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1000 results found for “Thymosin”
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Name :
Thymosin alpha 1Description:
Thymosin a1 Acetate
Product # :
HOR-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymosin a1 acetate, also known as thymalfasin has immunoregulatory properties enhancing immune functions. Thymosin a1 has a molecular formula of C129H215N33O55 a.a. sequence of Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn-OH and having a Mw of 3108.32 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Thymalfasin is a synthetic analogue of thymosin-alpha-1, a 28-amino acid protein derived from the precursor protein prothymosin-alpha. Exhibiting a variety of immunoregulating properties, thymosin-alpha-1 induces differentiation of murine T-cell precursors and human thymocytes and the terminal differentiation of functionally immature cord blood lymphocytes and induces production of IL-2, high affinity IL-2 receptors, and B-cell growth factors by peripheral blood mononuclear cells. T-helper and cytotoxic/suppressor T-cell populations are targets of thymosin activity. Thymosin-alpha-1 has been shown to increase the efficiency of antigen presentation by macrophages and to be an endogenous modulator of alpha-thrombin activity.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin a1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymalfasin 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 Thymosin a1 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 molecular weight/Mw of THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein has a total Mw of 3.1kDa.
What is the Purity of THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of THYMOSIN-A1 HUMAN Protein?
The biological functionality of THYMOSIN-A1 HUMAN Protein will be determined in the future.
What applications can THYMOSIN-A1 HUMAN Protein be used in?
THYMOSIN-A1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for THYMOSIN-A1 HUMAN Protein?
The endotoxin level is minimal, THYMOSIN-A1 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.
- View Data Sheet
Name :
Thymosin beta 4 HumanDescription:
Thymosin-b4 Human Recombinant
Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.
Product # :
HOR-003Price :
Quantity :
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Shipped at Room temp
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Description
Thymosin b4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 43 amino acids and having a molecular mass of 4.9kDa.The Thymosin b4 Human is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2um filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Citations
More Info
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Introduction
CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.
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Synonyms
Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin B4 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymosin B4 Human should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Thymosin B4 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
SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES
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Background
What is the molecular weight/Mw of THYMOSIN BETA 4 HUMAN Protein?
THYMOSIN BETA 4 HUMAN Protein has a total Mw of 4.9kDa.
What is the source or expression system of THYMOSIN BETA 4 HUMAN Protein?
Escherichia Coli.
What is the Purity of THYMOSIN BETA 4 HUMAN Protein?
THYMOSIN BETA 4 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of THYMOSIN BETA 4 HUMAN Protein?
The biological functionality of THYMOSIN BETA 4 HUMAN Protein will be determined in the future.
What is the amino acid sequence of THYMOSIN BETA 4 HUMAN Protein?
SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES
What applications can THYMOSIN BETA 4 HUMAN Protein be used in?
THYMOSIN BETA 4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for THYMOSIN BETA 4 HUMAN Protein?
The endotoxin level is minimal, THYMOSIN BETA 4 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant THYMOSIN BETA 4 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 THYMOSIN BETA 4 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
Thymosin beta 4Description:
Thymosin β4
Thymosin beta-4. TB500, TB-500
Product # :
HOR-275Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
Citations
More Info
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Introduction
Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.
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Synonyms
Thymosin beta-4. TB500, TB-500
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 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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Amino Acid Sequence
Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.
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Background
What is the molecular weight/Mw of THYMOSIN BETA 4 Protein?
THYMOSIN BETA 4 Protein has a total Mw of 4.96kDa.
What is the Purity of THYMOSIN BETA 4 Protein?
THYMOSIN BETA 4 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of THYMOSIN BETA 4 Protein?
The biological functionality of THYMOSIN BETA 4 Protein will be determined in the future.
What is the amino acid sequence of THYMOSIN BETA 4 Protein?
Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.
What applications can THYMOSIN BETA 4 Protein be used in?
THYMOSIN BETA 4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for THYMOSIN BETA 4 Protein?
The endotoxin level is minimal, THYMOSIN BETA 4 Protein was purified using conventional chromatography techniques.
Who supplies THYMOSIN BETA 4 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 THYMOSIN BETA 4?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
PTMA HumanDescription:
Prothymosin Alpha Human Recombinant
Prothymosin alpha, TMSA, PTMA, Prothymosin alpha, N-terminally processed, Thymosin alpha-1.
Product # :
PRO-1694Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PTMA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-110) and having a molecular mass of 14.5 kDa.PTMA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PTMA solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prothymosin alpha (PTMA) is a part of the pro/parathymosin family. PTMA mediates immune function by conferring resistance to some opportunistic infections.
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Synonyms
Prothymosin alpha, TMSA, PTMA, Prothymosin alpha, N-terminally processed,
Thymosin alpha-1. -
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 MGSMSDAAVD TSSEITTKDL KEKKEVVEEA ENGRDAPANG NANEENGEQE ADNEVDEEEE EGGEEEEEEE EGDGEEEDGD EDEEAESATG KRAAEDDEDD DVDTKKQKTD EDD.
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 :
ThymalinDescription:
Thymulin
Product # :
HOR-047Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymulin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 858 Dalton and a Molecular formula of C33H54N12O15.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymulin 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 Thymulin 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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Amino Acid Sequence
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.
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Background
Thymulin, a nonapeptide hormone, is produced primarily by the thymus gland and has been recognized for its pivotal role in the immune system. It plays a significant role in the maturation and differentiation of T lymphocytes, which are crucial for immune function. Beyond its immune-related functions, research has increasingly unveiled the diverse physiological roles of thymulin. This study aims to comprehensively investigate thymulin, shedding light on its immunological functions and exploring its potential applications in various aspects of health and medicine.
The primary objective of this research is to elucidate the mechanisms underlying thymulin's role in immune regulation. In vitro and in vivo experiments will be conducted to explore thymulin's interactions with immune cells, its impact on T cell development and function, and its potential modulation of immune responses. Understanding these mechanisms is fundamental for harnessing thymulin's immunomodulatory properties.
The second objective is to assess the clinical relevance of thymulin in immune-related disorders. Clinical trials and studies involving individuals with autoimmune diseases, immunodeficiencies, and age-related immune decline will be conducted to evaluate the potential therapeutic applications of thymulin. These investigations may offer insights into the use of thymulin as an immunomodulatory agent in various clinical settings.
The third objective is to explore the broader implications of thymulin in health and medicine. Research will investigate its potential roles in areas beyond immunology, such as neuroprotection, wound healing, and tissue regeneration. Understanding the multifaceted properties of thymulin may open new avenues for therapeutic interventions in various medical specialties.
By delving into the diverse functions of thymulin, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may have implications for the development of innovative approaches in immunology and healthcare, ultimately benefiting patients affected by immune-related disorders and other medical conditions.
What is the molecular weight/Mw of THYMALIN Protein?
THYMALIN Protein has a total Mw of 0.85kDa.
What is the Purity of THYMALIN Protein?
THYMALIN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of THYMALIN Protein?
The biological functionality of THYMALIN Protein will be determined in the future.
What is the amino acid sequence of THYMALIN Protein?
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.
What applications can THYMALIN Protein be used in?
THYMALIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for THYMALIN Protein?
The endotoxin level is minimal, THYMALIN 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 :
ThymopentinDescription:
Thymopentin
Product # :
HOR-241Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymopentin has a molecular formula of C30H49N9O9, Arg-Lys-Asp-Val-Tyr-OH having an Mw of 679.8 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
What is the molecular weight/Mw of THYMOPENTIN Protein? THYMOPENTIN Protein has a total Mw of 0.67kDa. What is the Purity of THYMOPENTIN Protein? THYMOPENTIN Protein is >99% pure as determined by SDS-PAGE. What is the Biological Activity of THYMOPENTIN Protein? The biological functionality of THYMOPENTIN Protein will be determined in the future. What applications can THYMOPENTIN Protein be used in? THYMOPENTIN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for THYMOPENTIN Protein? The endotoxin level is minimal, THYMOPENTIN Protein was purified using conventional chromatography techniques.Citations
More Info
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Introduction
Thymopentin, also known as TP-5, is a synthetic pentapeptide which is the active site of the naturally occurring hormone thymopoietin with immunomodulating properties (corresponding to the amino acids 32-36 of thymopoietin). Thymopentin enhances the production of thymic T cells and may help restore immunocompetence in immunosuppressed subjects. This agent also augments the effects of ionizing radiation by arresting cancer cells in the G2/M phase of the cell cycle.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymopentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TP-5 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 Thymopentin in sterile 18MΩ-cm H2O not less than 100 µg/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 :
PTMS HumanDescription:
Prothymosin Human Recombinant
ParaT, parathymosin.
Product # :
PRO-1735Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PTMS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-102aa) and having a molecular mass of 13.9kDa.PTMS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTMS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Parathymosin, also known as PTMS is a member of the pro/parathymosin family. PTMS may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to particular opportunistic infections. Among the diseases associated with PTMS are hepatitis b, and alzheimer's disease.
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Synonyms
ParaT, parathymosin.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEKSVE AAAELSAKDL KEKKEKVEEK ASRKERKKEV VEEEENGAEE EEEETAEDGE EEDEGEEEDE EEEEEDDEGP ALKRAAEEED EADPKRQKTE NGASA
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 :
CCL25 Human, HisDescription:
Thymus Expressed Chemokine (CCL25) Human Recombinant, His Tag
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Product # :
CHM-032Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TECK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (24-150 a.a.) and having a molecular mass of 16.8kDa.TECK is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TECK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils. -
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
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Physical Appearance
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 MGSHMQGVFE DCCLAYHYPI GWAVLRRAWT YRIQEVSGSC NLPAAIFYLP KRHRKVCGNP KSREVQRAMK LLDARNKVFA KLHHNTQTFQ AGPHAVKKLS SGNSKLSSSK FSNPISSSKR NVSLLISANS GL.
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Background
What is the molecular weight/Mw of CCL25 HUMAN, HIS Protein?
CCL25 HUMAN, HIS Protein has a total Mw of 16.8kDa.
What is the source or expression system of CCL25 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL25 HUMAN, HIS Protein?
CCL25 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL25 HUMAN, HIS Protein?
The biological functionality of CCL25 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL25 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMQGVFE DCCLAYHYPI GWAVLRRAWT YRIQEVSGSC NLPAAIFYLP KRHRKVCGNP KSREVQRAMK LLDARNKVFA KLHHNTQTFQ AGPHAVKKLS SGNSKLSSSK FSNPISSSKR NVSLLISANS GL.
What applications can CCL25 HUMAN, HIS Protein be used in?
CCL25 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL25 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL25 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL25 HUMAN, HIS 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 CCL25 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
CCL25 HumanDescription:
Thymus Expressed Chemokine Human Recombinant (CCL25)
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Product # :
CHM-364Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
TECK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The TECK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.Citations
More Info
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Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils. -
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TECK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TECK 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 TECK 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
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.
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Background
What is the molecular weight/Mw of CCL25 HUMAN Protein?
CCL25 HUMAN Protein has a total Mw of 14.2kDa.
What is the source or expression system of CCL25 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL25 HUMAN Protein?
CCL25 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL25 HUMAN Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL25 HUMAN Protein?
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.
What applications can CCL25 HUMAN Protein be used in?
CCL25 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL25 HUMAN Protein?
The endotoxin level is minimal, CCL25 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL25 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 CCL25 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
TSLP HumanDescription:
Thymic Stromal Lymphopoietin Human Recombinant
Thymic Stromal Lymphopoietin, TSLP.
Product # :
CYT-572Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TSLP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 15 kDa.The TSLP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated solution (1mg/ml) contains 130mM NaCl, and 20mM sodium phosphate, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 is determined by the ability to induce proliferation of human Interleukin-7 receptor alpha & human TSLP Receptor co-transfected with mouse BaF3 cells which was found to be less than 0.3ng/ml.Citations
More Info
-
Introduction
TSLP protein is a hemopoietic cytokine which signals throughout a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor & the Interleukin-7 receptor alpha chain. TSLP impacts myeloid cells thus induces the discharge of T cell-attracting chemokines from monocytes & increases the growth of CD11c(+) dendritic cells. TSLP is mainly expressed in the heart, liver and prostate. TSLP is related in its biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the Interleukin-7 receptor alpha chain & the TSLPR. Similar to IL-7, TSLP enhances phosphorylation of STAT3 and STAT5, though uses kinases excluding JAKs for its activation. TSLP induces the release of T cell-attracting chemokines such asTARC & MDC from monocytes & triggers CD11c(+) dendritic cells. TSLP activated dendritic cells primes naive T cells to manufacture pro-allergic cytokines such as Iinterleukin-4, Interleukin-5, Interleukin-13 and TNF-alpha whereas down-regulating Interleukin-10 and IFN-gamma play a role in the initiation of allergic inflammation.
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Synonyms
Thymic Stromal Lymphopoietin, TSLP.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TSLP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSLP 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 TSLP 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
MYDFTNCDFE KIKAAYLSTI SKDLITYMSG TKSTEFNNTV SCSNRPHCLT EIQSLTFNPT AGCASLAKEM FAMKTKAALA IWCPGYSETQ INATQAMKKR RKRKVTTNKC LEQVSQLQGL WRRFNRPLLK QQ.
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 :
TYMS HumanDescription:
Thymidylate Synthetase Human Recombinant
TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.
Product # :
ENZ-470Price :
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Shipped with Ice Packs
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Description
Thymidylate synthase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 333 amino acids (1-313 a.a.) and having a molecular mass of 37.8 kDa. The Thymidylate synthase fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Thymidylate synthase solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Thymidylate synthase catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5,10-methylenetetrahydrofolate as a cofactor which maintains the dTMP (thymidine-5-prime monophosphate) pool vital for DNA replication and repair. Thymidylate synthase plays an important role as a cancer chemotherapeutic agent. Thymidylate synthase is the primary site of action for 5-fluoro-2-prime-deoxyuridine and several folate analogs.
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Synonyms
TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPVAGSELPR RPLPPAAQER DAEPRPPHGE LQYLGQIQHI LRCGVRKDDR TGTGTLSVFG MQARYSLRDE FPLLTTKRVF WKGVLEELLW FIKGSTNAKE LSSKGVKIWD ANGSRDFLDS LGFSTREEGD LGPVYGFQWR HFGAEYRDME SDYSGQGVDQ LQRVIDTIKT NPDDRRIIMC AWNPRDLPLM ALPPCHALCQ FYVVNSELSC QLYQRSGDMG LGVPFNIASY ALLTYMIAHI TGLKPGDFIH TLGDAHIYLN HIEPLKIQLQ REPRPFPKLR ILRKVEKIDD FKAEDFQIEG YNPHPTIKME MAV.
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 :
TSLP Human, HisDescription:
Thymic Stromal Lymphopoietin Human Recombinant, His Tag
Thymic Stromal Lymphopoietin, TSLP.
Product # :
CYT-836Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TSLP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Tyr29-Gln159) containing 141 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 16.2kDa.
Source
Escherichia Coli.
Formulation
TSLP was filtered (0.4µm) and lyophilized in phosphate buffered saline.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TSLP protein is a hemopoietic cytokine which signals throughout a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor & the Interleukin-7 receptor alpha chain. TSLP impacts myeloid cells thus induces the discharge of T cell-attracting chemokines from monocytes & increases the growth of CD11c(+) dendritic cells. TSLP is mainly expressed in the heart, liver and prostate. TSLP is related in its biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the Interleukin-7 receptor alpha chain & the TSLPR. Similar to IL-7, TSLP enhances phosphorylation of STAT3 and STAT5, though uses kinases excluding JAKs for its activation. TSLP induces the release of T cell-attracting chemokines such asTARC & MDC from monocytes & triggers CD11c(+) dendritic cells. TSLP activated dendritic cells primes naive T cells to manufacture pro-allergic cytokines such as Iinterleukin-4, Interleukin-5, Interleukin-13 and TNF-alpha whereas down-regulating Interleukin-10 and IFN-gamma play a role in the initiation of allergic inflammation.
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Synonyms
Thymic Stromal Lymphopoietin, TSLP.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
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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. TSLP is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASYDFTNCDFEK IKAAYLSTIS KDLITYMSGT KSTEFNNTVS CSNRPHCLTE IQSLTFNPTA GCASLAKEMF AMKTKAALAI WCPGYSETQI NATQAMKKRR KRKVTTNKCL EQVSQLQGLW RRFNRPLLKQ Q.
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 :
Thyroglobulin HumanDescription:
Thyroglobulin Human Recombinant
Thyroglobulin, TGN, AITD3, TG.
Product # :
PRO-2803Price :
Quantity :
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Shipped at Room temp
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Description
Thyroglobulin Human produced in a mammalian cell line is a single, non-glycosylated polypeptide chain (1-2768 a.a.) and having a molecular mass of 304640 Dalton. Thyroglobulin Human is fused with GlyAlaProGly4SerHis10-tag at C-terminal and purified by proprietary chromatographic techniques.
Source
Mammalian cell line.
Formulation
Thyroglobulin was lyophilized from PBS, pH 7.4 and 5.4 % sucrose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Synonyms
Thyroglobulin, TGN, AITD3, TG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thyroglobulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thyroglobulin 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 Thyroglobulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Thyroglobulin, a glycoprotein primarily produced in the thyroid gland, stands at the center of thyroid hormone synthesis. Comprising a series of tyrosine residues, thyroglobulin serves as the scaffold upon which thyroid hormones are assembled. Beyond its pivotal role in thyroid physiology, thyroglobulin has garnered significant attention in the realm of thyroid disease diagnostics, offering valuable insights into thyroid function and disorders. This research delves into the intricacies of thyroglobulin human recombinant protein, exploring its biochemical properties, physiological significance, and its crucial applications in both clinical and research settings.
Structural Complexity of Thyroglobulin:
Thyroglobulin is a large, dimeric protein boasting an intricate structure composed of multiple domains. Within its structure lie tyrosine residues crucial for iodine incorporation, a process fundamental for thyroid hormone synthesis. Its size and complexity reflect the sophistication of thyroid hormone production, as thyroglobulin acts as a reservoir for thyroid hormones within the thyroid follicles.
Physiological Significance in Thyroid Function:
Thyroglobulin plays a central role in the synthesis of triiodothyronine (T3) and thyroxine (T4), the thyroid hormones essential for regulating metabolism and overall body homeostasis. During thyroid hormone synthesis, thyroglobulin is secreted into the follicular lumen, where it undergoes iodination and subsequent proteolysis, releasing T3 and T4. This process highlights the indispensable nature of thyroglobulin in thyroid hormone production, making it a key biomolecule in thyroid physiology.
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 :
GPHA2 HumanDescription:
Thyrostimulin Alpha Human Recombinant
GPA2, GPHA2, ZSIG51, Glycoprotein hormone alpha-2, MGC126572.
Product # :
HOR-258Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GPHA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a total molecular mass of 13.28 kDa. The Thyrostimulin contains His tag which consists of 14 additional amino acids.The amino acid sequence of the recombinant human Thyrostimulin beta subunit is 100% homologous to the amino acid sequence of the human Thyrostimulin beta subunit without signal sequence. (N-terminal 24AA).Thyrostimulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GPHA2 filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH 4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
Human thyrostimulin ranks among the glycoprotein hormone family. These hormones consist of two subunits, the common alpha- and specific beta-subunits, which associate noncovalently to form a heterodimer. The alpha-subunit combines with four distinct beta-subunits giving rise to four biologically active hormones in human: FSH, LH, TSH, and CG. FSH, LH, and TSH, mainly expressed in the anterior pituitary, are essential for coordinated endocrine regulation in the hypothalamus- pituitary axis and show to activate specific G protein–coupled receptors in the thyroid (TSH receptor) and gonads (LH and FSH receptors), respectively.
The heterodimeric glycoprotein hormones have only been identified in vertebrates and are highly conserved in organisms from primitive rayfin fish (Chondrostei) to human in both primary sequences and functional characteristics.
Corticotroph-derived glycoprotein hormone (CGH), also referred to as thyrostimulin, is a noncovalent heterodimer of glycoprotein hormone alpha 2 (GPHA2) and glycoprotein hormone beta 5 (GPHB5).
Recombinant A2/B5 heterodimeric glycoproteins activates human TSH receptors, but not LH and FSH receptors, and shows high affinity to TSH receptors in a radioligand receptor assay. The heterodimer also stimulates cAMP production and thymidine incorporation by cultured thyroid cells and increases serum thyroxine levels in TSH-suppressed rats in vivo. This new heterodimeric glycoprotein hormone was named as thyrostimulin based on its thyroid-stimulating activity. The expression of thyrostimulin in the anterior pituitary known to express TSH receptors suggested a paracrine mechanism. -
Synonyms
GPA2, GPHA2, ZSIG51, Glycoprotein hormone alpha-2, MGC126572.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Thyrostimulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GPHA2 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 add 0.1M Acetate buffer pH4 to prepare a working stock solution of ~ 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MRGSHHHHHH GMAS QEAVIPG CHLHPFNVTV RSDRQGTCQG SHVAQACVGH CESSAFPSRY SVLVASGYRH NITSVSQCCT ISGLKKVKVQ LQCVGSRREE LEIFTARACQCDMCRLSRY.
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 :
TYMS AntibodyDescription:
Thymidylate Synthetase, Mouse Anti Human
TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.
Product # :
ANT-002Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
-
Introduction
Thymidylate synthase catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5,10-methylenetetrahydrofolate as a cofactor which maintains the dTMP (thymidine-5-prime monophosphate) pool vital for DNA replication and repair. Thymidylate synthase plays an important role as a cancer chemotherapeutic agent. Thymidylate synthase is the primary site of action for 5-fluorouracil, 5-fluoro-2-prime-deoxyuridine, and several folate analogs.
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Synonyms
TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.
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Immunogen
Anti-human TYMS mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human TYMS amino acids 1-313 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
PAT1S5AT.
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Applications
TYMS 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 and Immunofluorescence analysis is 1:500 ~ 1000. Recommended starting dilution is 1:500.
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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
TYMS antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
THYN1 HumanDescription:
Thymocyte Nuclear Protein 1 Human Recombinant
MY105, THY28, Thymocyte Protein Thy28, Cyte Nuclear Protein 1.
Product # :
PRO-270Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
THYN1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-225a.a.) and having a molecular mass of 27.8kDa.THYN1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The THYN1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 100mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
THYN1, is greatly conserved among vertebrates and plant types. TYHN1 takes part in the induction of apoptosis. THYN1 in the thymocytes was primarily found in the nucleus, as shown in lymphoma cells, demonstrating that the THYN1 is localized in the nucleus, regardless of the cyclic or resting stage of the cell cycle.
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Synonyms
MY105, THY28, Thymocyte Protein Thy28, Cyte Nuclear Protein 1.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSRPRKRLAG TSGSDKGLSG KRTKTENSGE ALAKVEDSNP QKTSATKNCL KNLSSHWLMK SEPESRLEKG VDVKFSIEDL KAQPKQTTCW DGVRNYQARN FLRAMKLGEE AFFYHSNCKE PGIAGLMKIV KEAYPDHTQF EKNNPHYDPS SKEDNPKWSM VDVQFVRMMK RFIPLAELKS YHQAHKATGG PLKNMVLFTR QRLSIQPLTQ EEFDFVLSLE EKEPS
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 :
TPM1 HumanDescription:
Tropomyosin-1 Human Recombinant
Tropomyosin alpha-1 chain, Tropomyosin-1, Alpha-tropomyosin, TPM1, C15orf13, TMSA, CMD1Y, HTM-alpha.
Product # :
PRO-469Price :
Quantity :
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Shipped with Ice Packs
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Description
TPM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 304 amino acids (1-284 a.a.) and having a total molecular mass of 35kDa (Molecular weight on SDS-PAGE will appear higher). TPM1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TPM1 0.5mg/ml protein solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TPM1 is a member of the tropomyosin family which consists of a number of extremely conserved, extensively distributed 35-45 kDa actin-binding proteins that are involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin-1 is composed of 2 alpha-helical chains arranged as a coiled-coil. TPM1 is polymerized end to end alongside the two grooves of actin filaments and provides stability to the filaments. TPM1 binds to actin filaments in muscle and non-muscle cells. TPM1 also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In non-muscle cells TPM1 is implicated in stabilizing cytoskeleton actin filaments. Smooth muscle contraction is controlled by interaction with caldesmon.
Alternatively spliced transcript variants encoding a range of isoforms have been described in smooth muscle and non-muscle cells. TPM1 Isoform 1 is expressed in adult and fetal skeletal muscle and cardiac tissues, with higher expression levels in the cardiac tissues, whereas Isoform 10 is expressed in adult and fetal cardiac tissues, but not in skeletal muscle.
Mutations in the TPM1 gene are linked to type 3 familial hypertrophic cardiomyopathy. -
Synonyms
Tropomyosin alpha-1 chain, Tropomyosin-1, Alpha-tropomyosin, TPM1, C15orf13, TMSA, CMD1Y, HTM-alpha.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY SEALKDAQEK
LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR
KYEEVARKLV IIESDLERAE ERAELSEGQV RQLEEQLRIM DQTLKALMAA EDKYSQKEDR YEEEIKVLSD KLKEAETRAE FAERSVTKLE
KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSM.
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 :
TPM3 HumanDescription:
Tropomyosin-3 Human Recombinant
Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.
Product # :
PRO-1020Price :
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Description
TPM3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a.) and having a molecular mass of 31.6kDa. TPM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TPM3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 0.1M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Tropomyosin alpha-3 chain (TPM3) belongs to the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins which polymerize end-to-end along the major groove in most actin filaments. Tropomyosins give stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, tropomyosins regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.
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Synonyms
Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAGITT IEAVKRKIQV LQQQADDAEE RAERLQREVE GERRAREQAE AEVASLNRRI QLVEEELDRA QERLATALQK LEEAEKAADE SERGMKVIEN RALKDEEKME LQEIQLKEAK HIAEEADRKY EEVARKLVII EGDLERTEER AELAESRCRE MDEQIRLMDQ NLKCLSAAEE KYSQKEDKYE EEIKILTDKL KEAETRAEFA ERSVAKLEKT IDDLEDKLKC TKEEHLCTQR MLDQTLLDLN EM.
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 :
TPM4 HumanDescription:
Tropomyosin-4 Human Recombinant
Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4.
Product # :
PRO-187Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TPM4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 268 amino acids (1-248 a.a.) and having a molecular mass of 30.7kDa.TPM4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TPM4 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TPM4 is a member of the tropomyosin family. Tropomyosins exist in practically all eukaryotic cells (both muscle and nonmuscle), where they bind actin filaments and function to modulate actin-myosin interaction and stabilize actin filament structure. TPM4 binds to actin filaments in muscle and nonmuscle cells and plays a central role, in connection with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction.
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Synonyms
Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4.
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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 MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI.
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 :
TSLPR HumanDescription:
Thymic Stromal Lymphopoietin Receptor Human Recombinant
CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.
Product # :
CYT-742Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TSLPR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (23-231 a.a.) and having a molecular mass of 26.6kDa.TSLPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TSLPR protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Thymic Stromal Lymphopoietin Receptor (TSLPR) is a member of the type I cytokine receptor family. TSLPR alongside the interleukin 7 receptor (IL7R) activate STAT3, STAT5, and JAK2 pathways, which is regulated processes such as cell proliferation and development of the hematopoietic system. Two transcript variants encoding dissimilar isoforms have been found for this gene. TSLPR is expressed in heart, skeletal muscle, kidney and adult and fetal liver.
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Synonyms
CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.
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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 MGSQGGAAEG VQIQIIYFNL ETVQVTWNAS KYSRTNLTFH YRFNGDEAYD QCTNYLLQEG HTSGCLLDAE QRDDILYFSI RNGTHPVFTA SRWMVYYLKP SSPKHVRFSW HQDAVTVTCS DLSYGDLLYE VQYRSPFDTE WQSKQENTCN VTIEGLDAEK CYSFWVRVKA MEDVYGPDTY PSDWSEVTCW QRGEIRDACA ETPTPPKPKL SK.
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 :
DTYMK HumanDescription:
Deoxythymidylate Kinase Human Recombinant
Deoxythymidylate Kinase (Thymidylate Kinase), DTMP Kinase, CDC8, TMPK, TYMK, Thymidylate (DTMP) Kinase, EC 2.7.4.9, PP3731, Thymidylate kinase.
Product # :
PKA-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DTYMK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212 a.a) and having a molecular mass of 26kDa. DTYMK is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
DTYMK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Thymidylate kinase (DTYMK) is involved in pyrimidine metabolism. Specifically, DTYMK catalyzes the ATP-dependent conversion of dTMP (deoxythymidine monophosphate) to dTDP (deoxythymidine diphosphate), which then acts as one of the 4 nucleotides in DNA. Through its role in the catalytic creation of dTDP, DTYMK has an imperative role in the pathway of DNA synthesis and is assumed to be involved in cell cycle progression and cell growth.
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Synonyms
Deoxythymidylate Kinase (Thymidylate Kinase), DTMP Kinase, CDC8, TMPK, TYMK, Thymidylate (DTMP) Kinase, EC 2.7.4.9, PP3731, Thymidylate kinase.
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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 MAARRGALIV LEGVDRAGKS TQSRKLVEAL CAAGHRAELL RFPERSTEIG KLLSSYLQKK SDVEDHSVHL LFSANRWEQV PLIKEKLSQG VTLVVDRYAF SGVAFTGAKE NFSLDWCKQP DVGLPKPDLV LFLQLQLADA AKRGAFGHER YENGAFQERA LRCFHQLMKD TTLNWKMVDA SKSIEAVHED IRVLSEDAIR TATEKPLGEL WK.
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 :
Hepsin HumanDescription:
Hepsin Human Recombinant
HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.
Product # :
PRO-2846Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Hepsin Human Recombinant produced in Cho cells is a covalently-linked heterodimer having a total molecular mass of 43.0kDa. Hepsin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
CHO cells.
Formulation
The Hepsin protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity is >20,000 pmol/min/μg and was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC).Citations
More Info
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Synonyms
HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Hepsin Active although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hepsin Active should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles. -
Solubility
It is recommended to reconstitute the lyophilized Hepsin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR.
Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H.
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Background
Hepsin is a type II transmembrane serine protease expressed primarily on epithelial cells, it takes part in extracellular proteolysis by activating precursor proteins such as pro-HGF and contributes to tissue remodeling, cell signaling, and normal epithelial function. Recombinant Hepsin is used to study prostate cancer, extracellular matrix remodelling, protease signalling pathways, tumor invasion, metastasis, HGF/MET signaling, and for screening inhibitors that target serine proteases
What is the molecular weight / Mw of Hepsin Protein?
Hepsin Protein has a total Mw of 43kDa.
What is the source or expression system of Hepsin Protein?
CHO Cells
What is the Purity of Hepsin Protein?
Hepsin Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Hepsin Protein?
The enzymatic activity was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC). The specific activity is >20,000 pmol/min/μg.
What is the amino acid sequence of Hepsin Protein?
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR
Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H
What applications can Hepsin Protein be used in?
Hepsin Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for Hepsin Protein?
The endotoxin level is minimal, Hepsin Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Thyroglobulin Human, BiotinDescription:
Thyroglobulin Human, Biotinylated
Thyroglobulin, TGN, AITD3, TG.
Product # :
PRO-2563Price :
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Description
Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).
Source
Native, Isolated from human thyroid glands.
Formulation
Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease. -
Synonyms
Thyroglobulin, TGN, AITD3, TG.
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Physical Appearance
Sterile Filtered 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 IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)
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 :
TesamorelinDescription:
Tesamorelin
Product # :
HOR-062Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Tesamorelin is a synthetic single, non-glycosylated polypeptide chain containing 44 amino acids, having a molecular mass of 5135.78 Dalton and a Molecular formula of C221H366N72O67S.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tesamorelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Tesamorelin 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 Tesamorelin 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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Amino Acid Sequence
trans-3-hexenoyl-Tyr-Ala-Asp-Ala-IlePhe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-GluArg-Gly-Ala-Arg-Ala-Arg-Leu-NH2.
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Background
Tesamorelin is a growth hormone-releasing hormone (GHRH) analogue. Tesamorelin stimulates the pituitary gland to produce endogenous growth hormone, which targets visceral adipose tissue. Tesamorelin has evolved from a HIV treatment into an effective metabolic and regenerative therapy.
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.