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1000 results found for “Thrombin”
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Name :
PTPS HumanDescription:
6-Pyruvoyltetrahydropterin Synthase Human Recombinant
PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.
Product # :
ENZ-471Price :
Quantity :
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Shipped with Ice Packs
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Description
6-PyruvoylTetrahydropterin Synthase Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145) and having a molecular mass of 18.5kDa. 6-PyruvoylTetrahydropterin Synthase is fused to a 20 amino acid His Tag at N-terminus and purified using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
6-PyruvoylTetrahydropterin Synthase is formulated in 20mM Tris-HCl buffer pH-8, 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
6-PyruvoylTetrahydropterin Synthase is part of the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. 6-PyruvoylTetrahydropterin Synthase catalyzes the elimination of inorganic triphosphate from dihydroneopterin triphosphate, which is the second and irreversible step in the biosynthesis of tetrahydrobiopterin from GTP. Tetrahydrobiopterin, is a necessary cofactor and regulator of a range of enzyme activities, including enzymes involved in serotonin biosynthesis and NO synthase activity. Mutations in 6-PyruvoylTetrahydropterin Synthase gene result in hyperphenylalaninemia.
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Synonyms
PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.
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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 MSTEGGGRRC QAQVSRRISF SASHRLYSKF LSDEENLKLF GKCNNPNGHG HNYKVVVTVH GEIDPATGMV MNLADLKKYM EEAIMQPLDH KNLDMDVPYF ADVVSTTENV AVYIWDNLQK VLPVGVLYKV KVYETDNNIV VYKGE.
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 :
VAMP8 HumanDescription:
Endobrevin Human Recombinant
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
Product # :
PRO-660Price :
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Shipped with Ice Packs
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Description
VAMP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 96 amino acids (1-76 a.a.) and having a molecular mass of 10.9 kDa. The VAMP8 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatography techniques.
Source
Escherichia Coli.
Formulation
The VAMP8 protein solution (0.25mg/ml) contains 20mM Tris pH-8, 0.1mM PMSF, 0.2M NaCl and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.
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Synonyms
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
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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 MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM.
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 :
TXNDC12 HumanDescription:
Thioredoxin Domain Containing 12 Human Recombinant
Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.
Product # :
PRO-1133Price :
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Shipped with Ice Packs
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Description
TXNDC12 Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (27-172) and having a molecular mass of 20.8 kDa.TXNDC12 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TXNDC12 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TXNDC12 is a member of the thioredoxin super family. This Family members have a thioredoxin fold with a consensus active-site sequence (CxxC) and take part in redox regulation, protection against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors.
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Synonyms
Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMHN GLGKGFGDHI HWRTLEDGKK EAAASGLPLM VIIHKSWCGA CKALKPKFAE STEISELSHN FVMVNLEDEE EPKDEDFSPD GGYIPRILFL DPSGKVHPEI INENGNPSYK YFYVSAEQVV QGMKEAQERL TGDAFRKKHL EDEL
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TGFB2 HumanDescription:
Transforming Growth Factor Beta 2 Human Recombinant
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Product # :
CYT-441Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TGFB2 Human Recombinant produced in plants is a homodimeric polypeptide chain containing 2 x 118 amino acids and having a total molecular mass of 27.08kDa. The TGFB2 is fused to 6xHis Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Nicotiana benthamiana.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The biological activity of TGFB2 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 < 40ng/ml, corresponding to a specific activity of 25,000 units/mg.More Info
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Introduction
TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-β (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.
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Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB2 Human 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 TGFB2 in sterile 18M-cm H2O not less than 1µg/40µl, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HHHHHHALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIH
EPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASAS
PCCVSQDLEPLTI LYYIGKTPKIEQLSNMIVKSCKCS.
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 :
TSH HumanDescription:
Thyroid Stimulating Hormone Human
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
Product # :
HOR-001Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thyroid Stimulating Hormone Human produced in Human pituitary glands is an important indicator of thyroid function.
Source
Human pituitary glands
Formulation
Lyophilized from a concentrated solution containing 50mM ammonium bicarbonate.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
11.72 IU/mg vial by Centaur CP. Siemens Centaur CP is standardized against WHO 3rd IRP 81/565.More Info
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Introduction
Thyroid-stimulating hormone (also known as TSH or thyrotropin) is a hormone synthesized and secreted by thyrotrope cells in the anterior pituitary gland which regulates the endocrine function of the thyroid gland.
TSH stimulates the thyroid gland to secrete the hormones thyroxine (T4) and triiodothyronine (T3). TSH production is controlled by a Thyrotropin Releasing Hormone, (TRH), which is manufactured in the hypothalamus and transported to the Anterior Pituitary gland, where it increases TSH production and release. Somatostatin is also produced by the hypothalamus, and has an opposite effect on the pituitary production of TSH, decreasing or inhibiting its release.
The level of Thyroid hormones (T3 and T4) in the blood have an additional effect on the pituitary release of TSH, When the levels of T3 and T4 are low, the production of TSH is increased, and conversely, when levels of T3 and T4 are high, then TSH production is decreased. This effect creates a regulatory negative feedback loop.
TSH is a glycoprotein and consists of two subunits, the alpha and the beta subunit.
The a (alpha) subunit is identical to that of human chorionic gonadotropin (HCG), luteinising hormone (LH), follicle-stimulating hormone (FSH).
The b (beta) subunit is unique to TSH, and therefore determines its function. -
Synonyms
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSH 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 TSH in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the source or expression system of TSH HUMAN Protein?
Human pituitary glands
What is the Purity of TSH HUMAN Protein?
TSH HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of TSH HUMAN Protein?
11.72 IU/mg vial by Centaur CP. Siemens Centaur CP is standardized against WHO 3rd IRP 81/565.
What applications can TSH HUMAN Protein be used in?
TSH HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TSH HUMAN Protein?
The endotoxin level is minimal, TSH 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 :
Tri a 14.0101Description:
Non-Specific Lipid-Transfer Protein Tri a 14 Recombinant
Non-specific lipid-transfer protein, ltp142.
Product # :
ALR-025Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Non-Specific Lipid-Transfer Protein Tri a 14 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 13kDa. Tri a 14.0101 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Tri a 14.0101 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Tri a 14.0101 is a non-specific lipid transfer protein and a major wheat allergen. Those who are sensitive to this allergen may have baker’s asthma, a frequent occupational allergic disease caused mainly by inhalation of cereal flour, especially wheat flour. Tri a 14.0101 consists of 4 helical fragments and irregular C-terminal regions which are highly stable to heat treatment and proteolytic attack.
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Synonyms
Non-specific lipid-transfer protein, ltp142.
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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 samples.
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Applications
Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.
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 :
TROVE2 Human, His BiotinDescription:
TROVE Domain Family Member 2 Human Recombinant, His Tag Biotinylated
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-2560Price :
Quantity :
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Shipped with Ice Packs
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Description
TROVE2 Human Recombinant Biotin produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 56kDa. The TROVE2 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM HEPES (pH 8.0), 20% Glycerol and 150mM NaCl.
Purity
Greater than 89% as determined by Capillary Electrophoresis.
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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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.
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 :
TUBB3 HumanDescription:
Tubulin, Beta 3 Class III Human Recombinant
Beta-4, CDCBM, CFEOM3A, TUBB4 , Tubulin beta-3 chain, Tubulin beta-4 chain, Tubulin beta-III, TUBB3.
Product # :
PRO-1388Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TUBB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-450 a.a.) and having a molecular mass of 52.8kDa. TUBB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
TUBB3 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Tubulin, beta 3 class III (TUBB3), which is the major constituent of microtubules, is primarily Expressed in neurons and is involved in neurogenesis and in axon guidance and maintenance. TUBB3 binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.
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Synonyms
Beta-4, CDCBM, CFEOM3A, TUBB4 , Tubulin beta-3 chain, Tubulin beta-4 chain, Tubulin beta-III, TUBB3.
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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 MGSMREIVHI QAGQCGNQIG AKFWEVISDE HGIDPSGNYV GDSDLQLERI SVYYNEASSH KYVPRAILVD LEPGTMDSVR SGAFGHLFRP DNFIFGQSGA GNNWAKGHYT EGAELVDSVL DVVRKECENC DCLQGFQLTH SLGGGTGSGM GTLLISKVRE EYPDRIMNTF SVVPSPKVSD TVVEPYNATL SIHQLVENTD ETYCIDNEAL YDICFRTLKL ATPTYGDLNH LVSATMSGVT TSLRFPGQLN ADLRKLAVNM VPFPRLHFFM PGFAPLTARG SQQYRALTVP ELTQQMFDAK NMMAACDPRH GRYLTVATVF RGRMSMKEVD EQMLAIQSKN SSYFVEWIPN NVKVAVCDIP PRGLKMSSTF IGNSTAIQEL FKRISEQFTA MFRRKAFLHW YTGEGMDEME FTEAESNMND LVSEYQQYQD ATAEEEGEMY EDDEEESEAQ GPK.
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 :
HaptoglobinDescription:
Haptoglobin Human Recombinant
Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.
Product # :
PRO-567Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Haptoglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing fusion protein with His tag and having a total Mw of 33 kDa (4 kDa His-tag).
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Haptoglobin is a glycoprotein which is synthesized in the liver and circulates in the blood. Haptoglobin is produced typically by hepatocytes but also by other tissues: e.g. skin, lung, and kidney. It is a positive acute phase protein that binds free hemoglobin and removes it from the circulation to prevent kidney injury, and iron loss following hemolysis. The haptoglobin-hemoglobin complex is subsequently removed by the reticuloendothelial system (generally the spleen). As the reticuloendothelial system removes the haptoglobin-hemoglobin complex from the body, haptoglobin levels are reduced in hemolytic anaemias. In the course of binding hemoglobin, haptoglobin sequesters the iron inside hemoglobin, preventing iron-utilizing bacteria from benefitting from hemolysis.
Haptoglobin consists of two A- and two B-chains, connected by disulfide bonds. Three major haptoglobin phenotypes are known to exist (Hp 1-1, Hp 2-1, and Hp 2-2). Hp 1-1 is biologically the most effective in binding free hemoglobin and suppressing inflammatory responses associated with free hemoglobin. Hp 2-2 is biologically the least active, and Hp 2-1 is moderately active. Haptoglobin’s molecular mass ranges from 8-200 kDa.
Reduced levels can be seen in haemolysis and impaired liver function. High levels are a marker for acute or chronic inflammation. Ahaptoglobinemia or hypohaptoglobinemia are caused by mutations in the haptoglobin gene and/or its regulatory regions. Haptoglobin is also linked to diabetic nephropathy, the incidence of coronary artery disease in type 1 diabetes, Crohn's disease, inflammatory disease behavior, primary sclerosing cholangitis, susceptibility to idiopathic Parkinson's disease, and a reduced incidence of Plasmodium falciparum malaria. -
Synonyms
Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Haptoglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Haptoglobin 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 Haptoglobin 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
L ILGGHLDAKG SFPWQAKMVS HHNLTTGATL INEQWLLTTA KNLFLNHSEN ATAKDIAPTL TLYVGKKQLV EIEKVVLHPN YSQVDIGLIK LKQKVSVNER VMPICLPSKD YAEVGRVGYV SGWGRNANFK FTDHLKYVML PVADQDQCIR HYEGSTVPEK KTPKSPVGVQ PILNEHTFCA GMSKYQEDTC YGDAGSAFAV HDLEEDTWYA TGILSFDKSC AVAEYGVYVK VTSIQDWVQK TIAEN
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 :
TPO MouseDescription:
Thrombopoietin Mouse Recombinant
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.
Product # :
CYT-346Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thrombopoietin Mouse Recombinant produced in E.Coli is a single, non-glycosylated soluble polypeptide chain containing 174 amino acids and having a molecular mass of 18704 Dalton. The TPO is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
ED50 range is less than 0.8ng/ml as determined by the dose dependent stimulation of Mo7e cells.More Info
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Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidneyt hat regulates the production of platelets by the bone marrow. It stimulates the production and differentiation of megakaryocytes, the bone marrow cells that fragment into large numbers of platelets.
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Synonyms
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thrombopoietin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TPO Mouse 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 Thrombopoietin 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
SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKF.
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 :
D-Dimer HumanDescription:
D-Dimer Human
Product # :
PRO-2795Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
D-Dimer Human produced in Human Plasma is a specific degradation product of cross-linked fibrin and is used as a marker of hypercoagulation state that causes cardio-vascular diseases. D-Dimer is purified by proprietary chromatographic technique.
Source
Human plasma.
Formulation
D-Dimer was lyophilized from 10mM Tris-HCl and 0.15M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized D-Dimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution D-Dimer 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 D-Dimer in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
D-dimer, a small protein fragment present in the blood after a blood clot dissolves, is a vital marker in the realms of hematology and vascular medicine. Its presence signifies the ongoing process of fibrinolysis, where clots formed in blood vessels are broken down. Beyond its diagnostic significance, understanding the roles of D-dimer in human physiology and pathology is essential for comprehending coagulation disorders and cardiovascular diseases. This research delves into the multifaceted aspects of D-dimer, exploring its physiological functions, diagnostic applications, and implications in various medical conditions.
Physiological Functions:
In physiological conditions, coagulation and fibrinolysis are finely regulated processes, ensuring hemostasis and preventing excessive bleeding or clot formation. D-dimer is a natural byproduct of fibrinolysis, created when plasmin, an enzyme, breaks down fibrin clots. In this context, D-dimer acts as a marker of the body's intricate balance between clot formation and dissolution. It reflects the ongoing maintenance of vascular integrity, showcasing the body's ability to prevent unnecessary clotting.
Diagnostic Significance:
D-dimer holds significant diagnostic value, especially in the context of thrombotic disorders. Elevated levels of D-dimer in the blood are indicative of increased fibrinolysis, potentially signaling an underlying clotting disorder. Clinically, D-dimer assays are widely used to rule out thromboembolic events, such as deep vein thrombosis (DVT) or pulmonary embolism (PE). Moreover, D-dimer levels are crucial in risk stratification and decision-making processes in emergency departments, aiding in the timely diagnosis and treatment of thrombotic conditions.
Cardiovascular Implications:
Research has indicated a strong correlation between elevated D-dimer levels and cardiovascular diseases. In conditions like coronary artery disease (CAD) and stroke, where abnormal clot formation contributes to pathogenesis, D-dimer serves as a prognostic marker. Its presence hints at the ongoing vascular damage and the potential risk of acute events. Studying these correlations provides valuable insights into the progression of cardiovascular diseases, aiding in the development of targeted therapeutic strategies.
Beyond Coagulation Disorders:
Interestingly, recent research has begun to explore D-dimer's involvement in conditions beyond coagulation disorders. Studies suggest links between elevated D-dimer levels and inflammatory diseases, such as sepsis and rheumatoid arthritis. This expanding scope highlights the intricate interplay between coagulation, inflammation, and immune responses, shedding light on novel avenues for therapeutic interventions.
Conclusion:
D-dimer, once a simple marker of fibrinolysis, has evolved into a multifaceted indicator in the realm of medicine. Its physiological role as a byproduct of clot dissolution is intertwined with its diagnostic significance in thrombotic events and cardiovascular diseases. Furthermore, emerging research is uncovering its involvement in inflammatory processes, broadening its clinical implications. By delving into the complexities of D-dimer, scientists and clinicians pave the way for a deeper understanding of coagulation disorders and associated conditions, driving advancements in diagnostics and therapies.
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 :
TNNI3 HumanDescription:
Cardiac Troponin I Human Recombinant
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Product # :
PRO-324Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human TNNI3 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 210 amino acids having an additional methionine residue at N-terminus
The TNNI3 is purified by proprietary chromatographic techniques.Source
Escherichia Coli.
Formulation
Human TNNI3 was lyophilized in 0.01M HCl.
Purity
Greater than 95.0% as determined by both SDS-PAGE.
More Info
-
Introduction
Troponin I (TnI), troponin T (TnT) and troponin C (TnC) form the troponin complex of the thin filaments of striated muscle. TnI is acts as the inhibitory subunit by blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains 3 genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. The TNNI3 gene encodes the TnI-cardiac protein and is exclusively expressed in cardiac muscle tissues. Mutations in the TNNI3 gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).
-
Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TNNI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cardiac Troponin I 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 TNNI3 with urea /Tris buffer (20mM Tris, pH 7.5, 5 mM EDTA, 7 M urea and 15 mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQ
IAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEE
RYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKE
SLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES.
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 :
OTOR HumanDescription:
Otoraplin Human Recombinant
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
Product # :
CYT-582Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
- purity
- More Info
Description
Otoraplin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.7 kDa.The OTOR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OTOR protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM NaCl.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness. -
Synonyms
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized OTOR Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OTOR 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 Otoraplin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VHGIFMDRLASKKLCADDECVYTISLASAQEDYNAPDCRFINVKKGQQIYVYS
KLVKENGAGEFWAGSVYGDGQDEMGVVGYFPRNLVKEQRVYQEATKEVPTT
DIDFFCE.
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 :
Frataxin HumanDescription:
Frataxin Human Recombinant
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
Product # :
PRO-761Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
- purity
- More Info
Description
Frataxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids (42-210 a.a.) and having a molecular mass of 21.1 kDa. The Frataxin is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Frataxin solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Frataxin is a mitochondrial iron binding protein that is part of the FRATAXIN family. Frataxin functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Frataxin plays a role in iron homeostasis. Frataxin is an anti-apoptotic protein which prevents mitochondrial damage and reactive oxygen species (ROS) production.
-
Synonyms
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLRTDIDATC TPRRASSNQR GLNQIWNVKK QSVYLMNLRK SGTLGHPGSL DETTYERLAE ETLDSLAEFF EDLADKPYTF EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDWTG KNWVYSHDGV SLHELLAAEL TKALKTKLDL SSLAYSGKDA.
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 :
TSHR HumanDescription:
Thyroid Stimulating Hormone Receptor Human Recombinant
Product # :
HOR-051Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human Thyroid Stimulating Hormone Receptor produced in E. coli forms a dimer migrating at 46kDa on SDS-PAGE. TSHR Human contains multiple Leucine rich repeats with a histidine tag at N-terminus and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
TSHR solution (0.9mg/ml) contains PBS & 25mM K2CO3.
Purity
Protein is >85%.
More Info
-
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.
-
Applications
Serological assay for TSH receptor autoantibody.
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Background
The thyroid-stimulating hormone receptor (TSHR) is a critical component of the hypothalamic-pituitary-thyroid axis, playing an essential role in regulating thyroid function. TSHR, located on the surface of thyroid follicular cells, mediates the effects of thyroid-stimulating hormone (TSH) by stimulating the production and release of thyroid hormones. Research into human TSHR has revealed its significance not only in normal thyroid physiology but also in the pathogenesis of various thyroid disorders, including Graves' disease and thyroid cancer. This paper aims to provide an overview of research publications and information on human TSHR, highlighting its structure, function, and clinical implications.
What is the molecular weight/Mw of TSHR Protein?
TSHR Protein has a total Mw of 46kDa.
What is the source or expression system of TSHR Protein?
Escherichia Coli.
What is the Purity of TSHR Protein?
TSHR Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of TSHR Protein?
The biological functionality of TSHR Protein will be determined in the future.
What applications can TSHR Protein be used in?
TSHR Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TSHR Protein?
The endotoxin level is minimal, TSHR 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 :
Protein-A/G CysDescription:
Protein A/G Cys Recombinant
Product # :
PRO-1928Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
- formulation
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- More Info
- sds-page, HPLC
Description
Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-A/G was lyophilized without any additives.
Purity
Greater than 96.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.sds-page, HPLC
More Info
-
Introduction
The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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 Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEC.
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 :
Heparin Sodium PorcineDescription:
Heparin Sodium Porcine
Heparin, Porcine Heparin, Heparin Pig.
Product # :
PRO-2811Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- biological activity
- More Info
Description
Heparin Sodium Porcine is a natural native protein.
Source
Porcine Mucosa.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Biological Activity
200IU/mg.
More Info
-
Synonyms
Heparin, Porcine Heparin, Heparin Pig.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Heparin Sodium Porcine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heparin Sodium Porcine 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 Heparin Sodium Porcine in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
Heparin sodium, a highly sulfated glycosaminoglycan, has long been recognized for its pivotal role as an anticoagulant. In porcine systems, the study of Heparin Sodium takes on significance not only for its therapeutic applications in veterinary medicine but also for its potential translational impact on human health. This research embarks on an exploration of Heparin Sodium in porcine contexts, unraveling its structural intricacies, pharmacological attributes, and broader implications for health and biomedical interventions. By delving into the properties of Heparin Sodium in porcine models, scientists aim to deepen our understanding of its anticoagulant mechanisms, therapeutic potential, and the potential avenues for cross-species applications in healthcare.
Structural Insights into Porcine Heparin Sodium:
Porcine-derived Heparin Sodium, similar to its counterparts in other species, possesses a complex and highly sulfated structure. Understanding the nuances of its structure is fundamental for deciphering how Heparin Sodium interacts with antithrombin, leading to the inhibition of clotting factors and preventing the formation of blood clots. Structural insights contribute to optimizing its therapeutic efficacy.
Pharmacological Attributes and Anticoagulant Mechanisms:
Heparin Sodium's pharmacological attributes are central to its anticoagulant effects. In porcine systems, Heparin Sodium acts as an indirect anticoagulant by accelerating the activity of antithrombin, a natural inhibitor of clotting factors. Elucidating the specific mechanisms by which porcine Heparin Sodium modulates coagulation pathways contributes to refining its dosage and application in veterinary medicine.
Therapeutic Potential in Veterinary Medicine:
Porcine Heparin Sodium holds significant therapeutic potential in veterinary medicine, where clotting disorders and thrombotic events are prevalent. Understanding its pharmacokinetics, dosage requirements, and potential interactions with other drugs is crucial for optimizing its use in porcine healthcare. Additionally, exploring its safety profile in porcine models contributes to ensuring the well-being of animals under treatment.
Cross-Species Applications and Translational Insights:
Beyond its veterinary applications, porcine Heparin Sodium provides insights into potential cross-species applications, particularly in translational medicine. Understanding the similarities and differences in its anticoagulant mechanisms between porcine and human systems may open avenues for therapeutic innovations with relevance to both animal and human health.
Challenges and Future Directions:
While porcine Heparin Sodium presents opportunities for advancements in veterinary medicine and translational research, challenges persist. Fine-tuning its applications, addressing potential variations in its anticoagulant properties across different porcine breeds, and ensuring its safety and efficacy in diverse clinical scenarios are critical considerations for translational success.
Porcine Heparin Sodium emerges as a key player in the landscape of anticoagulation, offering a bridge between veterinary and translational medicine. Its structural insights, pharmacological attributes, and therapeutic potential in porcine systems contribute not only to veterinary care but also offer translational insights with implications for human health. As researchers continue to unravel the molecular intricacies of porcine Heparin Sodium, they not only deepen our understanding of anticoagulation in veterinary contexts but also pave the way for innovative biomedical applications, shaping the future of healthcare for both animals and humans.
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 :
scIC2Description:
Single Chain Cardiac Troponin I-C 2nd generation Recombinant
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Product # :
PRO-346Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Single Chain Cardiac Troponin I-C 2nd generation produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa28-110-Linker-cTnC), having a molecular weight of 30kDa.1mg of scIC2 is equivalent to 0.82mg of full length human cardiac TNI on a molar basis.The scIC2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl, 250mM NaCl and 50% glycerol, pH 7.5.
Purity
Greater than 91.0% as determined by SDS-PAGE.
More Info
-
Introduction
Troponin Complex is a heteromeric protein playing an important role in the regulation of skeletal and cardiac muscle contraction. It consists of three subunits, Troponin I, Troponin T and TroponinC. Each subunit is responsible for part of Troponin Complex function. E.g. Troponin I inhibits ATP-ase activity of acto-myosin.Troponin T and Troponin Iare presented in cardiac muscles in different forms than in skeletal muscles. Purified subunits of rcTnI, rcTnC and rcTnT are recomplexed in vitro under appropriate conditions.
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
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Physical Appearance
Sterile Filtered colourless liquid formualtion.
-
Stability
scIC2 although stable at 10°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TROVE2 Bovine, BiotinDescription:
TROVE Domain Family Member 2 Human Recombinant, Biotinlyated
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-2561Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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- More Info
Description
TROVE2 is a biotinlyated natural protein having a molecular mass of 58kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.
Source
Bovine tissues.
Formulation
TROVE2 is supplied in 20mM HEPES buffer pH-8.0, 150mM NaCl and 20% glycerol.
Purity
Greater than 83.0% as determined by SDS-PAGE.
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
B2M Human RecombinantDescription:
Beta 2 Microglobulin Human Recombinant
Beta-2-microglobulin, B2M.
Product # :
PRO-337Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
B2 Microglobulin Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 12 kDa.
The B2M is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated solution (1mg/ml) containing Citrate-Na, PH 6.9.
Purity
Greater than 95.0% as determined by HPLC.
More Info
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Introduction
B2 microglobulin is an 11 kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. ?2 microglobulin associates with class I-like molecules such as CD1 and Qa as well as with the alpha chain of MHC class I molecules. Very limited amounts of MHC class I molecules can be found on the surface in the absence of ?2 microglobulin. CD8 T cells cannot develop in the absence of MHC class I.
Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinaemia, renal failure, or kidney transplants. Human Beta 2 microglobulin levels can rise either because its rate of synthesis has increased (e.g. in AIDS, malignant monoclonal plasma cell dyscrasia, solid tumors and autoimmune disease) or because of impaired renal filtration (e.g. due to renal insufficiency, graft rejection or nephrotoxicity induced by post-transplantation immunosuppressive therapy). Beta-2 microglobulin levels might also be elevated in multiple myeloma and lymphoma cases. Dialysis-related amyloidosis develops after a long-term hemodialysis, it can aggregate into amyloid fibers that deposit in joint spaces. -
Synonyms
Beta-2-microglobulin, B2M.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized B2M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution B2M 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 B2M in sterile 18MΩ-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 :
sRAGE HumanDescription:
Advanced Glycosylation End Product-Specific Receptor Human Recombinant
Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.
Product # :
PRO-600Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
sRAGE Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 339 amino acids and having a molecular mass of 36.5 kDa. The Human sRAGE is fused to a 14 a.a. His tag at N-Terminus.The Human sRAGE is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile filtered (0.4 µm) concentrated (0.5mg/ml) protein solution was lyophilized with 30mM acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
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Introduction
sRAGE is a member of the immunoglobulin superfamily of cell surface molecules. sRAGE is a receptor for various molecules, including the amyloidogenic form of serum amyloid A, amyloid-beta protein, members of the S100/calgranulin superfamily and advanced glycation end products. sRAGE lies within the major histocompatibility complex (MHC) class III region on chromosome 6. Alternative splicing results in two transcript variants encoding different isoforms. sRAGE mediates interactions of nonenzymatic glycosylated proteins which accumulate in vascular tissue during aging & at an increasing rate in diabetes. sRAGE is a receptor for amyloid beta peptide.
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Synonyms
Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
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Solubility
Add 0.1M Acetate buffer pH4 to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MRGSHHHHHH GMASAQNITA RIGEPLVLKC KGAPKKPPQR LEWKLNTGRT EAWKVLSPQG GGPWDSVARV LPNGSLFLPAV GIQDEGIFRCQ AMNRNGKETKS NYRVRVYQIP GKPEIVDSASE LTAGVPNKVG TCVSEGSYPA GTLSWHLDGKPL VPNEKGVSVK EQTRRHPETG LFTLQSELMV TPARGGDPRP TFSCSFSPGL PRHRALRTAP IQPRVWEPVPL EEVQLVVEPE GGAVAPGGTV TLTCEVPAQP SPQIHWMKDGVP LPLPPSPVLI LPEIGPQDQG TYSCVATHSS HGPQESRAVS ISIIEPGEEG PTAGEGFDKV REAEDSPQHM
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 :
TPO HumanDescription:
Thyroid Peroxidase Human Recombinant
Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.
Product # :
ENZ-285Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Thyroid Peroxidase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing 834 amino acids and having a molecular mass of 92,872 Dalton (excluding glycosylation), 101 kDa total mass.The TPO is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
TPO is supplied in 16mM HEPES pH-7.6, 160mM NaCl, 0.08mM Kl and 20% glycerol.
Purity
Greater than 95% as determined by Densitometric Analysis
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Introduction
Thyroid Peroxidase (TPO) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. Its identity with the formerly so-called `microsomal antigen` has been shown several years ago. As an integral membrane glycoprotein it is restricted to the apical plasma membrane of the follicular epithelial cells and comprises two identical subunits of approx. 100 kDa molecular weight. The hemoprotein TPO plays a key role in the thyroid hormone biosynthesis by catalysing both the iodination of tyrosyl residues and the coupling of iodotyrosyl residues in thyroglobulin (TG) to form precursors of the thyroid hormones T4 and T3.
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Synonyms
Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.
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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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coating concentration
0.15-0.375 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.
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 :
TRIB3 HumanDescription:
Tribbles Pseudokinase 3 Human Recombinant
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Tribbles homolog 3.
Product # :
PKA-070Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- purity
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Description
TRIB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 42.0kDa. TRIB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TRIB3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
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Introduction
Tribbles Pseudokinase 3, also known as TRIB3, is a putative protein kinase which is induced by the transcription factor NF-kappaB. In addition, TRIB3 is a negative regulator of NF-kappaB, and can as well sensitize cells to TNF- and TRAIL-induced apoptosis. Furthermore, TRIB3 is able to negatively regulate the cell survival serine-threonine kinase AKT1. One of the diseases which are associated with TRIB3 is anoxia.
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Synonyms
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Tribbles homolog 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
MGSSHHHHHH SSGLVPRGSH MGSMRATPLA APAGSLSRKK RLELDDNLDT ERPVQKRARS GPQPRLPPCL LPLSPPTAPD RATAVATASR LGPYVLLEPE EGGRAYQALH CPTGTEYTCK VYPVQEALAV LEPYARLPPH KHVARPTEVL AGTQLLYAFF TRTHGDMHSL VRSRHRIPEP EAAVLFRQMA TALAHCHQHG LVLRDLKLCR FVFADRERKK LVLENLEDSC VLTGPDDSLW DKHACPAYVG PEILSSRASY SGKAADVWSL GVALFTMLAG HYPFQDSEPV LLFGKIRRGA YALPAGLSAP ARCLVRCLLR REPAERLTAT GILLHPWLRQ DPMPLAPTRS HLWEAAQVVP DGLGLDEARE EEGDREVVLY G.
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 :
TXNRD1 Human 161-649 a.a.Description:
Thioredoxin Reductase 1 161-649 a.a. Human Recombinant
Thioredoxin reductase 1 cytoplasmic, TR, Gene associated with retinoic and interferon-induced mortality 12 protein, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.
Product # :
ENZ-042Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- purity
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Description
TXNRD1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 510 amino acids (161-649 a.a.) and having a molecular mass of 55.9kDa. The TXNRD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TXNRD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TXNRD1 belongs to the selenium-containing pyridine nucleotide-disulphide oxidoreductase family, which has a conserved catalytic site of Cys-Val-Asn-Val-Gly-Cys. TXNRD1 decreases thioredoxins as well as other substrates, and participates in selenium metabolism and protection against oxidative stress. Inhibition of TXNRD1 activity serves as a potential treatment for cancer, AIDS and other autoimmune diseases as well as bacterial infections and parasitic diseases.
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Synonyms
Thioredoxin reductase 1 cytoplasmic, TR, Gene associated with retinoic and interferon-induced mortality 12 protein, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.
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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 MYDYDLIIIG GGSGGLAAAK EAAQYGKKVM VLDFVTPTPL GTRWGLGGTC VNVGCIPKKL MHQAALLGQA LQDSRNYGWK VEETVKHDWD RMIEAVQNHI GSLNWGYRVA LREKKVVYEN AYGQFIGPHR IKATNNKGKE KIYSAERFLI ATGERPRYLG IPGDKEYCIS SDDLFSLPYC PGKTLVVGAS YVALECAGFL AGIGLDVTVM VRSILLRGFD QDMANKIGEH MEEHGIKFIR QFVPIKVEQI EAGTPGRLRV VAQSTNSEEI IEGEYNTVML AIGRDACTRK IGLETVGVKI NEKTGKIPVT DEEQTNVPYI YAIGDILEDK VELTPVAIQA GRLLAQRLYA GSTVKCDYEN VPTTVFTPLE YGACGLSEEK AVEKFGEENI EVYHSYFWPL EWTIPSRDNN KCYAKIICNT KDNERVVGFH VLGPNAGEVT QGFAAALKCG LTKKQLDSTI GIHPVCAEVF TTLSVTKRSG ASILQAGCCG.
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.