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1000 results found for “natural coagulation factors”
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Name :
GDF11 HumanDescription:
Growth and Differentiation factor 11 Human Recombinant
Growth Differentiation Factor 11, GDF-11, Bone Morphogenetic Protein 11, BMP11.
Product # :
CYT-402Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GDF11 Human Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2x109 amino acids and having a total molecular mass of 25kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, determined by the ability to inhibit alkaline phosphatase activity in ATDC5 cells, is typically less than 1 ng/mL. This corresponds to a specific activity of 1x106 units/mg.Citations
More Info
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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
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Synonyms
Growth Differentiation Factor 11, GDF-11, Bone Morphogenetic Protein 11, BMP11.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF11 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 GDF11 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
NLGLDCDEHS SESRCCRYPL TVDFEAFGWD WIIAPKRYKA NYCSGQCEYM FMQKYPHTHLVQQANPRGSA GPCCTPTKMS PINMLYFNDK QQIIYGKIPG MVVDRCGCS
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Background
What is the molecular weight/Mw of GDF11 HUMAN Protein?
GDF11 HUMAN Protein has a total Mw of 25kDa.
What is the source or expression system of GDF11 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF11 HUMAN Protein?
GDF11 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF11 HUMAN Protein?
The ED50, determined by the ability to inhibit alkaline phosphatase activity in ATDC5 cells, is typically less than 1 ng/mL. This corresponds to a specific activity of 1x106 units/mg.
What is the amino acid sequence of GDF11 HUMAN Protein?
NLGLDCDEHS SESRCCRYPL TVDFEAFGWD WIIAPKRYKA NYCSGQCEYM FMQKYPHTHL
VQQANPRGSA GPCCTPTKMS PINMLYFNDK QQIIYGKIPG MVVDRCGCS.
What applications can GDF11 HUMAN Protein be used in?
GDF11 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF11 HUMAN Protein?
The endotoxin level is minimal, GDF11 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Activin-A Human Plant-ActiveDescription:
Activin-A Human Recombinant, Plant-Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-414Price :
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Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana.
Formulation
Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4
Purity
Greater than 98% as obsereved by SDS-PAGE.
Biological Activity
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.Citations
More 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
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.
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Solubility
INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.
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Amino Acid Sequence
HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS. -
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.What is the source or expression system of Activin A Protein?
Nicotiana benthamiana.What is the Purity of Activin A Protein?
Activin A Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.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?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
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 :
NRG1 HumanDescription:
Heregulin-B2 Human Recombinant
Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.
Product # :
CYT-407Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Neuregulin-1 beta 2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. NRG-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in PBS, pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 5ng/ml, corresponding to a specific activity of > 2.0 × 105 U/mg.
Citations
More Info
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Introduction
Neuregulin is a signaling protein for ErbB2/ErbB4 receptor heterodimers on the cardiac muscle cells, playing an important role in heart structure and function through inducing ErbB2/ErbB4 receptor phosphorylation and cardiomyocyte differentiation. Research on molecular level discovered that neuregulin recombinant could make disturbed myocardial cell structure into order and strengthen the connection between myocardial cells by intercalated discs re-organization. Pharmacodynamic experiments in animals showed that neuregulin (NRG1) recombinant can reduce the degree of damage on myocardial cells caused by ischemia, hypoxia and viral infection.
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Synonyms
Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NRG1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heregulin 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 NRG1 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
SHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYKAEELYQ.
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 :
CEBPB AntibodyDescription:
CCAAT/enhancer-binding protein beta, Mouse Anti Human
CCAAT/enhancer-binding protein beta, C/EBP beta, Liver activator protein, Nuclear factor NF-IL6, Transcription factor 5, TCF-5, CEBPB, LAP, TCF5, CRP2, IL6DBP, MGC32080.
Product # :
ANT-406Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
-
Introduction
CEBPB is an intronless gene and its protein is a bZIP transcription factor which can bind as a homodimer to certain DNA regulatory regions. CEBPB can also form heterodimers with the related proteins CEBP-alpha, CEBP-delta, and CEBP-gamma. CEBPB is important in the regulation of genes involved in immune and inflammatory responses and has been shown to bind to the IL-1 response element in the IL-6 gene, as well as to regulatory regions of several acute-phase and cytokine genes. In addition, CEBPB can bind the promoter and upstream element and stimulate the expression of the collagen type I gene.
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Synonyms
CCAAT/enhancer-binding protein beta, C/EBP beta, Liver activator protein, Nuclear factor NF-IL6, Transcription factor 5, TCF-5, CEBPB, LAP, TCF5, CRP2, IL6DBP, MGC32080.
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Immunogen
Anti-human CEBPB mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CEBPB amino acids 1-271 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P47A1AT.
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Applications
CEBPB antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
CEBPB antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
MAPT Human 383a.a.Description:
Microtubule-Associated Protein Tau 383 a.a. Human Recombinant
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
Product # :
PRO-012Price :
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Shipped with Ice Packs
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Description
MAPT Human Recombinant (Isoform 3) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 403 amino acids (1-383 a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MAPT is a neuronal microtubule associated protein localized mostly on axons.
MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain. -
Synonyms
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL.
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 :
NDUFA2 HumanDescription:
NADH Dehydrogenase 1 Alpha Subcomplex 2 Human Recombinant
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2, Complex I-B8, CI-B8, NADH-ubiquinone oxidoreductase B8 subunit, NDUFA2, CD14, CIB8.
Product # :
ENZ-660Price :
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Shipped with Ice Packs
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Description
NDUFA2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 122 amino acids (1-99) and having a molecular mass of 13.3kDa.NDUFA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFA2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (NDUFA5) is a member of the complex I NDUFA5 subunit family. The human NDUFA5 gene codes for the B13 subunit of complex I of the respiratory chain that transfers electrons from NADH to ubiquinone. The NDUFA5 protein localizes to the inner mitochondrial membrane as part of the seven component-containing, water soluble 'iron-sulfur protein' (IP) fraction of complex I, even though its exact role is undetermined.
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Synonyms
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2, Complex I-B8, CI-B8, NADH-ubiquinone oxidoreductase B8 subunit, NDUFA2, CD14, CIB8.
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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 MGSMAAAAAS RGVGAKLGLR EIRIHLCQRS PGSQGVRDFI EKRYVELKKA NPDLPILIRE CSDVQPKLWA RYAFGQETNV PLNNFSADQV TRALENVLSG KA.
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 :
PhosphotransacetylaseDescription:
Phosphotransacetylase Bacillus S. Recombinant
Phosphate Acetyltransferase, EC 2.3.1.8, Phosphotransacetylase, phosphoacylase.
Product # :
ENZ-1205Price :
Quantity :
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Shipped at Room temp
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Description
Phosphotransacetylase Bacillus Stearothermophilus Recombinant produced in E.Coli is a single, non glycosylated polypeptide chain containing 325 amino acids and having a total molecular mass of 34.7kDa.
Phosphotransacetylase Recombinant is purified by proprietary chromatographic techniques.Source
E.Coli
Formulation
The protein was lyophilized with 0.15M NaCl and 20mM Tris pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Phosphotransacetylase activity is assessed by using the DTNB spectrophotometric method which was found to be greater than 3,000 Units/mg.Citations
More Info
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Introduction
Phosphotransacetylase (PTA) is a metabolic enzyme (EC 2.3.1.8) that catalyzes the reversible conversion: acetyl-CoA + Pi ⇄ acetyl-phosphate + CoA. The reversible reaction of acetyl-CoA to acetate node and back, is useful in R&D and biotech assays such as Metabolic engineering, Synthetic biology, Production of biopolymers, Enzymatic synthesis of acetyl-phosphate, bacterial signaling
and Fermentation. Phosphotransacetylase controls acetate formation and manipulates acetyl-CoA flux thus is widely used in protein expression, metabolic engineering, and synthetic pathways. -
Synonyms
Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Phosphate Acetyltransferase although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Phosphate Acetyltransferase should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Phosphate Acetyltransferase in
sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be
further diluted to other aqueous solutions. -
Amino Acid Sequence
TTDLFTALKA KVTGTARKIV FPEGTDDRIL TAASRLATEQ VLQPIVLGDE QAIRVKAAAL GLPLEGVEIV NPRRYGGFDE LVSAFVERRK GKVTEETARE LLFDENYFGT MLVYMGAADG LVSGAAHSTA DTVRPALQII KTKPGVGKTS GVFIMVRGDE KYVFADCAIN IAPNSQDLAE IAVESARTAK MFGLKPRVAL LSFSTKGSAS SPETEKVVEA VRLAKEMAPD LILDGEFQFD AAFVPEVAKK KAPDSVIQGD ANVFIFPSLE AGNIGYKIAQ RLGGFEAVGP ILQGLNKPVN DLSRGCSAED AYKLALITAA QSLGE
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Unit Definition
1 unit will convert 1umole of Coenzyme A to acetyl coenzyme A /min/pH-7.5/30˚C using acetyl phosphate as substrate
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 MouseDescription:
Leptin Mouse Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-351Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa. The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The mouse Leptin was lyophilized from a concentrated (1mg/ml) solution containing 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological activity of Mouse Leptin is performed by including proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.
Citations
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
AVPIQKVQDD TKTLIKTIVT RINDISHTQS VSAKQRVTGL DFIPGLHPIL SLSKMDQTLA VYQQVLTSLP SQNVLQIAND LENLRDLLHL LAFSKSCSLP QTSGLQKPES LDGVLEASLY STEVVALSRL QGSLQDILQQ LDVSPEC.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 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 :
FGFR1 Human, (22-374)Description:
Fibroblast Growth Factor Receptor-1, (22-374 a.a.) Human Recombinant
Fibroblast growth factor receptor 1 isoform 2, FGFR 1a, bFGF-R-1, BFGFR, CD331, CEK, ECCL, FGFBR, FGFR-1, FLG, FLT-2, FLT2, HBGFR, HH2, HRTFDS, KAL2, N-SAM, OGD.
Product # :
PKA-117Price :
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Shipped with Ice Packs
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Description
FGFR1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 361 amino acids (22-374a.a.) and having a molecular mass of 40.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). FGFR1 Human is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
FGFR1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FGFR1, also called fibroblast growth factor receptor 1 protein is encoded by the FGFR1 Gene. There are 4 types of related proteins (fibroblast growth factor receptors), one of them is the FGFR1 protein. The fibroblast growth factor receptors are responsible for many key cell pathways and processes, cell growth regulations, maturation processes, cell division, embryonic development, blood vessels formations etc.
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Synonyms
Fibroblast growth factor receptor 1 isoform 2, FGFR 1a, bFGF-R-1, BFGFR, CD331, CEK, ECCL, FGFBR, FGFR-1, FLG, FLT-2, FLT2, HBGFR, HH2, HRTFDS, KAL2, N-SAM, OGD.
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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
RPSPTLPEQA QPWGAPVEVE SFLVHPGDLL QLRCRLRDDV QSINWLRDGV QLAESNRTRI TGEEVEVQDS VPADSGLYAC VTSSPSGSDT TYFSVNVSDA LPSSEDDDDD DDSSSEEKET DNTKPNPVAP YWTSPEKMEK KLHAVPAAKT VKFKCPSSGT PNPTLRWLKN GKEFKPDHRI GGYKVRYATW SIIMDSVVPS DKGNYTCIVE NEYGSINHTY QLDVVERSPH RPILQAGLPA NKTVALGSNV EFMCKVYSDP QPHIQWLKHI EVNGSKIGPD NLPYVQILKT AGVNTTDKEM EVLHLRNVSF EDAGEYTCLA GNSIGLSHHS AWLTVLEALE ERPAVMTSPL YLELEHHHHH H
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 :
EIF2B1 HumanDescription:
Eukaryotic Translation Initiation Factor 2B Subunit 1 Alpha Human Recombinant
Translation initiation factor eIF-2B subunit alpha, eIF-2B GDP-GTP exchange factor subunit alpha, EIF2B1, EIF2BA, EIF2B.
Product # :
PRO-209Price :
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Shipping Method :
Shipped with Ice Packs
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Description
EIF2B1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (1-305 a.a.) and having a molecular mass of 35.8kDa.EIF2B1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF2B1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
EIF2B1 is one of five subunits of eukaryotic translation initiation factor 2B (EIF2B), which is a GTP exchange factor for eukaryotic initiation factor 2 and an essential regulator for protein synthesis. Phosphorylation of eIF2 inhibits GEF activity of EIF2B, an inhibition which requires the eIF2B1 subunit. Defects in eIF2B1 are a cause of leukoencephalopathy with vanishing white matter (VWM), a brain disease which is characterized by head trauma and motor deterioration.
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Synonyms
Translation initiation factor eIF-2B subunit alpha, eIF-2B GDP-GTP exchange factor subunit alpha, EIF2B1, EIF2BA, EIF2B.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT SAIETLCGVD SSVAVSSGGE LFLRFISLAS LEYSDYSKCK KIMIERGELF LRRISLSRNK IADLCHTFIK DGATILTHAY SRVVLRVLEA AVAAKKRFSV YVTESQPDLS GKKMAKALCH LNVPVTVVLD AAVGYIMEKA DLVIVGAEGV VENGGIINKI GTNQMAVCAK AQNKPFYVVA ESFKFVRLFP LNQQDVPDKF KYKADTLKVA QTGQDLKEEH PWVDYTAPSL ITLLFTDLGV LTPSAVSDEL IKLYL.
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 :
LGALS1 HumanDescription:
Galectin-1 Human Recombinant
Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.
Product # :
CYT-544Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
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Description
LGALS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids and having a molecular mass of 14.7kDa.The LGALS1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-1 protein was lyophilized from a concentrated (1mg/ml) containing 10mM sodium phosphate, pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity of Human Galectin-1 which is determined by the ability to induce chemotaxis of human THP-1 cells is detectable starting at 100ng/ml, corresponding to a specific activity of 1.0x104 units/mg.Citations
More Info
-
Introduction
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. Galectin-1 is an autocrine negative growth factor that regulates cell proliferation. Galectin-1 regulates cell apoptosis and cell differentiation. Galectin-1 binds CD45, CD3 and CD4 & inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of lyn kinase. Galectin-1 and its ligands are one of the master regulators of immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host–pathogen interactions. Galectin-1 expression or overexpression in tumors and/or the tissue surrounding them must be considered as a sign of the malignant tumor progression that is often related to the long-range dissemination of tumoral cells (metastasis), to their dissemination into the surrounding normal tissue, and to tumor immune-escape. Galectin-1 in its oxidized form plays a number of important roles in the regeneration of the central nervous system after injury. The targeted overexpression (or delivery) of Galectin-1 should be considered as a method of choice for the treatment of some kinds of inflammation-related diseases, neurodegenerative pathologies and muscular dystrophies. In contrast, the targeted inhibition of Galectin-1 expression is what should be developed for therapeutic applications against cancer progression. Galectin-1 is thus a promising molecular target for the development of new and original therapeutic tools. There is 88% homology between the human and mouse galectin-1.
-
Synonyms
Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Galectin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized LGALS1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD.
-
Background
What is the molecular weight/Mw of LGALS1 HUMAN Protein?
LGALS1 HUMAN Protein has a total Mw of 14.7kDa.
What is the source or expression system of LGALS1 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS1 HUMAN Protein?
LGALS1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS1 HUMAN Protein?
The activity of Human Galectin-1 which is determined by the ability to induce chemotaxis of human THP-1 cells is detectable starting at 100ng/ml, corresponding to a specific activity of 1.0x104 units/mg.
What is the amino acid sequence of LGALS1 HUMAN Protein?
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD.
What applications can LGALS1 HUMAN Protein be used in?
LGALS1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS1 HUMAN Protein?
The endotoxin level is minimal, LGALS1 HUMAN Protein was purified using conventional chromatography techniques.
-
Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.59 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.
- View Data Sheet
Name :
IRF5 AntibodyDescription:
Interferon Regulatory Factor-5, Mouse Anti Human
Interferon regulatory factor 5, IRF-5, IRF5, SLEB10.
Product # :
ANT-407Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
- Citations
Formulation
1mg/ml containing PBS, pH-7.4, & 0.02% Sodium Azide and 10% Glycerol.
Citations
More Info
-
Introduction
IRF5 belongs to the interferon regulatory factor (IRF) family, which is a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats.
-
Synonyms
Interferon regulatory factor 5, IRF-5, IRF5, SLEB10.
-
Immunogen
Anti-human IRF5 mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human IRF5 amino acids 176-240 purified from E. coli.
-
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
-
Clone
P10T1AT.
-
Applications
IRF5 antibody has been tested by ELISA, Western blot, ICC/IF, FACS and IHC analysis
to assure specificity and reactivity. Since application varies, however, each
investigation should be titrated by the reagent to obtain optimal results. -
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
IRF5 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
CASQ2 DogDescription:
Calsequestrin-2 Dog
Calsequestrin-2, Calsequestrin cardiac muscle isoform, CASQ2, CSQ.
Product # :
PRO-410Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Calsequestrin is the major calcium storage protein of the sarcoplasmic reticulum. Intraluminar Ca2+ binds to calsequestrin during diastole to prevent Ca2+ precipitation and to lower its free ionic concentration to facilitate efficient storage. During systole, Calsequestrin coordinately releases ~40-50 Ca2+ ions per molecule for each contraction-relaxation cycle by an uncertain mechanism. Calsequestrin has been shown to be of major importance in the regulation of cardiac excitation-contraction coupling.
Source
Dog Heart.
Formulation
The protein was lyophilized from a concentrated solution (1mg/ml) containing 10mM Tris-HCl and 1mM EGTA.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Synonyms
Calsequestrin-2, Calsequestrin cardiac muscle isoform, CASQ2, CSQ.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CASQ2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CASQ2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized CASQ2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
ABHD10 HumanDescription:
Abhydrolase Domain Containing 10 Human Recombinant
Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.
Product # :
ENZ-612Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ABHD10 Human Recombinant produced in E. coli is a single polypeptide chain containing 279 amino acids (53-306) and having a molecular mass of 30.9kDa.ABHD10 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ABHD10 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 100mM NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Abhydrolase domain-containing protein 10 (ABHD10) is a member of the AB hydrolase superfamily.
-
Synonyms
Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTSLSF LNRPDLPNLA YKKLKGKSPG IIFIPGYLSY MNGTKALAIE EFCKSLGHAC IRFDYSGVGS SDGNSEESTL GKWRKDVLSI IDDLADGPQI LVGSSLGGWL MLHAAIARPE KVVALIGVAT AADTLVTKFN QLPVELKKEV EMKGVWSMPS KYSEEGVYNV QYSFIKEAEH HCLLHSPIPV NCPIRLLHGM KDDIVPWHTS MQVADRVLST DVDVILRKHS DHRMREKADI QLLVYTIDDL IDKLSTIVN
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 :
DNMT3L HumanDescription:
DNA Cytosine-5--Methyltransferase 3-Like Human Recombinant
DNMT3L, DNA (Cytosine-5-)-Methyltransferase 3-Like, Human Cytosine-5-Methyltransferase 3-Like Protein 11, Cytosine-5-Methyltransferase 3-Like Protein, DNA (Cytosine-5)-Methyltransferase 3-Like.
Product # :
ENZ-787Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DNMT3L Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 411 amino acids (1-386) and having a molecular mass of 46.2kDa.DNMT3L is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DNMT3L solution (0.25mg/ml) contains 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.
Citations
More Info
-
Introduction
DNA Cytosine-5--Methyltransferase 3-Like (DNMT3L) is a nuclear protein with similarity to DNA methyltransferases, but is not believed to act as a DNA methyltransferase since it doesn’t contain the amino acid residues needed for methyltransferase activity. Nevertheless, DNMT3L stimulates de novo methylation by DNA cytosine methyltransferase 3 alpha and is assumed to be required for the formation of maternal genomic imprints. DNMT3L also mediates transcriptional repression as a result of interaction with histone deacetylase 1. DNMT3L is a catalytically inactive regulatory factor of DNA methyltransferases, which is vital for the function of DNMT3A and DNMT3B. DNMT3L activates DNMT3A and DNMT3B by binding to their catalytic domain. Furthermore, DNMT3L accelerates the binding of DNA and AdoMet to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases.
-
Synonyms
DNMT3L, DNA (Cytosine-5-)-Methyltransferase 3-Like, Human Cytosine-5-Methyltransferase 3-Like Protein 11, Cytosine-5-Methyltransferase 3-Like Protein, DNA (Cytosine-5)-Methyltransferase 3-Like.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMAAIP ALDPEAEPSM DVILVGSSEL SSSVSPGTGR DLIAYEVKAN QRNIEDICIC CGSLQVHTQH PLFEGGICAP CKDKFLDALF LYDDDGYQSY CSICCSGETL LICGNPDCTR CYCFECVDSL VGPGTSGKVH AMSNWVCYLC LPSSRSGLLQ RRRKWRSQLK AFYDRESENP LEMFETVPVW RRQPVRVLSL FEDIKKELTS LGFLESGSDP GQLKHVVDVT DTVRKDVEEW GPFDLVYGAT PPLGHTCDRP PSWYLFQFHR LLQYARPKPG SPRPFFWMFV DNLVLNKEDL DVASRFLEME PVTIPDVHGG SLQNAVRVWS NIPAIRSRHW ALVSEEELSL LAQNKQSSKL AAKWPTKLVK NCFLPLREYF KYFSTELTSS 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.
- View Data Sheet
Name :
CXCL10 Human, HisDescription:
IP-10 Human Recombinant (CXCL10), His Tag
Small inducible cytokine B10, CXCL10, 10 kDa interferon-gamma-induced protein, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
Product # :
CHM-346Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IP-10 His Tag Human Recombinant ?produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (22-98) and having a total molecular mass of 8.5 kDa with an amino-terminal hexahistidine tag. The IP-10 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IP-10 His is supplied in 10mM Tris HCl pH8, 1mM EDTA and 50% glycerol.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family that is also known as 10 kDa interferon-gamma-induced protein (?-IP10 or IP-10). CXCL10 is secreted by several cell types in response to IFN-?. These cell types include monocytes, endothelial cellsand fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytesand T cells, promotion of T cell adhesion to endothelial cells, anti tumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
-
Synonyms
Small inducible cytokine B10, CXCL10, 10 kDa interferon-gamma-induced protein, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
-
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. Please avoid freeze thaw cycles.
-
Background
What is the molecular weight/Mw of CXCL10 HUMAN, HIS Protein?
CXCL10 HUMAN, HIS Protein has a total Mw of 8.5kDa.
What is the source or expression system of CXCL10 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL10 HUMAN, HIS Protein?
CXCL10 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL10 HUMAN, HIS Protein?
The biological functionality of CXCL10 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL10 HUMAN, HIS Protein?
CXCL10 HUMAN, HIS Protein is composed from 77 amino acids.
What applications can CXCL10 HUMAN, HIS Protein be used in?
CXCL10 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL10 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL10 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
RHOC HumanDescription:
Ras Homolog Gene Family Member C Human Recombinant
ARH9, ARHC, H9, RHOH9, RAS-related homolog 9, Rho cDNA clone 9, Rho-related GTP-binding protein RhoC, ARH9, MGC1448, MGC61427, RHOC.
Product # :
PRO-865Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RHOC Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-190 a.a.) and having a molecular mass of 23.8 kDa. The RHOC is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RHOC Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
RHOC is a small signaling G protein/GTPase which is part of the Rac subfamily of the family Rho family of GTPases. RHOC rotats between inactive GDP-bound and active GTP-bound states and has a role as a molecular switch in signal transduction cascades. RHOC promotes reorganization of the actin cytoskeleton and regulates cell shape, attachment, and motility.
-
Synonyms
ARH9, ARHC, H9, RHOH9, RAS-related homolog 9, Rho cDNA clone 9, Rho-related GTP-binding protein RhoC, ARH9, MGC1448, MGC61427, RHOC.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD LRQDEHTRRE LAKMKQEPVR SEEGRDMANR ISAFGYLECS AKTKEGVREV FEMATRAGLQ VRKNKRRRGC.
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 :
LYG2 HumanDescription:
Lysozyme G-Like 2 Human Recombinant
Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.
Product # :
PRO-1245Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
- purity
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Description
LYG2 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (20-212) and having a molecular mass of 23.9 kDa. LYG2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The LYG2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
lysozyme G-like 2 and LYGH (LYG2), is a member of the glycosyl hydrolase 23 family. Lysozyme takes part in human innate immunity by causing bacterial cell lysis. LYG2 contains a SLT domain, a protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc).
-
Synonyms
Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSYPFSHS MKPHLHPRLY HGCYGDIMTM KTSGATCDAN SVMNCGIRGS EMFAEMDLRA IKPYQTLIKE VGQRHCVDPA VIAAIISRES HGGSVLQDGW DHRGLKFGLM QLDKQTYHPV GAWDSKEHLS QATGILTERI KAIQKKFPTW SVAQHLKGGL SAFKSGIEAI ATPSDIDNDF VNDIIARAKF YKRQSF.
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 :
NELL2 AntibodyDescription:
NEL-Like 2, Monoclonal Mouse Anti Human Antibody
NEL-like 2, NRP2, Nel-related protein 2, protein kinase C-binding protein NELL2, neural epidermal growth factor-like 2.
Product # :
ANT-030Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- More Info
- Citations
Formulation
1mg/ml containing Phosphate-Buffered Saline (pH 7.4) with 0.1% Sodium Azide.
Citations
More Info
-
Introduction
NELL2 is expressed in large quantities in neural tissues and has a significant role in the development of neural tissues. In addition, NELL protein has six epidermal growth factor (EGF)-like repeat domains which plays a part in calcium binding.
-
Synonyms
NEL-like 2, NRP2, Nel-related protein 2, protein kinase C-binding protein NELL2, neural epidermal growth factor-like 2.
-
Immunogen
Anti-human NELL2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human NELL2 protein.
-
Ig Subclass
Mouse IgG2b heavy chain and Kappa light chain
-
Clone
AT13E7.
-
Applications
The antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500.
Recommended starting dilution is 1:500 -
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
Recombinant human NELL2 antibody (30-258aa) is purified from E. coli.
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 :
Flt3 Ligand PorcineDescription:
Flt3 Ligand Porcine Recombinant
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Product # :
CYT-1041Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- purity
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Description
Flt3-Ligand Porcine Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.3kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein is lyophilized with 10mM Sodium Phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
-
Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Porcine Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.
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Background
What is the molecular weight/Mw of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein has a total Mw of 17.3kDa.
What is the source or expression system of FLT3 LIGAND PORCINE Protein?
Escherichia Coli.
What is the Purity of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FLT3 LIGAND PORCINE Protein?
The biological functionality of FLT3 LIGAND PORCINE Protein will be determined in the future.
What is the amino acid sequence of FLT3 LIGAND PORCINE Protein?
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.
What applications can FLT3 LIGAND PORCINE Protein be used in?
FLT3 LIGAND PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FLT3 LIGAND PORCINE Protein?
The endotoxin level is minimal, FLT3 LIGAND PORCINE 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 :
ANGPT1 HumanDescription:
Angiopoietin-1 Human Recombinant
Angiopoietin 1, KIAA0003, ANG-1, AGP1, AGPT.
Product # :
CYT-074Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
ANGPT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 480 amino acids (20-498) and having a molecular mass of 55.6 kDa.The ANGPT1 is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ANGPT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 5% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
ANGPT1 is an angiogenic factor which intervenes in blood vessel maturation and takes part in endothelial development. ANGPT1 is a secreted ligand for Tie-2, a cell surface receptor tyrosine kinase expressed in endothelial and hemopoietic cells. The glycosylated ANGPT1 protein has a coiled-coil region in the amino terminus and a fibrinogen-like domain at the carboxy terminus.
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Synonyms
Angiopoietin 1, KIAA0003, ANG-1, AGP1, AGPT.
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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
MSNQRRSPEN SGRRYNRIQH GQCAYTFILP EHDGNCREST TDQYNTNALQ RDAPHVEPDF SSQKLQHLEH VMENYTQWLQ KLENYIVENM KSEMAQIQQN AVQNHTATML EIGTSLLSQT AEQTRKLTDV ETQVLNQTSR LEIQLLENSL STYKLEKQLL QQTNEILKIH EKNSLLEHKI LEMEGKHKEE LDTLKEEKEN LQGLVTRQTY IIQELEKQLN RATTNNSVLQ KQQLELMDTV HNLVNLCTKE GVLLKGGKRE EEKPFRDCAD VYQAGFNKSG IYTIYINNMP EPKKVFCNMD VNGGGWTVIQ HREDGSLDFQ RGWKEYKMGF GNPSGEYWLG NEFIFAITSQ RQYMLRIELM DWEGNRAYSQ YDRFHIGNEK QNYRLYLKGH TGTAGKQSSL ILHGADFSTK DADNDNCMCK CALMLTGGWW FDACGPSNLN GMFYTAGQNH GKLNGIKWHY FKGPSYSLRS TTMMIRPLDF
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Background
This factor was found in the conditioned medium of the human neuroepithelioma cell line SHEP1 and the mouse myoblast cell line C2C12ras. The cDNA encoding a protein of 498 amino acids was isolated by using a secretion-trap expression cloning procedure exploiting the presence of a signal sequence present in growth factors that are secreted by producer cells (Davis et al, 1996). Murine and human factors show 97 % identity at the amino acid level. For a related factor see: CDT6. The human gene has been mapped to chromosome 8q22.3-q23 (Cheung et al, 1998).
The expression of angiopoietin-1 mRNA is downregulated by PDGF, EGF, IL1-beta, and TGF-beta (Enholm et al, 1997).
Angiopoietin-1 is a ligand for the receptor-like tyrosine kinase designated TIE-2 (Davis et al, 1996). Binding of Angiopoietin-1 to its receptor induces tyrosine phosphorylation of the cytoplasmic receptor domain. A naturally occuring antagonist of Angiopoietin-1 binding to TIE-2 is Angiopoietin-2. Angiopoietin-1 also binds to the TIE-1 receptor and this interaction appears to be critical for the development of the right-hand side venous system. It is dispensable for the left-hand side venous system, suggesting that right-hand and left-hand side vascular networks are established early before asymmetrical features of the network become morphologically discernible Loughna and Sato, 2001).
Angiopoietin-1 does not directly promote the growth of cultured endothelial cells. Angiopoietin-1 is chemotactic for endothelial cells (Witzenbichler et al, 1998). Excess soluble TIE-2 receptors abolish the chemotactic response of endothelial cells toward angiopoietin-1. Angiopoietin-1 has been shown to counteract cell death by apoptosis in cultured endothelial cells (Holash et al, 1999). Angiopoietin-1 also acts as an apoptosis survival factor for endothelial cells and this effect is augmented by the presence of VEGF (Kwak et al, 1999).
Angiopoietin-2 dose-dependently blocks directed migration toward Angiopoietin-1. Carlson et al (2001) have shown that Ang-1 binds rather selectively to vitronectin and that Ang-1 can directly support adhesion of human umbilical vein endothelial cells and fibroblasts in a process mediated by integrins.
The physiologic roles of Angiopoietin-1 and its receptor are limited to angiogenic processes that occur subsequent to the earlier vasculogenic and angiogenic actions of the VEGF family and their receptors. However, it is unlike most of the known angiogenesis factors such as VEGF and other classical endothelial cell growth factors in that addition of the factor to cultures of endothelial cells does not directly promote cell growth even though the TIE-2 receptor becomes activated. Angiopoietin-1 also appears to be incapable of inducing the formation of tubules by endothelial cells.
Angiopoietins can potentiate the effects of other angiogenic cytokines. An investigation of the impact of angiopoietins on neovascularization in vivo in the cornea micropocket assay of neovascularization demonstrates that neither Angiopoietin-1 nor Angiopoietin-2 alone promote neovascularization. Holash et al (1999) have shown that a subset of tumors initially grows by coopting existing host vessels. Regression of these vessels via a process that involves disruption of interactions between endothelial cells and smooth muscle cells as well as cell death by apoptosis of endothelial cells first causes loss of tumour cells before angiogenesis begins at the tumor margin and the tumor is rescued under the influence of VEGF, Angiopoietin-1, and probably other angiogenic stimuli.
The embryonic expression pattern of Angiopoietin-1 suggests that it plays a particularly important role in the developing heart. Angiopoietin-1 is expressed highly in the myocardial wall surrounding the endocardium expressing TIE-2. Expression of Angiopoietin-1 becomes much more widespread later in development.
ANGPT1 Protein has a total Mw of 55.6kDa.
What is the source or expression system of ANGPT1 Protein?
Escherichia Coli.
What is the Purity of ANGPT1 Protein?
ANGPT1 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPT1 Protein?
The biological functionality of ANGPT1 Protein will be determined in the future.
What is the amino acid sequence of ANGPT1 Protein?
MSNQRRSPEN SGRRYNRIQH GQCAYTFILP EHDGNCREST TDQYNTNALQ RDAPHVEPDF SSQKLQHLEH VMENYTQWLQ KLENYIVENM KSEMAQIQQN AVQNHTATML EIGTSLLSQT AEQTRKLTDV ETQVLNQTSR LEIQLLENSL STYKLEKQLL QQTNEILKIH EKNSLLEHKI LEMEGKHKEE LDTLKEEKEN LQGLVTRQTY IIQELEKQLN RATTNNSVLQ KQQLELMDTV HNLVNLCTKE GVLLKGGKRE EEKPFRDCAD VYQAGFNKSG IYTIYINNMP EPKKVFCNMD VNGGGWTVIQ HREDGSLDFQ RGWKEYKMGF GNPSGEYWLG NEFIFAITSQ RQYMLRIELM DWEGNRAYSQ YDRFHIGNEK QNYRLYLKGH TGTAGKQSSL ILHGADFSTK DADNDNCMCK CALMLTGGWW FDACGPSNLN GMFYTAGQNH GKLNGIKWHY FKGPSYSLRS TTMMIRPLDF
What applications can ANGPT1 Protein be used in?
ANGPT1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPT1 Protein?
The endotoxin level is minimal, ANGPT1 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 :
RFXANK HumanDescription:
Regulatory Factor X-Associated Ankyrin-Containing Protein Human Recombinant
ANKRA1, BLS, F14150_1, RFX-B, DNA-binding protein RFXANK, Ankyrin repeat family A protein 1, Regulatory factor X subunit B, Regulatory factor X-associated ankyrin-containing protein, RFXANK, RFXB.
Product # :
PRO-1537Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RFXANK Human Recombinant produced in E. coli is a single polypeptide chain containing 260 amino acids (1-237) and having a molecular mass of 28kDa. RFXANK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RFXANK solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Regulatory Factor X-Associated Ankyrin-Containing Protein (RFXANK) contains ankyrin repeats involved in protein-protein interactions. RFXANK, along with regulatory factor X-associated protein and regulatory factor-5, figures a complex which binds to the X box motif of certain MHC class II gene promoters and activates their transcription. After bound to the promoter, this complex associates with the non-DNA-binding factor MHC class II transactivator, which controls the cell type specificity and inducibility of MHC class II gene expression. Mutations in RFXANK have been linked to bare lymphocyte syndrome type II, complementation group B.
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Synonyms
ANKRA1, BLS, F14150_1, RFX-B, DNA-binding protein RFXANK, Ankyrin repeat family A protein 1, Regulatory factor X subunit B, Regulatory factor X-associated ankyrin-containing protein, RFXANK, RFXB.
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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 MGSMELTQPA EDLIQTQQTP ASELGDPEDP GEEAADGSDT VVLSLFPCTP EPVNPEPDAS VSSPQGSSLK HSTTLTNRQR GNEVSALPAT LDCDNLVNKP DERGFTPLIW ASAFGEIETV RFLLEWGADP HILAKERESA LSLASTGGYT DIVGLLLERD VDINIYDWNG GTPLLYAVRG NHVKCVEALL ARGADLTTEA DSGYTPMDLA VALGYRKVQQ VIENHILKLF QSNLVPADPE.
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 :
NTRK2 MouseDescription:
Neurotrophic Receptor Tyrosine Kinase 2 Mouse Recombinant
TrkB, NTRK2, NTRK-2, Tyrosine Kinase Receptor B, BDNF/NT-3 Growth Factors Receptor
Product # :
CYT-919Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NTRK2 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 409 amino acids (32-429a.a.) and having a molecular mass of 45.7kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa under reducing conditions).NTRK2 Mouse is expressed with an 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
NTRK2 Mouse protein solution (0.5mg/ml) contains PBS pH 7.4 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NTRK2 plays a role in the growth and the development of the central and the peripheral nervous systems using the regulation of neuron proliferation, migration, survival, differentiation, and synapse production. NTRK2 is a receptor for B-DNF and NT4. NTRK2 binds to neurotrophin-3 which regulates neuron survival through NTRK2. NTRK-2 activates numerous effectors such as SHC-1, SH2B-1, PLCG-1 and SH2B-2 that control overlapping signaling cascades.
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Synonyms
TrkB, NTRK2, NTRK-2, Tyrosine Kinase Receptor B, BDNF/NT-3 Growth Factors Receptor
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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
CPTSCKCSSA RIWCTEPSPG IVAFPRLEPN SVDPENITEI LIANQKRLEI INEDDVEAYV GLRNLTIVDS GLKFVAYKAF LKNSNLRHIN FTRNKLTSLS RRHFRHLDLS DLILTGNPFT CSCDIMWLKT LQETKSSPDT QDLYCLNESS KNMPLANLQI PNCGLPSARL AAPNLTVEEG KSVTLSCSVG GDPLPTLYWD VGNLVSKHMN ETSHTQGSLR ITNISSDDSG KQISCVAENL VGEDQDSVNL TVHFAPTITF LESPTSDHHW CIPFTVRGNP KPALQWFYNG AILNESKYIC TKIHVTNHTE YHGCLQLDNP THMNNGDYTL MAKNEYGKDE RQISAHFMGR PGVDYETNPN YPEVLYEDWT TPTDIGDTTN KSNEIPSTDV ADQSNREHAA ALEHHHHHH.
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 :
AMBP HumanDescription:
Microglobulin Alpha-1 Protein Human
Alpha-1 Microglobulin, A1M.
Product # :
PRO-407Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Alpha 1-microglobulin (A1M) is an immunomodulatory protein with a broad spectrum of possible clinical applications and seems a promising marker for evaluation of tubular function.
Source
Purified from the urine of patients with chronic renal tubular proteinuria.
Formulation
Lyophilized from 0.02M NH4HCO3. May contain traces of buffer salts.
Purity
Greater than 96.0%.
Citations
More Info
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Introduction
Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species. A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore. Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin. Alpha-1-microglobulin was first discovered in pathological human urine. It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include: inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.
Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis. -
Synonyms
Alpha-1 Microglobulin, A1M.
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Physical Appearance
Sterile Filtered Off-White lyophilized (freeze-dried) powder.
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Stability
Human A1M although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
Use phosphate buffer, pH>7.0 containing 0.15M NaCl, is recommended.
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Human Virus Test
Starting material tested and certified negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.
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.