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1000 results found for “Growth Hormone”
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Name :
TEK HumanDescription:
TEK Tyrosine Kinase Endothelial Human Recombinant
TEK Receptor Tyrosine Kinase, Tyrosine Kinase With Ig And EGF Homology Domains-2, Tunica Interna Endothelial Cell Kinase, Tyrosine-Protein Kinase Receptor TIE-2, Tyrosine-Protein Kinase Receptor TEK, TEK Tyrosine Kinase, Endothelial, Endothelial Tyrosine Kinase, EC 2.7.10.1, VMCM1, VMCM, TIE2, Venous Malformations, Multiple Cutaneous And Mucosal, Angiopoietin-1 Receptor, CD202b Antigen, EC 2.7.10, P140 TEK, CD202B, GLC3E, TIE-2, HTIE2.
Product # :
PKA-110Price :
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Shipped with Ice Packs
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Description
TEK produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 965 amino acids (23-748 a.a.) and having a molecular mass of 107.9kDa. (Molecular size on SDS-PAGE will appear at approximately 100-150 kDa).TEK is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TEK protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by the ability of the binding activity in a functional ELISA. The ED50 range ≤1ug/ml.
More Info
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Introduction
TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.
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Synonyms
TEK Receptor Tyrosine Kinase, Tyrosine Kinase With Ig And EGF Homology Domains-2, Tunica Interna Endothelial Cell Kinase, Tyrosine-Protein Kinase Receptor TIE-2, Tyrosine-Protein Kinase Receptor TEK, TEK Tyrosine Kinase, Endothelial, Endothelial Tyrosine Kinase, EC 2.7.10.1, VMCM1, VMCM, TIE2, Venous Malformations, Multiple Cutaneous And Mucosal, Angiopoietin-1 Receptor, CD202b Antigen, EC 2.7.10, P140 TEK, CD202B, GLC3E, TIE-2, HTIE2.
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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
AMDLILINSL PLVSDAETSL TCIASGWRPH EPITIGRDFE ALMNQHQDPL EVTQDVTREW AKKVVWKREK ASKINGAYFC EGRVRGEAIR IRTMKMRQQA SFLPATLTMT VDKGDNVNIS FKKVLIKEED AVIYKNGSFI HSVPRHEVPD ILEVHLPHAQ PQDAGVYSAR YIGGNLFTSA FTRLIVRRCE AQKWGPECNH LCTACMNNGV CHEDTGECIC PPGFMGRTCE KACELHTFGR TCKERCSGQE GCKSYVFCLP DPYGCSCATG WKGLQCNEAC HPGFYGPDCK LRCSCNNGEM CDRFQGCLCS PGWQGLQCER EGIPRMTPKI VDLPDHIEVN SGKFNPICKA SGWPLPTNEE MTLVKPDGTV LHPKDFNHTD HFSVAIFTIH RILPPDSGVW VCSVNTVAGM VEKPFNISVK VLPKPLNAPN VIDTGHNFAV INISSEPYFG DGPIKSKKLL YKPVNHYEAW QHIQVTNEIV TLNYLEPRTE YELCVQLVRR GEGGEGHPGP VRRFTTASIG LPPPRGLNLL PKSQTTLNLT WQPIFPSSED DFYVEVERRS VQKSDQQNIK VPGNLTSVLL NNLHPREQYV VRARVNTKAQ GEWSEDLTAW TLSDILPPQP ENIKISNITH SSAVISWTIL DGYSISSITI RYKVQGKNED QHVDVKIKNA TITQYQLKGL EPETAYQVDI FAENNIGSSN PAFSHELVTL PESQAPADLG GGKMLLLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH 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 :
Leptin PufferfishDescription:
Leptin Pufferfish Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-530Price :
Quantity :
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Shipped at Room temp
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Description
Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pufferfish Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE
GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE
QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
SPA-Cys LongDescription:
Staphylococcal Protein-A Cys Long Form Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1924Price :
Quantity :
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Shipped at Room temp
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Description
SPA-Cys long Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain with a Cys on C-terminus. SPA-Cys is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 423 amino acids and having a molecular mass of 46.7kDa containing little or no carbohydrate.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
AQHDEAQQNA FYQVLNMPNL NADQRNGFIQ SLKDDPSQSA NVLGEAQKLN DSQAPKADAQ QNNFNKDQQS AFYEILNMPN LNEAQRNGFI QSLKDDPSQS TNVLGEAKKL NESQAPKADN NFNKEQQNAF YEILNMPNLN EEQRNGFIQS LKDDPSQSAN LLSEAKKLNE SQAPKADNKF NKEQQNAFYE ILHLPNLNEE QRNGFIQSLK DDPSQSANLL AEAKKLNDAQ APKADNKFNK EQQNAFYEIL HLPNLTEEQR NGFIQSLKDD PSVSKEILAE AKKLNDAQAP KEEDNKKPGK EDGNKPGKED GNKPGKEDNK KPGKEDGNKP GKEDNNKPGK EDGNKPGKED NNKPGKEDGN KPGKEDGNKP GKEDGNGVHV VKPGDTVNDI AKANGTTADK IAADNKLADK NMIKPGQELV VDC
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 :
OSM RatDescription:
Oncostatin-M Rat Recombinant
Oncostatin-M, OSM, OncoM.
Product # :
CYT-169Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
OSM Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 214 amino acids and having a molecular mass of 24.3kDa.The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of rat C6 cells is < 5.0 µg/ml, corresponding to a specific activity of > 200 units/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
Oncostatin-M, OSM, OncoM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Oncostatin M 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
KRGCSSSSPK LLSQLKSQAN ITGNTASLLE PYILHQNLNT LTLRAACTEH PVAFPSEDML RQLSKPDFLS TVHATLGRVW HQLGAFRQQF PKIQDFPELE RARQNIQGIR NNVYCMARLL HPPLEIPEPT QADSGTSRPT TTAPGIFQIK IDSCRFLWGY HRFMGSVGRV FEEWGDGSRR SR RHSPLWAW LKGDHRIRPS RSSQSAMLRS LVPR.
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 :
LGALS8 MouseDescription:
Galectin-8 Mouse Recombinant
Galectin-8, Gal-8, LGALS-8, AI326142, D13Ertd524e, 1200015E08Rik.
Product # :
CYT-185Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
LGALS8 mouse Recombinant produced E. coli is a single polypeptide chain containing 339 amino acids (1-316) and having a molecular mass of 38kDa.LGALS8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LGALS8 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is ≤ 2ug/ml. Measured by its ability to agglutinate human red blood cells.
SDS-PAGE
More Info
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Introduction
LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.
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Synonyms
Galectin-8, Gal-8, LGALS-8, AI326142, D13Ertd524e, 1200015E08Rik.
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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 MGSMLSLNNL QNIIYNPIIP YVGTITEQLK PGSLIVIRGH VPKDSERFQV DFQLGNSLKP RADVAFHFNP RFKRSSCIVC NTLTQEKWGW EEITYDMPFR KEKSFEIVFM VLKNKFQVAV NGRHVLLYAH RISPEQIDTV GIYGKVNIHS IGFRFSSDLQ
SMETSALGLT QINRENIQKP GKLQLSLPFE ARLNASMGPG RTVVIKGEVN TNARSFNVDL VAGKTRDIAL HLNPRLNVKA FVRNSFLQDA WGEEERNITC FPFSSGMYFE MIIYCDVREF KVAINGVHSL EYKHRFKDLS SIDTLSVDGD IRLLDVRSW. -
Background
What is the molecular weight/Mw of LGALS8 MOUSE Protein?
LGALS8 MOUSE Protein has a total Mw of 38kDa.
What is the source or expression system of LGALS8 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS8 MOUSE Protein?
LGALS8 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS8 MOUSE Protein?
The biological functionality of LGALS8 MOUSE Protein will be determined in the future.
What is the amino acid sequence of LGALS8 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMLSLNNL QNIIYNPIIP YVGTITEQLK PGSLIVIRGH VPKDSERFQV DFQLGNSLKP RADVAFHFNP RFKRSSCIVC NTLTQEKWGW EEITYDMPFR KEKSFEIVFM VLKNKFQVAV NGRHVLLYAH RISPEQIDTV GIYGKVNIHS IGFRFSSDLQ
SMETSALGLT QINRENIQKP GKLQLSLPFE ARLNASMGPG RTVVIKGEVN TNARSFNVDL VAGKTRDIAL HLNPRLNVKA FVRNSFLQDA WGEEERNITC FPFSSGMYFE MIIYCDVREF KVAINGVHSL EYKHRFKDLS SIDTLSVDGD IRLLDVRSW.
What applications can LGALS8 MOUSE Protein be used in?
LGALS8 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS8 MOUSE Protein?
The endotoxin level is minimal, LGALS8 MOUSE Protein was purified using conventional chromatography techniques.
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Assay Conditions
1. Mix equal volumes of human blood and Alsever’s solution (pH 7.0). (Alsever’s solution: NaCl 0.42g, Sodium citric acid 0.8g, Citric acid 0.055g, D-glucose 2.05g in DW100 ml).2. Centrifuge at 15000rpm for 10 minutes and wash 4 times with PBS.3. Dilute packed cells in a 0.5mg/ml trypsin-EDTA solution to give 4% red cell suspension.4. Incubate for 1 hour at 37°C and wash 4 times with PBS.5. Dilute packed cells in PBS to give a 4% red cell suspension.6. Load 50µl of 0.5%BSA-in-0.15M-NaCl solution and 25µl of 4%-Red-Cell-in-PBS in U shaped wells.7. Add 25µl of serial diluted galectin protein in PBS to each well plate (Round bottom 96 well plate).8. Incubate for 30 minutes at room temperature to observe visible agglutination.
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 :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
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Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
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Physical Appearance
Sterile Filtered clear solution.
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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 MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LGALS4 MouseDescription:
Galectin-4 Mouse Recombinant
gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 4.
Product # :
CYT-187Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
LGALS4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-326a.a) and having a molecular mass of 38.8kDa.LGALS4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LGALS4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.
SDS-PAGE
More Info
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Introduction
Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 & IL-17.
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Synonyms
gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 4.
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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 MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.
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Background
What is the molecular weight/Mw of LGALS4 MOUSE Protein?
LGALS4 MOUSE Protein has a total Mw of 38.8kDa.
What is the source or expression system of LGALS4 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS4 MOUSE Protein?
LGALS4 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS4 MOUSE Protein?
The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.
What is the amino acid sequence of LGALS4 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.
What applications can LGALS4 MOUSE Protein be used in?
LGALS4 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS4 MOUSE Protein?
The endotoxin level is minimal, LGALS4 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KGF 2 RatDescription:
Keratinocyte Growth Factor-2 Rat Recombinant
FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.
Product # :
CYT-127Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
Description
KGF 2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 20.0kDa. The KGF 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 containing 5% trehalose.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF receptors is <0.5ng/ml.sds-page
More Info
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Introduction
KGF-2 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. FGF-10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7. Studies of the mouse homolog of suggested that this gene is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of lim bud formation. This gene is also implicated to be a primary factor in the process of wound healing.
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Synonyms
FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KGF 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KGF 2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized KGF 2 Rat Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QALGQDMVSP EATNSSSSSS SSSSSSSFSS PSSAGRHVRS YNHLQGDVRW RKLFSFTKYF LKIEKNGKVS GTKKENCPYS ILEITSVEIG VVAVKAINSN YYLAMNKKGK LYGSKEFNND CKLKERIEEN GYNTYASFNW QHNGRQMYVA LNGKGAPRRG QKTRRKNTSA HFLPMVVHS
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 :
Holo Transferrin HumanDescription:
Holo Transferrin Human Recombinant
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Product # :
PRO-2844Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- sds-page, activity
Description
Human Holo Transferrin Recombinant produced in HEK Cells is a glycosylated polypeptide containing 679 amino acids and having a Mw of of 76 kDa.
Source
HEK Cells
Formulation
The protein was lyophilized from 1x PBS pH-7.4.
Purity
Protein is >98% pure as determined by 10% PAGE (coomassie staining).
Biological Activity
The activity of Recombinant Holo Transferrin was determined by the proliferation assay using MDCK cells stimulated with recombinant human Holo Transferrin. The protein was found biologically activesds-page, activity
More Info
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Introduction
Recombinant Human Holo Transferrin is an iron-delivery signaling protein which functions in the delivery of Fe³⁺ iron to cells using transferrin receptor-1 (TfR1/CD71).
Holo-transferrin binds TfR1, undergoes receptor-mediated endocytosis and the iron is released intracellularly. Transferrin Human Recombinant is crucial for brain and the nervous system, neuronal mitochondrial metabolism, neurotransmitter synthesis, oligodendrocyte myelination and synaptic activity. Recombinant holo-transferrin can be used in cell therapy, stem-cell expansion, CHO production, or drug-delivery platforms.
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Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Holo Transferrin recombinant between 2-8°C, do not freeze.
Upon reconstitution Holo Transferrin 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 Holo Transferrin recombinant in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VPDKTVRWCA VSEHEATKCQ SFRDHMKSVI PSDGPSVACV KKASYLDCIR AIAANEADAV TLDAGLVYDA YLAPNNLKPV VAEFYGSKED PQTFYYAVAV VKKDSGFQMN QLRGKKSCHT GLGRSAGWNI PIGLLYCDLP EPRKPLEKAV ANFFSGSCAP CADGTDFPQL CQLCPGCGCS TLNQYFGYSG AFKCLKDGAG DVAFVKHSTI FENLANKADR DQYELLCLDN TRKPVDEYKD CHLAQVPSHT VVARSMGGKE DLIWELLNQA QEHFGKDKSK EFQLFSSPHG KDLLFKDSAH GFLKVPPRMD AKMYLGYEYV TAIRNLREGT CPEAPTDECK PVKWCALSHH ERLKCDEWSV NSVGKIECVS AETTEDCIAK IMNGEADAMS LDGGFVYIAG KCGLVPVLAE NYNKSDNCED TPEAGYFAVA VVKKSASDLT WDNLKGKKSC HTAVGRTAGW NIPMGLLYNK INHCRFDEFF SEGCAPGSKK DSSLCKLCMG SGLNLCEPNN KEGYYGYTGA FRCLVEKGDV AFVKHQTVPQ NTGGKNPDPW AKNLNEKDYE LLCLDGTRKP VEEYANCHLA RAPNHAVVTR KDKEACVHKI LRQQQHLFGS NVTDCSGNFC LFRSETKDLL FRDDTVCLAK LHDRNTYEKY LGEEYVKAVG NLRKCSTSSL LEACTFRRP.
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 :
TGFB3 MouseDescription:
Transforming Growth Factor-Beta 3 Mouse Recombinant
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Product # :
CYT-143Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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Description
TGF-β 3 Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.7kDa. The TGF-β 3 is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Mouse TGFB3 protein solution contains 20% Ethanol and 10mM Acetic acid.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity is determined by the ability to induce chondrogenic differentiation.More Info
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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Mouse TGF-beta 3 although stable at room temperature for 3 weeks, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
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Amino Acid Sequence
MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.718 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TGF-b 3 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 3 Human, Sf9Description:
Interleukin-3 Human Recombinant, Sf9
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Product # :
CYT-417Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Interleukin-3 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. The IL-3 CSF is fused to a C-terminal His-tag (6x His) and purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.5X PBS pH-7.4.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.More Info
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Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
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Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Pro-Thr.
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 :
Adiponectin Human, Sf9Description:
Adiponectin Human Recombinant, Sf9
Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.
Product # :
CYT-1002Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Acrp30 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules. -
Synonyms
Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.
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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
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.9kDa.
What is the source or expression system of ADIPONECTIN Protein?
Sf9, Baculovirus cells.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
Erythropoietin Human, ActiveDescription:
Erythropoietin Receptor Human Recombinant, Active
EPO-R, EPOR, Erythropoietin Receptor.
Product # :
CYT-997Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
EPOR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (25-250a.a.) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPOR is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPOR protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.More Info
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Introduction
Erythropoietin receptor, also known as EPOR arbitrates erythropoietin-induced erythroblast proliferation as well as differentiation. During EPO binding, EPOR activates Jak2 tyrosine kinase which activates various intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. Furthermore, stimulated EPOR has a function in erythroid cell survival. Mutations in EPOR may possibly produce erythroleukemia and familial erythrocytosis. In addition, dysregulation of EPOR can affect on the growth of selected tumors.
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Synonyms
EPO-R, EPOR, Erythropoietin Receptor.
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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
APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.
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Background
What is the molecular weight/Mw of ERYTHROPOIETIN Protein?
ERYTHROPOIETIN Protein has a total Mw of 25.6kDa.
What is the source or expression system of ERYTHROPOIETIN Protein?
Sf9, Baculovirus cells.
What is the Purity of ERYTHROPOIETIN Protein?
ERYTHROPOIETIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ERYTHROPOIETIN Protein?
Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.
What is the amino acid sequence of ERYTHROPOIETIN Protein?
APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.
What applications can ERYTHROPOIETIN Protein be used in?
ERYTHROPOIETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ERYTHROPOIETIN Protein?
The endotoxin level is minimal, ERYTHROPOIETIN 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 :
Leptin OvineDescription:
Leptin Ovine Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-239Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Leptin Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Ovine as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Adiponectin Human, HisDescription:
Adiponectin Human Recombinant, His tag
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-433Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
The Acrp30 Human is created as a recombinant protein with N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is 26.4 kDa protein containing 230 amino acid residues of the Acrp30 Human and 12 additional amino acid residues - HisTag (underlined).
Source
Escherichia Coli.
Formulation
Acrp30 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.02M Tris buffer pH7.5, 0.15M NaCl.
Purity
Acrp30 Human purity is greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human 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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Amino Acid Sequence
MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.
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Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26.4kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
DBH HumanDescription:
DBH Human Recombinant
EC 1.14.17.1, DBM, DBH.
Product # :
ENZ-891Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DBH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 599 amino acids (40-617 a.a) and having a molecular mass of 67.2kDa.DBH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DBH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
DBH catalyzes the chemical reaction. DBH is an oxidoreductase which belongs to the copper type II, ascorbate-dependent monooxygenase family, in particular those performing on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated can not be derived from O2 with reduced ascorbate as one donor, as well as incorporation of one ato of oxygen into the other donor.
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Synonyms
EC 1.14.17.1, DBM, DBH.
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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 MSAPRESPLP YHIPLDPEGS LELSWNVSYT QEAIHFQLLV RRLKAGVLFG MSDRGELENA DLVVLWTDGD TAYFADAWSD QKGQIHLDPQ QDYQLLQVQR TPEGLTLLFK RPFGTCDPKD YLIEDGTVHL VYGILEEPFR SLEAINGSGL QMGLQRVQLL KPNIPEPELP SDACTMEVQA PNIQIPSQET TYWCYIKELP KGFSRHHIIK YEPIVTKGNE ALVHHMEVFQ CAPEMDSVPH FSGPCDSKMK PDRLNYCRHV LAAWALGAKA FYYPEEAGLA FGGPGSSRYL RLEVHYHNPL VIEGRNDSSG IRLYYTAKLR RFNAGIMELG LVYTPVMAIP PRETAFILTG YCTDKCTQLA LPPSGIHIFA SQLHTHLTGR KVVTVLVRDG REWEIVNQDN HYSPHFQEIR MLKKVVSVHP GDVLITSCTY NTEDRELATV GGFGILEEMC VNYVHYYPQT QLELCKSAVD AGFLQKYFHL INRFNNEDVC TCPQASVSQQ FTSVPWNSFN RDVLKALYSF APISMHCNKS SAVRFQGEWN LQPLPKVIST LEEPTPQCPT SQGRSPAGPT VVSIGGGKG
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 :
BRAF HumanDescription:
B-Raf Proto-Oncogene Human Recombinant
Proto-Oncogene B-Raf, BRAF1, RAFB1, NS7, EC 2.7.11.1, B-RAF1, P94.
Product # :
PKA-071Price :
Quantity :
Shipping Method :
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Description
BRAF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 360 amino acids (432-766a.a) and having a molecular mass of 40.6kDa. BRAF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BRAF protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
B-Raf Proto-Oncogene, also known as BRAF is a member of the raf/mil family of serine/threonine protein kinases. BRAF participates in regulating the MAP kinase/ERKs signaling pathway, which eventually have an effect on cell division, differentiation, and secretion. Mutations in BRAF have been associated with cardiofaciocutaneous syndrome, which is a disease characterized by heart defects, mental retardation and a distinctive facial appearance. In addition, mutations in BRAF have also been associated with different cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, thyroid carcinoma, non-small cell lung carcinoma, as well as adenocarcinoma of lung.
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Synonyms
Proto-Oncogene B-Raf, BRAF1, RAFB1, NS7, EC 2.7.11.1, B-RAF1, P94.
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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 MGSEFSEDRN RMKTLGRRDS SDDWEIPDGQ ITVGQRIGSG SFGTVYKGKW HGDVAVKMLN VTAPTPQQLQ AFKNEVGVLR KTRHVNILLF MGYSTKPQLA IVTQWCEGSS LYHHLHIIET KFEMIKLIDI ARQTAQGMDY LHAKSIIHRD LKSNNIFLHE DLTVKIGDFG LATVKSRWSG SHQFEQLSGS ILWMAPEVIR MQDKNPYSFQ SDVYAFGIVL YELMTGQLPY SNINNRDQII FMVGRGYLSP DLSKVRSNCP KAMKRLMAEC LKKKRDERPL FPQILASIEL LARSLPKIHR SASEPSLNRA GFQTEDFSLY ACASPKTPIQ AGGYGAFPVH.
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 :
FHL3 HumanDescription:
Four And A Half LIM Domains 3 Human Recombinant
Four And A Half LIM Domains 3, SLIM2, Skeletal Muscle LIM-Protein 2, FHL-3, SLIM-2, Four And A Half LIM Domains Protein 3, LIM-Only Protein FHL3.
Product # :
PRO-1757Price :
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Description
FHL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 33.6kDa. FHL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FHL3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Four and a half LIM domains 3 (FHL3) belongs to a family of proteins containing a four-and-a-half LIM domain, which is a highly conserved double zinc finger motif. FHL3 has been shown to interact with the cancer developmental regulators SMAD2, SMAD3, and SMAD4, the skeletal muscle myogenesis protein MyoD, and the high-affinity IgE beta chain regulator MZF-1. FHL3 is involved in tumor suppression, repression of MyoD expression, and repression of IgE receptor expression. Two transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Four And A Half LIM Domains 3, SLIM2, Skeletal Muscle LIM-Protein 2, FHL-3, SLIM-2, Four And A Half LIM Domains Protein 3, LIM-Only Protein FHL3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSESFDC AKCNESLYGR KYIQTDSGPY CVPCYDNTFA NTCAECQQLI GHDSRELFYE DRHFHEGCFR CCRCQRSLAD EPFTCQDSEL LCNDCYCSAF SSQCSACGET VMPGSRKLEY GGQTWHEHCF LCSGCEQPLG SRSFVPDKGA HYCVPCYENK FAPRCARCSK TLTQGGVTYR DQPWHRECLV CTGCQTPLAG QQFTSRDEDP YCVACFGELF APKCSSCKRP IVGLGGGKYV SFEDRHWHHN CFSCARCSTS LVGQGFVPDG DQVLCQGCSQ AGP.
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 :
GFRA1 HumanDescription:
GDNF Family Receptor Alpha 1 Human Recombinant
GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.
Product # :
CYT-1026Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GFRA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-423) containing 409 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 46.0kDa (calculated).
Source
HEK293 cells.
Formulation
GFRA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline pH 7.5 containing 5 % (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.
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Synonyms
GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.
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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. GFRA1 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
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.
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Background
What is the molecular weight/Mw of GFRA1 Protein?
GFRA1 Protein has a total Mw of 46kDa.
What is the source or expression system of GFRA1 Protein?
HEK293 cells.
What is the Purity of GFRA1 Protein?
GFRA1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GFRA1 Protein?
The biological functionality of GFRA1 Protein will be determined in the future.
What is the amino acid sequence of GFRA1 Protein?
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.
What applications can GFRA1 Protein be used in?
GFRA1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GFRA1 Protein?
The endotoxin level is minimal, GFRA1 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 :
HBG2 HumanDescription:
Hemoglobin Gamma G Human Recombinant
TNCY, Hemoglobin subunit gamma-2, Gamma-2-globin, Hb F Gamma, Hemoglobin gamma-2 chain, Hemoglobin gamma-G chain.
Product # :
PRO-021Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HBG2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-147 a.a.) and having a molecular mass of 18.5kDa.HBG2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HBG2 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl,20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Hemoglobin subunit gamma-2 (HBG2), is a member of the globin family. HBG2 belongs to the fetal hemoglobin subunit, which comprised of two alpha chains organized with 2 gamma chains. HBG2 Amplified fetal hemoglobin production in adults and improve the clinical severity of sickle cell disease and beta-thalassemia major.
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Synonyms
TNCY, Hemoglobin subunit gamma-2, Gamma-2-globin, Hb F Gamma, Hemoglobin gamma-2 chain, Hemoglobin gamma-G chain.
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Physical Appearance
Sterile filtered reddish 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 MGSMGHFTEE DKATITSLWG KVNVEDAGGE TLGRLLVVYP WTQRFFDSFG NLSSASAIMG NPKVKAHGKK VLTSLGDAIK HLDDLKGTFA QLSELHCDKL HVDPENFKLL GNVLVTVLAI HFGKEFTPEV QASWQKMVTG VASALSSRYH.
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 :
RCHY1 HumanDescription:
Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant
ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.
Product # :
PRO-1536Price :
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Description
RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RCHY1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.
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Synonyms
ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.
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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 MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.
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 :
TGFB2 MouseDescription:
Transforming Growth Factor-Beta 2 Mouse Recombinant
Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.
Product # :
CYT-1266Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Transforming Growth Factor-Beta 2 Mouse Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
TGFB2 Mouse Recombinant is purified by proprietary chromatographic techniques.Source
CHO Cells.
Formulation
The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.More Info
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Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.
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Background
TGFB2 differ from TGFB1 in the tissue distribution, receptor interactions, and several biological roles.
TGFB2 requires TGFBR3 for its binding to TGFBR2 while TGFB1 binds directly to the receptor TGFBR2.
TGFB2 is crucial for embryonic development ocular biology, neural development, and tissue morphogenesis while TGFB1 is crucial for immune regulation and fibrosis.
TGFB2 exhibits more tissue-specific developmental expression Vs TGFB1.
What is the source or expression system of Mouse TGFB2 Protein?
CHO Cells
What is the Purity of Mouse TGFB2 Protein?
Mouse TGFB2 Protein is >97% pure as determined by SDS-PAGE.
What is the molecular weight / Mw of Mouse TGFB2 Protein?
Mouse TGFB2 Protein having a total Mw of 25.6kDa.
What is the Biological Activity of Mouse TGFB2 Protein?
The biological functionality of Mouse TGFB2 Protein is determined by mouse HT-2 cells.
What is the endotoxin level for Mouse TGFB2 Protein?
The endotoxin level is minimal, Mouse TGFB2 Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of Mouse TGFB2 Protein?
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.
Is TGFB2 a homodimer / homodimeric protein?
Yes, TGFB2 is homo dimer consisting of 2 identical chains.
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 :
Hepsin HumanDescription:
Hepsin Human Recombinant
HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.
Product # :
PRO-2846Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Hepsin Human Recombinant produced in Cho cells is a covalently-linked heterodimer having a total molecular mass of 43.0kDa. Hepsin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
CHO cells.
Formulation
The Hepsin protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity is >20,000 pmol/min/μg and was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC).More Info
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Synonyms
HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Hepsin Active although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hepsin Active should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles. -
Solubility
It is recommended to reconstitute the lyophilized Hepsin 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
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR.
Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H.
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Background
Hepsin is a type II transmembrane serine protease expressed primarily on epithelial cells, it takes part in extracellular proteolysis by activating precursor proteins such as pro-HGF and contributes to tissue remodeling, cell signaling, and normal epithelial function. Recombinant Hepsin is used to study prostate cancer, extracellular matrix remodelling, protease signalling pathways, tumor invasion, metastasis, HGF/MET signaling, and for screening inhibitors that target serine proteases
What is the molecular weight / Mw of Hepsin Protein?
Hepsin Protein has a total Mw of 43kDa.
What is the source or expression system of Hepsin Protein?
CHO Cells
What is the Purity of Hepsin Protein?
Hepsin Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Hepsin Protein?
The enzymatic activity was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC). The specific activity is >20,000 pmol/min/μg.
What is the amino acid sequence of Hepsin Protein?
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR
Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H
What applications can Hepsin Protein be used in?
Hepsin Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for Hepsin Protein?
The endotoxin level is minimal, Hepsin 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 :
Leptin BovineDescription:
Leptin Bovine Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-502Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Protein content
Protein quantitation 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. 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.