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1000 results found for “Serum Amyloid A”
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Name :
PRKAA1 HumanDescription:
Protein Kinase, AMP-Activated, Alpha 1 Human Recombinant
5'-AMP-activated protein kinase catalytic subunit alpha-1, Protein Kinase, AMP-Activated, Alpha 1, PRKAA1, AMPK subunit alpha-1, Acetyl-CoA carboxylase kinase, ACACA kinase, Hydroxymethylglutaryl-CoA reductase kinase, HMGCR kinase, Tau-protein kinase PRKAA1, AMPK1, 5-AMP-activated protein kinase catalytic subunit alpha-1 isoform 1, AMPK, AMPKa11.
Product # :
PKA-074Price :
Quantity :
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Shipped with Ice Packs
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Description
PRKAA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279a.a) and having a molecular mass of 34.3kDa.PRKAA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
PRKAA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Protein Kinase, AMP-Activated, Alpha 1 (PRKAA1) is a protein coding gene which is the catalytic subunit of AMPK. AMPK is an energy sensor protein kinase which regulates cellular energy metabolism. AMPK adjusts the activity of various important metabolic enzymes by direct phosphorylation. Among its other features, AMPK protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways.
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Synonyms
5'-AMP-activated protein kinase catalytic subunit alpha-1, Protein Kinase, AMP-Activated, Alpha 1, PRKAA1, AMPK subunit alpha-1, Acetyl-CoA carboxylase kinase, ACACA kinase, Hydroxymethylglutaryl-CoA reductase kinase, HMGCR kinase, Tau-protein kinase PRKAA1, AMPK1, 5-AMP-activated protein kinase catalytic subunit alpha-1 isoform 1, AMPK, AMPKa11.
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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 MGSMRRLSSW RKMATAEKQK HDGRVKIGHY ILGDTLGVGT FGKVKVGKHE LTGHKVAVKI LNRQKIRSLD VVGKIRREIQ NLKLFRHPHI IKLYQVISTP SDIFMVMEYV SGGELFDYIC KNGRLDEKES RRLFQQILSG VDYCHRHMVV HRDLKPENVL LDAHMNAKIA DFGLSNMMSD GEFLRTSCGS PNYAAPEVIS GRLYAGPEVD IWSSGVILYA LLCGTLPFDD DHVPTLFKKI CDGIFYTPQY LNPSVISLLK HMLQVDPMKR ATIKDIREHE WF.
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 :
PSMA1 HumanDescription:
Proteasome Subunit Alpha Type 1 Human Recombinant
Proteasome (prosome macropain) subunit alpha type 1, PROS30, HC2, NU, Macropain subunit C2, Multicatalytic endopeptidase complex subunit C2, Proteasome component C2, Proteasome nu chain, 30 kDa prosomal protein, protein P30-33K, PROS-30, PSC2, EC 3.4.25.1.
Product # :
ENZ-178Price :
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Description
PSMA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 32.0 kDa.PSMA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PSMA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PSMA1 is a prosomal protein who takes part in a nonlysosomal ATP/ubiquitin-dependent proteolytic pathway. PSMA1 is a multicatalytic proteinase complex that is characterized by its capacity to cleave peptides with Arg, Phe, Tyr, Leu, and Glu next to the leaving group at neutral or slightly basic pH. PSMA1 is vastly expressed in prostate epithelium.
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Synonyms
Proteasome (prosome macropain) subunit alpha type 1, PROS30, HC2, NU, Macropain subunit C2, Multicatalytic endopeptidase complex subunit C2, Proteasome component C2, Proteasome nu chain, 30 kDa prosomal protein, protein P30-33K, PROS-30, PSC2, EC 3.4.25.1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMFRNQYD NDVTVWSPQG RIHQIEYAME AVKQGSATVG LKSKTHAVLV ALKRAQSELA AHQKKILHVD NHIGISIAGL TADARLLCNF MRQECLDSRF VFDRPLPVSR LVSLIGSKTQ IPTQRYGRRP YGVGLLIAGY DDMGPHIFQT CPSANYFDCR AMSIGARSQS ARTYLERHMS EFMECNLNEL VKHGLRALRE TLPAEQDLTT KNVSIGIVGK DLEFTIYDDD DVSPFLEGLE ERPQRKAQPA QPADEPAEKA DEPMEH
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 :
RAB2A HumanDescription:
RAB2A, Member RAS Oncogene Family Human Recombinant
Ras-related protein Rab-2A, RAB2A, RAB2.
Product # :
PRO-244Price :
Quantity :
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Shipped with Ice Packs
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Description
RAB2A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-212 a.a) and having a molecular mass of 26.1kDa.RAB2A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RAB2A protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ras-related protein Rab-2A (RAB2A)is a member of the small GTPase superfamily. RAB protein family members are nontransforming monomeric GTP-binding proteins of the Ras superfamily, which contain four highly conserved regions involved in GTP binding and hydrolysis. In addition, RAB proteins are a fundamental part of endocytic pathways. RAB2A and RAB2B are essential for protein transport from the ER to the Golgi; RAB2A is lipid-anchored to the ER-Golgi intermediate compartment membrane whereas RAB2B is lipid anchored to the cytoplasmic side of the cell membrane. RAB2A also interacts with GOLGA2.
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Synonyms
Ras-related protein Rab-2A, RAB2A, RAB2.
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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 SGSHMAYAYL FKYIIIGDTG VGKSCLLLQF TDKRFQPVHD LTIGVEFGAR MITIDGKQIK LQIWDTAGQE SFRSITRSYY RGAAGALLVY DITRRDTFNH LTTWLEDARQ HSNSNMVIML IGNKSDLESR REVKKEEGEA FAREHGLIFM ETSAKTASNV EEAFINTAKE IYEKIQEGVF DINNEANGIK IGPQHAATNA THAGNQGGQQ AGGGCC.
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 :
PPM1A AntibodyDescription:
Protein Phosphatase 1A Alpha Isoform, Mouse Anti Human
Protein phosphatase 1A, EC 3.1.3.16, Protein phosphatase 2C isoform alpha, PP2C-alpha, IA, PPM1A, PP2CA, MGC9201.
Product # :
ANT-309Price :
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
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Introduction
Protein Phosphatase 2C alpha is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding two distinct isoforms have been described. Protein phosphatase 2C(PP2Cα) is a Mn2+- or Mg2+-dependent protein serine/threonine phosphatase that is essential for regulating cellular stress response in eukaryotes.
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Synonyms
Protein phosphatase 1A, EC 3.1.3.16, Protein phosphatase 2C isoform alpha, PP2C-alpha, IA, PPM1A, PP2CA, MGC9201.
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Immunogen
Anti-human PPM1A mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PPM1A amino acids 1-382 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
Pp6c7AT.
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Applications
PPM1A 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 1:250 ~ 500. Recommended starting dilution is 1:250.
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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
PPM1A 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 :
IL1A PorcineDescription:
Interleukin-1 Alpha Porcine Recombinant
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.
Product # :
CYT-396Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-1A Porice Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 158 amino acids and having a molecular mass of 18076 Dalton. The IL-1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
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 D10S cells is < 0.03 ng/ml.Citations
More Info
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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
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Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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-1 alpha 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 Ser-Ala-Thr-Tyr-Ser.
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Background
What is the molecular weight/Mw of IL1A PORCINE Protein?
IL1A PORCINE Protein has a total Mw of 18kDa.
What is the source or expression system of IL1A PORCINE Protein?
Escherichia Coli.
What is the Purity of IL1A PORCINE Protein?
IL1A PORCINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL1A PORCINE Protein?
The ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.
What is the amino acid sequence of IL1A PORCINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Thr-Tyr-Ser.
What applications can IL1A PORCINE Protein be used in?
IL1A PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL1A PORCINE Protein?
The endotoxin level is minimal, IL1A PORCINE Protein was purified using conventional chromatography techniques.
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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 0.669 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 standard solution of IL-1 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.
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Name :
GlycininDescription:
Allergen Ara h 3.0101 Recombinant
Glycinin, Arah3.
Product # :
ALR-008Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa. Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Glycinin is supplied in 20mM HEPES buffer pH-8, 6M Urea and 0.25M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.
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Synonyms
Glycinin, Arah3.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
IL1A RatDescription:
Interleukin-1 alpha Rat Recombinant
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Product # :
CYT-381Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-1A Rat Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17703 Dalton. The IL-1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Tris-HCl, pH=8.
Purity
Greater than 98.0% 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 murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.Citations
More Info
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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
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Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 1a 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-His-Ser-Phe.
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Background
What is the molecular weight/Mw of IL1A RAT Protein?
IL1A RAT Protein has a total Mw of 17.7kDa.
What is the source or expression system of IL1A RAT Protein?
Escherichia Coli.
What is the Purity of IL1A RAT Protein?
IL1A RAT Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IL1A RAT Protein?
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.
What is the amino acid sequence of IL1A RAT Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-His-Ser-Phe.
What applications can IL1A RAT Protein be used in?
IL1A RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL1A RAT Protein?
The endotoxin level is minimal, IL1A RAT 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 :
HAVCR2 Human, Sf9Description:
Hepatitis A Virus Cellular Receptor 2 Human Recombinant, Sf9
Hepatitis A virus cellular receptor 2, HAVCR2, Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell immunoglobulin mucin receptor 3, TIM-3, T-cell membrane protein 3, TIM3, TIMD3, KIM-3.
Product # :
HAV-221Price :
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Shipped with Ice Packs
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Description
Recombinant Human HAVCR2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (aa 22-202) and having a molecular mass of 47.3kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). HAVCR2 is fused to a 239 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The HAVCR2 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hepatitis A Virus Cellular Receptor 2 (HAVCR2) is a member of the immunoglobulin superfamily. HACVR2 controls macrophage activation. HACVR2 inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and stimulates immunological tolerance.
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Synonyms
Hepatitis A virus cellular receptor 2, HAVCR2, Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell immunoglobulin mucin receptor 3, TIM-3, T-cell membrane protein 3, TIM3, TIMD3, KIM-3.
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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
ADLSEVEYRA EVGQNAYLPC FYTPAAPGNL VPVCWGKGAC PVFECGNVVL RTDERDVNYW TSRYWLNGDF RKGDVSLTIE NVTLADSGIY CCRIQIPGIM NDEKFNLKLV IKPAKVTPAP TRQRDFTAAF PRMLTTRGHG PAETQTLGSL PDINLTQIST LANELRDSRL ANDLRDSGAT IRIGLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.
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 :
H3N2 Influenza-A AntibodyDescription:
Influenza-A Hemagglutinin H3N2, Mouse Antibody
Product # :
ANT-215Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Hybridoma clones have been derived from hybridization of Sp2/0 myeloma cells with spleen cells of Balb/c mice immunized with Influenza A/Shandong/9/93 H3N2 derived from allantoic fluid of 10 days old embryonated eggs.
Formulation
In PBS, pH 7.4 and 0.1 % NaN3.
Citations
More Info
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Introduction
H3N2 is a subtype of the influenza A virus. Its name derives from the forms of the two kinds of proteinson the surface of its coat, hemagglutinin(H) and neuraminidase(N). H3N2 exchanges genes for internal proteins with other influenza subtypes. H3N2 has tended to dominate in prevalence over H1N1, H1N2, and influenza B. H3N2 strain descended from H2N2by antigenic shift, in which genes from multiple subtypes re-assorted to form a new virus. Both the H2N2and H3N2 strains contained genesfrom avian influenzaviruses.
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Physical Appearance
Sterile Filtered clear solution.
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Immunogen
Influenza A hemagglutinin H3N2.
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Ig Subclass
mouse IgG1.
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Clone
IA-H3N2.
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Applications
Influenza A haemagglutinin H3N2 immunodetection in direct or indirect ELISA, and Western Blotting.
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Shipping Conditions
Antibody is shipped as in liquid form with ice packs.
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Type
Mouse Antibody Monoclonal.
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Storage Procedures
Should be stored at 4C.Do not freeze.
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Purification Method
Protein-A column.
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 :
IL 28A HumanDescription:
Interleukin-28A Human Recombinant
Interleukin-28A, IL-28A, IFN-Lambda 2, IFN-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
Product # :
CYT-602Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL-28A human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 19.6 kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2 μm filtered solution containing no additives.
Purity
Greater than 85% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
IL-28A is distantly related to type I IFNs and the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection. -
Synonyms
Interleukin-28A, IL-28A, IFN-Lambda 2, IFN-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-Lambda 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 2 Recombinant 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 IL-28A 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
VPVAR LHGALPDARG CHIAQFKSLS PQELQAFKRAKDALEESLLL KDCRCHSRLF PRTWDLRQLQ VRERPMALEA ELALTLKVLE ATADTDPALV DVLDQPLHTL HHILSQFRAC IQPQPTAGPR TRGRLHHWLY RLQEAPKKES PGCLEASVTFNLFRLLTRDL NCVASGDLCV.
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 :
KRAS 2A HumanDescription:
Kirsten Rat Sarcoma Viral Oncogene, Isoform 2A Human Recombinant
GTPase KRas, K-Ras 2, Ki-Ras, c-K-ras, c-Ki-ras, KRAS, KRAS2, RASK2, C-K-RAS, CFC2, K-RAS2A, K-RAS2B, K-RAS4A, K-RAS4B, KI-RAS, KRAS1, NS, NS3, Kirsten rat sarcoma viral oncogene homolog.
Product # :
PRO-1446Price :
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Shipped with Ice Packs
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Description
KRAS 2A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-186 a.a) and having a molecular mass of 23.8kDa.KRAS 2A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KRAS 2A protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Kirsten Rat Sarcoma Viral Oncogene, Isoform 2A (KRAS-2A) belongs to the small GTPase superfamily. The KRAS-2A protein is involved in a variety of malignancies, including lung adenocarcinoma, mucinous adenoma, ductal carcinoma of the pancreas and colorectal carcinoma. Ras family members impact cell growth and differentiation events in a subcellular membrane compartmentalization-based signaling system under normal conditions. Oncogenic Ras can deregulate processes which control both cell proliferation and apoptosis.
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Synonyms
GTPase KRas, K-Ras 2, Ki-Ras, c-K-ras, c-Ki-ras, KRAS, KRAS2, RASK2, C-K-RAS, CFC2, K-RAS2A, K-RAS2B, K-RAS4A, K-RAS4B, KI-RAS, KRAS1, NS, NS3, Kirsten rat sarcoma viral oncogene homolog.
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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 MGSHMTEYKL VVVGAGGVGK SALTIQLIQN HFVDEYDPTI EDSYRKQVVI DGETCLLDIL DTAGQEEYSA MRDQYMRTGE GFLCVFAINN TKSFEDIHHY REQIKRVKDS EDVPMVLVGN KCDLPSRTVD TKQAQDLARS YGIPFIETSA KTRQRVEDAF YTLVREIRQY RLKKISKEEK TPGCVKIKKC.
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 :
APOE4 HumanDescription:
Apolipoprotein E4 Human Recombinant
Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.
Product # :
CYT-968Price :
Quantity :
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Description
Apolipoprotein E4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 299 amino acids and having a molecular mass of 34.4kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 20mM PBS, pH7.8 and 5% trehalose.
Purity
Greater than 95% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Biological Activity
When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.
Citations
More Info
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Introduction
Apolipoprotein E (APOE) is a chylomicron lipoprotein which is essential for the metabolism of lipoproteins and lipid transport. The APOE gene has 3 alleles, designated APOE2, APOE3, and APOE4. The APOE allelic proteins differ by only one or two amino acids, however have different biological structures and functions. APOE3 is the most common and neutral allele. The APOE4 allele is linked with an increased risk for Alzheimer's Disease (AD) and coronary artery disease (CAD). The APOE4 protein morphology decreases the ability of APOE4 to clear beta-amyloid protein from the brain, resulting in AD progression. The APOE2 allele is linked with type III hyperlipoproteinemia, which is characterized by defects in the clearance of plasma lipoproteins, however APOE2 may have a protective effect against AD.
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Synonyms
Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized APOE4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOE4 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 APOE4 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
KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.
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Background
What is the molecular weight/Mw of APOE4 Protein?
APOE4 Protein has a total Mw of 34.4kDa.
What is the source or expression system of APOE4 Protein?
Escherichia Coli.
What is the Purity of APOE4 Protein?
APOE4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of APOE4 Protein?
When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.
What is the amino acid sequence of APOE4 Protein?
KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.
What applications can APOE4 Protein be used in?
APOE4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOE4 Protein?
The endotoxin level is minimal, APOE4 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 :
HAV P2C-P3BDescription:
Hepatitis A Virus P2C-P3B Recombinant
Product # :
HAV-230Price :
Quantity :
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Description
The E.Coli derived 53.7 kDa recombinant protein fused to a GST tag contains the P2C-P3B immunodominant regions, amino acids 1492-1606.
Source
Escherichia Coli.
Formulation
10mM Tris-HCl, pH 9.6, 0.1% SDS and 50% glycerol.
Purity
HAV P2C-P3B protein is >90% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
Forty-two antigenic domains were identified across the hepatitis A virus (HAV) polyprotein by using a set of 237 overlapping 20-mer synthetic peptides spanning the entire HAV polyprotein. Nineteen antigenic domains were found within the structural proteins, and 22 were found within the nonstructural proteins, with 1 domain spanning the junction of VP1 and P2A proteins. Five of these domains were considered immunodominant, as judged by both the breadth and the strength of their immunoreactivity. One domain is located within the VP2 protein at position 57-90 aa. A second domain, located at position 767-842 aa, contains the C-terminal part of the VP1 protein and the entire P2A protein. A third domain, located at position 1403-1456 aa, comprises the C-terminal part of the P2C protein and the N-terminal half of the P3A protein. The fourth domain, located at position 1500-1519 aa, includes almost the entire P3B, and the last domain, located at position 1719-1764 aa, contains the C-terminal region of the P3C protein and the N-terminal region of the P3D protein. Four of the five most immunoreactive domains are derived from small HAV proteins and/or encompass protein cleavage sites separating different HAV proteins.
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Stability
HAV P2C-P3B Protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles
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Applications
HAV P2C-P3B antigen is suitable for ELISA and Western blots, excellent antigen for detection of HAV with minimal specificity problems.
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Specificity
Immunoreactive with sera HAV-infected individuals.
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Purification Method
HAV P2C-P3B protein was purified by proprietary chromatographic technique.
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 :
MEP1A HumanDescription:
Meprin A Subunit Alpha Human Recombinant
Meprin A Subunit Alpha, PABA Peptide Hydrolase, N-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit Alpha, Meprin A, Alpha (PABA Peptide Hydrolase), Endopeptidase-2, EC 3.4.24.18, PPH Alpha, BA268F1.1 (Meprin A Alpha (PABA Peptide Hydrolase)), EC 3.4.24, PPHA, MEP1A.
Product # :
PRO-2349Price :
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Description
MEP1A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 589 amino acids (22-601 a.a.) and having a molecular mass of 67.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). MEP1A is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MEP1A protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Meprin A subunit alpha (MEP1A) is a single-pass type I membrane protein which is a member of the peptidase M12A family. MEP1A is abundantly expressed in the kidney and intestinal epithelial cells, is secreted into the urinary tract and intestinal lumen, and found in leukocytes and cancer cells under certain conditions. MEP1A is capable of proteolytically degrading extracellular matrix proteins, proteolytically processing bioactive proteins, and has a role in inflammatory processes.
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Synonyms
Meprin A Subunit Alpha, PABA Peptide Hydrolase, N-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit Alpha, Meprin A, Alpha (PABA Peptide Hydrolase), Endopeptidase-2, EC 3.4.24.18, PPH Alpha, BA268F1.1 (Meprin A Alpha (PABA Peptide Hydrolase)), EC 3.4.24, PPHA, MEP1A.
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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
ADPVPIKYLP EENVHDADFG EQKDISEINL AAGLDLFQGD ILLQKSRNGL RDPNTRWTFP IPYILADNLG LNAKGAILYA FEMFRLKSCV DFKPYEGESS YIIFQQFDGC WSEVGDQHVG QNISIGQGCA YKAIIEHEIL HALGFYHEQS RTDRDDYVNI WWDQILSGYQ HNFDTYDDSL ITDLNTPYDY ESLMHYQPFS FNKNASVPTI TAKIPEFNSI IGQRLDFSAI DLERLNRMYN CTTTHTLLDH CTFEKANICG MIQGTRDDTD WAHQDSAQAG EVDHTLLGQC TGAGYFMQFS TSSGSAEEAA LLESRILYPK RKQQCLQFFY KMTGSPSDRL VVWVRRDDST GNVRKLVKVQ TFQGDDDHNW KIAHVVLKEE QKFRYLFQGT KGDPQNSTGG IYLDDITLTE TPCPTGVWTV RNFSQVLENT SKGDKLQSPR FYNSEGYGFG VTLYPNSRES SGYLRLAFHV CSGENDAILE WPVENRQVII TILDQEPDVR NRMSSSMVFT TSKSHTSPAI NDTVIWDRPS RVGTYHTDCN CFRSIDLGWS GFISHQMLKR RSFLKNDDLI IFVDFEDITH LSQHHHHHH.
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 :
METTL21A HumanDescription:
Methyltransferase Like 21A Human Recombinant
Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.
Product # :
ENZ-718Price :
Quantity :
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Shipped with Ice Packs
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Description
METTL21A Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (93-218) and having a molecular mass of 17 kDa.METTL21A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The METTL21A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
METTL21A, which is a part of the methyltransferase superfamily, is a Protein-lysine methyltransferase that in vitro methylates HSPA1, HSPA5 and HSPA8.
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Synonyms
Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.
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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 MGSTDRKVAL EFLKSNVQAN LPPHIQTKTV VKELTWGQNL GSFSPGEFDL ILGADIIYLE ETFTDLLQTL EHLCSNHSVI LLACRIRYER DNNFLAMLER QFTVRKVHYD PEKDVHIYEA QKRNQKEDL.
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 :
FCER1A Human 201 a.aDescription:
IgE Receptor Subunit A Human Recombinant
Fc Fragment Of IgE, High Affinity I, Receptor For; Alpha Polypeptide, FCE1A, IgE Fc Receptor Subunit Alpha, FcERI, Fc-Epsilon RI-Alpha, Fc Epsilon RI Alpha-Chain, Fc IgE Receptor, Alpha Polypeptide, High Affinity Immunoglobulin Epsilon Receptor Alpha-Subunit, High Affinity Immunoglobulin Epsilon Receptor Subunit Alpha, Immunoglobulin E Receptor, High-Affinity, Of Mast Cells, Alpha Polypeptide.
Product # :
PRO-2357Price :
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Shipped with Ice Packs
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Description
FCER1A Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 201 amino acids.FCER1Ais fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1x PBS, 50mM Arginine and 0.05% NaN3.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide (FCER1A) binds to the Fc region of immunoglobulins epsilon. FCER1A is a high affinity receptor. In addition FCER1A is responsible for starting the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators such as histamine which is responsible for the manifestations of allergy. This receptor is contains of an alpha subunit, a beta subunit, and two gamma subunits. FCER1A stands for the alpha subunit. Among the diseases associated with FCER1A are mast-cell leukemia, and allergic asthma.
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Synonyms
Fc Fragment Of IgE, High Affinity I, Receptor For; Alpha Polypeptide, FCE1A, IgE Fc Receptor Subunit Alpha, FcERI, Fc-Epsilon RI-Alpha, Fc Epsilon RI Alpha-Chain, Fc IgE Receptor, Alpha Polypeptide, High Affinity Immunoglobulin Epsilon Receptor Alpha-Subunit, High Affinity Immunoglobulin Epsilon Receptor Subunit Alpha, Immunoglobulin E Receptor, High-Affinity, Of Mast Cells, Alpha Polypeptide.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
The Recombinant FCER1A protein although stable at 4°C for 1 week, should be stored 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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Amino Acid Sequence
HMAPAMESPTL LCVALLFFAP DGVLAVPQKP KVSLNPPWNR IFKGENVTLT CNGNNFFEVS STKWFHNGSL SEETNSSLNI VNAKFEDSGE YKCQHQQVNE SEPVYLEVFS DWLLLQASAE VVMEGQPLFL RCHGWRNWDV YKVIYYKDGE ALKYWYENHN ISITNATVED SGTYYCTGKV WQLDYESEPL NITVIKAPLEHHHHHH.
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 :
INHBC HumanDescription:
Inhibin-Beta C Chain Human Recombinant
Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.
Product # :
HOR-010Price :
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Shipped with Ice Packs
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Description
INHBC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (237-352) and having a molecular mass of 14.9kDa.INHBC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The INHBC solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
INHBC, the beta C chain of inhibin, belongs to the TGF-beta superfamily. INHBC formulates heterodimers with beta A and beta B subunits. Other members of the TGF-beta superfamily are Actv's and Inhibins, hormones with contradictory roles which take part in pituitary, hypothalamic, and gonadal hormone secretion, as well as differentiation and growth of numerous cell types.
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Synonyms
Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.
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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 MGSGIDCQGG SRMCCRQEFF VDFREIGWHD WIIQPEGYAM NFCIGQCPLH IAGMPGIAAS FHTAVLNLLK ANTAAGTTGG GSCCVPTARR PLSLLYYDRD SNIVKTDIPD MVVEACGCS
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 :
C3a HumanDescription:
Complement C3a Human
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Product # :
PRO-2685Price :
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Description
Human Complement C3a produced in Human plasma is an non glycosylated polypeptide chain containing 77 amino acids having a molecular weight of 9,089 daltons.
Source
Human Plasma.
Formulation
C3a solution contains Phosphate buffered saline, pH 7.2.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Native human C3a is created by cleavage of human C3 protein by a human C3 convertase. C3a is a member of the anaphylatoxin family of three proteins (C3a, C4a and C5a) created by the activation of complement. C3a mediates various inflammatory responses including smooth muscle contraction, increased vascular permeability, vasodilation and release of histamine from mast cells and basophils. C3a (In contrast to C5a) does not exhibit significant neutrophil stimulating activities and does not induce chemotaxis, granule release or superoxide production. C3a acts through the C3a Receptor which is a G-protein coupled receptor found mainly on peripheral tissues, lymphoid cells and in the central nervous system. These activities of C3a are inactivated by removal of the C-terminal arginine which happens rapidly in plasma due to the action of carboxypeptidase N.
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Synonyms
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
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Physical Appearance
Sterile Filtered solution.
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Stability
C3a Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HTLV-I &II and HBSAG.
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 :
ANXA10 Human (1-162)Description:
Annexin A10 (1-162 a.a.) Human Recombinant
anxa-10.
Product # :
PRO-2837Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The ANXA10 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The ANXA10 His-Tagged Fusion Protein, produced in E. coli, is a 21kDa protein containing 162 amino acid residues of the ANXA10 Human, 1-162 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
anxa-10.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized ANXA10 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Annexin A10 also known as ANXA10 is a part of the annexin family of calcium-binding proteins which members own a conserved core domain and a unique amino-terminal region which may convene binding specificity. The ANXA10 protein contains 4 annexin domains and plays a role in the regulation of cellular growth and signal transduction pathways throughout the cell.
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 :
CDKN1A Human (20-149)Description:
Cyclin-Dependent Kinase Inhibitor 1A (20-149 a.a.) Human Recombinant
Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.
Product # :
PKA-137Price :
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Shipping Method :
Shipped at Room temp
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Description
The CDKN1A Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CDKN1A His-Tagged Fusion Protein, produced in E. coli, is a 20kDa protein containing 130 amino acid residues of the CDKN1A Human, 20-149 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized CDKN1A 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. 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
LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLEGDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLVPRSGEQAEGS PGGPGDSQGR KRRQTSMTDF
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Background
CDKN1A gene in humans plays an important role in maintaining genomic stability which is critical to cancer prevention and proper function of regular cellular processes. CDKN1A plays a main role in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. CDKN1A, along with CDK2 complexes aids to prevent kinase activity and inhibits progression through G1/S. CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Leptin-A TilapiaDescription:
Leptin-A Tilapia Recombinant
Product # :
CYT-1109Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Leptin-A Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 16,491 Dalton. The Leptin-A Tilapia is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.
Citations
More Info
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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin-A Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-A Tilapia 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-A Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.33 for 1 mg/ml Leptin-A Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
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 :
BMP 4 HumanDescription:
Bone Morphogenetic Protein-4 Human Recombinant
BMP4, ZYME, BMP2B, BMP2B1.
Product # :
CYT-361Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.
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Synonyms
BMP4, ZYME, BMP2B, BMP2B1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 Bone Morphogenetic Protein-4 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
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
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Background
What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant
As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.
Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.
Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!
How Does Bone Morphogenetic Protein-4 (BMP-4) Work?
Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.
The Role of BMP-4
This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.
However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:
- Embryonic development
- Wound healing
- Bone remodeling
- Immune response modulation
- Tissue repair
- Cardiac development and function
What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?
To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.
As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.
More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:
- Cancer therapy
- Development of engineered tissues and organs
- Bone regeneration for the treatment of osteoporosis and nonunion fractures
- Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
- Promotion of tissue repair and regeneration
Final Thoughts BMP-4
Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.
However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.
What is the molecular weight/Mw of BMP4 Protein?
BMP4 Protein has a total Mw of 13kDa.
What is the source or expression system of BMP4 Protein?
Escherichia Coli.
What is the Purity of BMP4 Protein?
BMP4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP4 Protein?
The biological functionality of BMP4 Protein will be determined in the future.
What is the amino acid sequence of BMP4 Protein?
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
What applications can BMP4 Protein be used in?
BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP4 Protein?
The endotoxin level is minimal, BMP4 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 :
IL1RA HumanDescription:
Interleukin-1 Receptor Antagonist Human Recombinant
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Product # :
CYT-203Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- purity
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Description
IL1ra Human Recombinant produced in E.Coli is a non-glycosylated, N-terminal methionyl form of the human naturally-occurring polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton. The IL1ra is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized protein with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant inhibition of IL-1 stimulation of D10S cells was found to be 0.5 ng/ml corresponding to a Specific Activity of 2,000,000IU/mg.Citations
More Info
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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
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Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin 1ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1ra 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-1 ra 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
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly.
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Background
What is the molecular weight/Mw of IL 1RA HUMAN Protein?
IL 1RA HUMAN Protein has a total Mw of 17kDa.
What is the source or expression system of IL 1RA HUMAN Protein?
Escherichia Coli.
What is the Purity of IL 1RA HUMAN Protein?
IL 1RA HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IL 1RA HUMAN Protein?
The ED50 as determined by the dose-dependant inhibition of IL-1 stimulation of D10S cells was found to be 0.5 ng/ml corresponding to a Specific Activity of 2,000,000IU/mg.
What is the amino acid sequence of IL 1RA HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly.
What applications can IL 1RA HUMAN Protein be used in?
IL 1RA HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL 1RA HUMAN Protein?
The endotoxin level is minimal, IL 1RA HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL 1RA HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL 1RA HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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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 0.89 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 standard solution of IL-1 ra 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.
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Name :
TNF a MouseDescription:
Tumor Necrosis Factor-Alpha Mouse Recombinant
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
CYT-252Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(c) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.Citations
More Info
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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha 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
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
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Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
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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 1.24 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 TNF-a 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.