to abnormal blood vessel formation and function.
7. Conclusion and Future Perspectives
Our understanding of ACVRL1 and its functions has grown significantly in recent years, but there is much yet to be discovered. Continued research into ACVRL1's precise molecular mechanisms and its roles in disease will undoubtedly open new doors for therapeutic developmen
What is the molecular weight / Mw of ACVRL1 Protein?
ACVRL1 Protein has a total Mw of 11.5kDa.What is the source or expression system of ACVRL1 Protein?
Sf9, Insect cells.
What is the Purity of ACVRL1 Protein?
ACVRL1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVRL1 Protein?
The biological functionality of ACVRL1 Protein will be determined in the future.
What is the amino acid sequence of ACVRL1 Protein?
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
What applications can ACVRL1 Protein be used in?
ACVRL1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ACVRL1 Protein?
The endotoxin level is minimal, ACVRL1 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 :
Cyclophilin B MouseDescription:
Cyclophilin-B Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.
Product # :
ENZ-1039Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Cyclophilin B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (34-216 a.a) and having a molecular mass of 22.7kDa.Cyclophilin B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cyclophilin B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,000 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.
More Info
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Introduction
Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.
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Synonyms
Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.
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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 MGSMNDKKKG PKVTVKVYFD LQIGDESVGR VVFGLFGKTV PKTVDNFVAL ATGEKGFGYK NSKFHRVIKD FMIQGGDFTR GDGTGGKSIY GERFPDENFK LKHYGPGWVS MANAGKDTNG SQFFITTVKT SWLDGKHVVF GKVLEGMDVV RKVESTKTDS
RDKPLKDVII VDSGKIEVEK PFAIAKE.
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 :
Cyclophilin C HumanDescription:
Cyclophilin-C Human Recombinant
Peptidylprolyl Isomerase C (Cyclophilin C), Cyclophilin C, Rotamase C, EC 5.2.1.8, PPIase C, CYPC, Peptidyl-Prolyl Cis-Trans Isomerase C, Parvulin, PPIC.
Product # :
ENZ-809Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cyclophilin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Phe29-Trp212) containing 194 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 21.3kDa.
Source
Escherichia Coli.
Formulation
Cyclophilin-C was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cyclophilin-C belongs to the peptidyl-prolyl cis-trans isomerase (PPIase)) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Like other PPIases, the Cyclophilin-C protein can bind immunosuppressant cyclosporin A.
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Synonyms
Peptidylprolyl Isomerase C (Cyclophilin C), Cyclophilin C, Rotamase C, EC 5.2.1.8, PPIase C, CYPC, Peptidyl-Prolyl Cis-Trans Isomerase C, Parvulin, PPIC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after 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. Cyclophilin-C is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASFRKRGPSVTA KVFFDVRIGD KDVGRIVIGL FGKVVPKTVE NFVALATGEK GYGYKGSKFH RVIKDFMIQG GDITTGDGTG GVSIYGETFP DENFKLKHYG IGWVSMANAG PDTNGSQFFI TLTKPTWLDG KHVVFGKVID GMTVVHSIEL QATDGHDRPL TNCSIINSGK IDVKTPFVVE IADW.
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 :
AKT1 Human, Sf9Description:
Protein Kinase B Alpha Human Recombinant, Sf9
V-Akt Murine Thymoma Viral Oncogene Homolog 1, Protein Kinase B Alpha, Proto-Oncogene C-Akt, RAC-PK-Alpha, EC 2.7.11.1, PKB Alpha, CWS6, PKB, RAC, RAC-Alpha Serine/Threonine-Protein Kinase, Rac Protein Kinase Alpha, Protein Kinase B, PKB-ALPHA, RAC-ALPHA, EC 2.7.11, AKT1m, PRKBA, AKT, RAC-alpha serine/threonine-protein kinase.
Product # :
PKA-069Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AKT1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 488 amino acids (1-480a.a.) and having a molecular mass of 56.7kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). AKT1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AKT1 protein solution (0. 5mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Akt1, also known as Akt or else protein kinase B (PKB) is an important molecule in mammaliancellular signaling. In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. Moreover, these enzymes are members of the serine/threonine-specific protein kinase family (EC2.7.11.1). Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesis pathways, and is therefore a key signaling protein in the cellular pathways which lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a most important factor in numerous types of cancer. Akt (now also called Akt1) was at first identified as the oncogenein the transforming retrovirus, AKT8.
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Synonyms
V-Akt Murine Thymoma Viral Oncogene Homolog 1, Protein Kinase B Alpha, Proto-Oncogene C-Akt, RAC-PK-Alpha, EC 2.7.11.1, PKB Alpha, CWS6, PKB, RAC, RAC-Alpha Serine/Threonine-Protein Kinase, Rac Protein Kinase Alpha, Protein Kinase B, PKB-ALPHA, RAC-ALPHA, EC 2.7.11, AKT1m, PRKBA, AKT, RAC-alpha serine/threonine-protein kinase.
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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
MSDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDVDQREA PLNNFSVAQC QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWT TAIQTVADGL KKQEEEEMDF RSGSPSDNSG AEEMEVSLAK PKHRVTMNEF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS RERVFSEDRA RFYGAEIVSA LDYLHSEKNV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY NQDHEKLFEL ILMEEIRFPR TLGPEAKSLL SGLLKKDPKQ RLGGGSEDAK EIMQHRFFAG IVWQHVYEKK LSPPFKPQVT SETDTRYFDE EFTAQMITIT PPDQDDSMEC VDSERRPHFP QFSYSASGTA LEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MVD HumanDescription:
Mevalonate Decarboxylase Human Recombinant
Diphosphomevalonate decarboxylase, Mevalonate (diphospho)decarboxylase, MDDase, Mevalonate pyrophosphate decarboxylase, MVD, MPD, FP17780.
Product # :
ENZ-226Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MVD Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (1-400) and having a molecular mass of 45.6kDa.MVD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MVD solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Diphosphomevalonate decarboxylase (MVD) catalyzes the conversion of mevalonate pyrophosphate into isopentenyl pyrophosphate in one of the early steps in cholesterol biosynthesis. MVD decarboxylates and dehydrates its substrate while hydrolyzing ATP. MVD is expressed in the heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta.
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Synonyms
Diphosphomevalonate decarboxylase, Mevalonate (diphospho)decarboxylase, MDDase, Mevalonate pyrophosphate decarboxylase, MVD, MPD, FP17780.
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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 MASEKPLAAV TCTAPVNIAV IKYWGKRDEE LVLPINSSLS VTLHQDQLKT TTTAVISKDF TEDRIWLNGR EEDVGQPRLQ ACLREIRCLA RKRRNSRDGD PLPSSLSCKV HVASVNNFPT AAGLASSAAG YACLAYTLAR VYGVESDLSE VARRGSGSAC RSLYGGFVEW QMGEQADGKD SIARQVAPES HWPELRVLIL VVSAEKKLTG STVGMRASVE TSPLLRFRAE SVVPARMAEM ARCIRERDFP SFAQLTMKDS NQFHATCLDT FPPISYLNAI SWRIIHLVHR FNAHHGDTKV AYTFDAGPNA VIFTLDDTVA EFVAAVWHGF PPGSNGDTFL KGLQVRPAPL SAELQAALAM EPTPGGVKYI IVTQVGPGPQ ILDDPCAHLL GPDGLPKPAA.
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 :
AMH Human, HEKDescription:
Anti-Mullerian Hormone Human Recombinant, HEK
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
Product # :
PRO-2665Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
AMH Human Recombinant is a single, glycosylated polypeptide chain containing 439 amino acids (19-451a.a) and having a molecular mass of 46.5kDa (calculated). AMH is fused to a 6 a.a His tag at C-terminal.
Source
HEK293
Formulation
AMH filtered (0.4 µm) and lyophilized in PBS and 5% (w/v) trehalose.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Anti-Mullerian Hormone also known as AMH is a member of the TGF-beta family. AMH is a glycoprotein which is produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. AMH inhibits the growth of tumors derived from tissues of Muellerian duct origin. Moreover, AMH participates in Leydig cell differentiation and function in addition to follicular development in adult females.
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Synonyms
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
LLGTEALRAE EPAVGTSGLI FREDLDWPPG SPQEPLCLVA LGGDSNGSSS PLRVVGALSA YEQAFLGAVQ RARWGPRDLA TFGVCNTGDR QAALPSLRRL GAWLRDPGGQ RLVVLHLEEV TWEPTPSLRF QEPPPGGAGP PELALLVLYP GPGPEVTVTR AGLPGAQSLC PSRDTRYLVL AVDRPAGAWR GSGLALTLQP RGEDSRLSTA RLQALLFGDD HRCFTRMTPA LLLLPRSEPA PLPAHGQLDT VPFPPPRPSA ELEESPPSAD PFLETLTRLV RALRVPPARA SAPRLALDPD ALAGFPQGLV NLSDPAALER LLDGEEPLLL LLRPTAATTG DPAPLHDPTS APWATALARR VAAELQAAAA ELRSLPGLPP ATAPLLARLL ALCPGGPGGL GDPLRALLLL KALQGLRVEW RGRDPRGPGR AQRHHHHHH
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 :
HPCAL1 HumanDescription:
Hippocalcin-Like 1 Human Recombinant
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3, VILIP-3
Product # :
PRO-254Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HPCAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213amino acids (1-193a.a.) and having a molecular wieght of 24.4kDa. The HPCAL1 is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HPCAL1 protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 1mM DTT 0.2M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.
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Synonyms
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3,
VILIP-3 -
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 MGKQNSKLRP EVLQDLRENT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD ASKFAEHVFR TFDTNGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA SQF
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 :
NAT1 HumanDescription:
N-Acetyltransferase 1 Human Recombinant
N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.
Product # :
ENZ-144Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-290) and having a molecular mass of 36.1 kDa.The NAT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAT1 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 2mM DTT and 10% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
NAT1 is a member of the arylamine N-acetyltransferase family. NAT1 catalyzes N- or O-acetylation of heterocyclic and arylamine substrates in the detoxification of a large number of drugs. Several alleles triggering high levels of N-acetyltransferase activity were linked to colon and urinary bladder cancers, since NAT1 also bioactivate numerous known carcinogens. NAT1 aids metabolize drugs and other xenobiotics, and takes part in the detoxification of a plethora of hydrazine and arylamine drugs.
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Synonyms
N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.
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Physical Appearance
NAT1 is supplied as a 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 MDIEAYLERI GYKKSRNKLD LETLTDILQH QIRAVPFENL NIHCGDAMDL GLEAIFDQVV RRNRGGWCLQ VNHLLYWALT TIGFETTMLG GYVYSTPAKK YSTGMIHLLL QVTIDGRNYI VDAGFGRSYQ MWQPLELISG KDQPQVPCIF RLTEENGFWY LDQIRREQYI PNEEFLHSDL LEDSKYRKIY SFTLKPRTIE DFESMNTYLQ TSPASVFTSK SFCSLQTPDG VHCLVGFTLT HRRFNYKDNT DLIEFKTLSE EEIEKVLKNI FNISLQRKLV PKHGDRFFTI
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 :
ASNS MouseDescription:
Asparagine Synthetase Mouse Recombinant
Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.
Product # :
ENZ-1100Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ASNS produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 567 amino acids (1-561a.a.) and having a molecular mass of 65.1 kDa.ASNS is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
ASNS protein solution ( 0.25mg/ml ) contains PBS (pH 7.4) and 40% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.
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Synonyms
Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.
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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
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPDMRIPK NGIEKHLLRE TFEDCNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDEMMSA SQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK WINATDPSAR TLTHYKS AAK AHHHHHH.
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 :
IF HumanDescription:
Intrinsic Factor Human Recombinant
Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.
Product # :
PRO-375Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Intrinsic Factor Human Recombinant produced in baculovirus is a glycosylated, polypeptide chain having a molecular mass of 55,000 Dalton. The Intrinsic Factor is fused to a hexa-histidine at the C-terminus and purified by proprietary chromatographic techniques for removal of bound Vitamin B-12.
Source
Sf9 Insect Cells.
Formulation
The protein solution contains 20mM HEPES pH-8.0, 100mM NaCl and 20% Glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Intrinsic Factor is a member of the cobalamin transport protein family. It encodes a glycoprotein secreted by parietal cells of the gastric mucosa and is required for adequate absorption of vitamin B12 in the terminal ileum. Vitamin B12 is essential for erythrocyte maturation and mutations in the Intrinsic Factor may lead to congenital pernicious anemia. Upon entry into the stomach, vitamin B12 binds to one of two B12 binding proteins present in the gastric fluid. In the less acidic environment of the small intestine, these proteins dissociate from the vitamin, allowing it to bind to intrinsic factor and enter the portal circulation through a receptor in the ileal mucosa specific for the B12-intrinsic factor complex.
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Synonyms
Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.
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Physical Appearance
Sterile Filtered pink 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.
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 HumanDescription:
Eukaryotic Translation Initiation Factor 3K Human Recombinant
Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.
Product # :
PRO-179Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EIF3K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218a.a.) and having a molecular mass of 27.2 kDa. EIF3K is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF3K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
EIF3K is a member of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a number of other subunits of eIF3 and the 40S ribosomal subunit. EIF3K is conserved among high eukaryotes, including mammals, insects, and plants, and it is universally expressed in human tissues. EIF3K is distributed both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4 (Cdk4).
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Synonyms
Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.
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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 MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS ADESGQIFIC SQEESIKPKN IVEKIDFDSV SSIMASSQ
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 :
OCM HumanDescription:
Oncomodulin-1 Human Recombinant
Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.
Product # :
PRO-143Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human Oncomodulin-1 produced in E.coli has a molecular mass of 13.21kDa containing 117 amino acid residues of the human Oncomodulin-1 and fused to a 9 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
Oncomodulin-1 was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
More Info
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Introduction
Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.
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Synonyms
Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.
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Applications
Western blotting.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
STK17A HumanDescription:
Serine/Threonine Kinase 17A Human Recombinant
DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.
Product # :
PKA-314Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STK17A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (64-321 a.a) and having a molecular mass of 31.9kDa.STK17A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STK17A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
STK17A belongs to the DAP kinase-associated apoptosis-inducing protein kinase family and encodes an autophosphorylated nuclear protein with a protein kinase domain. STK17A acts as a positive regulator of apoptosis. STK17A is greatly expressed in the placenta with lower levels in the heart, lung, skeletal muscle, kidney and pancreas.
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Synonyms
DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.
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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 MGSGRELGRG KFAVVRKCIK KDSGKEFAAK FMRKRRKGQD CRMEIIHEIA VLELAQDNPW VINLHEVYET ASEMILVLEY AAGGEIFDQC VADREEAFKE KDVQRLMRQI LEGVHFLHTR DVVHLDLKPQ NILLTSESPL GDIKIVDFGL SRILKNSEEL REIMGTPEYV APEILSYDPI SMATDMWSIG VLTYVMLTGI SPFLGNDKQE TFLNISQMNL SYSEEEFDVL SESAVDFIRT LLVKKPEDRA TAEECLKHPW 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 :
STMN2 HumanDescription:
Stathmin Like-2 Human Recombinant
SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.
Product # :
PRO-752Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Stathmin Like-2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (39-179 a.a) and having a molecular mass of 16.4 kDa. STMN2 is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STMN2 protein solution contains 50mM MES, pH-6.0, 0.1mM PMSF, 1 mM EDTA and 10% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
STMN2 is a neuronal growth-associated protein which shares a majority of its amino acid sequence with the phosphoprotein stathmin. STMN2 is involved in neuronal differentiation and in modulating membrane interaction with the cytoskeleton through neurite outgrowth. STMN2 is necessary for maintaining the anchorage-independent growth state of beta-catenin/TCF-activated hepatoma cells. SCG10 is a novel indicator of osteogenesis and osteoblast that takes part in the regulation of the adipocyte/osteoblast balance. STMN2 plays a role as an effector downstream of Rnd1 to regulate axon extensions by modulating microtubule organization.
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Synonyms
SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MDMEVKQINK RASGQAFELI LKPPSPISEA PRTLASPKKK DLSLEEIQKK LEAAEERRKS QEAQVLKQLA EKREHEREVL QKALEENNNF SKMAEEKLIL KMEQIKENRE ANLAAIIERL QEKERHAAEV RRNKELQVEL SG.
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 :
EXOSC8 HumanDescription:
Exosome Component 8 Human Recombinant
Exosome Component 8, EXOSC8, OIP2, RRP43, CBP-Interacting Protein 3, Opa Interacting Protein 2, Opa-Interacting Protein 2, Ribosomal RNA-Processing Protein 43, OIP-2, p9, CIP3, EAP2, Rrp43p, bA421P11.3, Exosome Complex Component RRP43, Exosome Complex Exonuclease RRP43.
Product # :
PRO-483Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EXOSC8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276) and having a molecular mass of 32.4 kDa.EXOSC8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EXOSC8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Exosome component 8 and transcription factor 4 (EXOSC8) is a part of the exosome complex. In the cytoplasm, the RNA exosome complex is engaged in general mRNA turnover and specifically degrades naturally unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA inspection pathways, preventing translation of aberrant mRNAs. EXOSC8 appears to be involved in degradation of histone mRNA. EXOSC8 attaches to ARE-containing RNAs. The EXOSC8 gene encodes a 3'-5' exoribonuclease, which specifically interacts with mRNAs containing AU-rich elements. The EXOSC8 protein is part of the exosome complex, which is significant for the degradation of many RNA species.
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Synonyms
Exosome Component 8, EXOSC8, OIP2, RRP43, CBP-Interacting Protein 3, Opa Interacting Protein 2, Opa-Interacting Protein 2, Ribosomal RNA-Processing Protein 43, OIP-2, p9, CIP3, EAP2, Rrp43p, bA421P11.3, Exosome Complex Component RRP43, Exosome Complex Exonuclease RRP43.
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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 MGSMAAGFKT VEPLEYYRRF LKENCRPDGR ELGEFRTTTV NIGSISTADG SALVKLGNTT VICGVKAEFA APSTDAPDKG YVVPNVDLPP LCSSRFRSGP PGEEAQVASQ FIADVIENSQ IIQKEDLCIS PGKLVWVLYC DLICLDYDGN ILDACTFALL AALKNVQLPE VTINEETALA EVNLKKKSYL NIRTHPVATS FAVFDDTLLI VDPTGEEEHL ATGTLTIVMD EEGKLCCLHK PGGSGLTGAK LQDCMSRAVT RHKEVKKLMD EVIKSMKPK.
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 :
FAM3C HumanDescription:
Family with Sequence Similarity 3, Member C Human Recombinant
Family with sequence similarity 3 member C, ILEI, Interleukin-like EMT inducer, predicted osteoblast protein, GS3876, protein FAM3C.
Product # :
PRO-952Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FAM3C Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (25-227) and having a molecular mass of 24.5 kDa.FAM3C is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The FAM3C solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 200mM NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
FAM3C is a member of the FAM3 family and holds a GG domain. Pancreatic cancer-derived cells demonstrate a difference in expression of this protein. FAM3C is a downstream target gene for the Nkx5-1 transcription factor, and there for takes part in cell differentiation and proliferation through inner ear embryogenesis. In addition, FAM3C has a role in retinal laminar formation and promotes epithelial to mesenchymal transition.
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Synonyms
Family with sequence similarity 3 member C, ILEI, Interleukin-like EMT inducer, predicted osteoblast protein, GS3876, protein FAM3C.
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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 MQVFEIKMDA SLGNLFARSA LDTAARSTKP PRYKCGISKA CPEKHFAFKM ASGAANVVGP KICLEDNVLM SGVKNNVGRG INVALANGKT GEVLDTKYFD MWGGDVAPFI EFLKAIQDGT IVLMGTYDDG ATKLNDEARR LIADLGSTSI TNLGFRDNWV FCGGKGIKTK SPFEQHIKNN KDTNKYEGWP EVVEMEGCIP QKQD
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 :
TKT HumanDescription:
Transketolase Human Recombinant
Transketolase, TK, TKT1, EC 2.2.1.1.
Product # :
ENZ-588Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TKT Human Recombinant produced in E. coli is a single polypeptide chain containing 643 amino acids (1-623) and having a molecular mass of 70.0kDa.TKT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TKT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
TKT is a thiamine-dependent enzyme that takes part in the channeling of leftover sugar phosphates to glycolysis in the pentose phosphate pathway. Multiple alternatively spliced variants are known that encode the same protein.
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Synonyms
Transketolase, TK, TKT1, EC 2.2.1.1.
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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 MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE LLKMFGIDRD AIAQAVRGLI TKA.
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 :
KLK5 Human, Sf9Description:
Kallikrein-5 Human Recombinant, Sf9
Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.
Product # :
ENZ-1021Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Kallikrein-5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 236 amino acids (67-293 a.a.) and having a molecular mass of 26.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).KLK5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.
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Synonyms
Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.
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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
ADLIINGSDC DMHTQPWQAA LLLRPNQLYC GAVLVHPQWL LTAAHCRKKV FRVRLGHYSL SPVYESGQQM FQGVKSIPHP GYSHPGHSND LMLIKLNRRI RPTKDVRPIN VSSHCPSAGT KCLVSGWGTT KSPQVHFPKV LQCLNISVLS QKRCEDAYPR QIDDTMFCAG DKAGRDSCQG DSGGPVVCNG SLQGLVSWGD YPCARPNRPG VYTNLCKFTK WIQETIQANS 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.