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1000 results found for “thrombin”
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Name :
TGFBI HumanDescription:
Transforming Growth Factor Beta Induced Human Recombinant
Transforming growth factor-beta-induced protein ig-h3, Beta ig-h3, Kerato-epithelin, RGD-containing collagen-associated protein, RGD-CAP, TGFBI, BIGH3, CSD, CDB1, CDG2, CSD1, CSD2, CSD3, EBMD, LCD1, CDGG1.
Product # :
PRO-568Price :
Quantity :
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Shipped with Ice Packs
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Description
TGFBI Human Recombinant produced in e.Coli is a single, non-glycosylated, polypeptide containing 135 amino acids (502-636) and having a molecular mass of 14.5 kDa. The TGFBI recombinant Human protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TGFBI recombinant Human is formulated 20mM Tris-HCl pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Transforming Growth Factor Beta Induced protein also known as TGFBI is an extracellular matrix protein induced by transforming growth factor (TGF)-beta 1. TGFBI protein is involved in cell growth, cell differentiation, wound healing and cell adhesion. In addition, some missense mutations of TGFBI were identified in families affected with human autosomal dominant corneal dystrophies. TGFBI gene encodes for a 683 amino-acid protein containing an RGD motif and four internal repeated domains which have highly conserved sequences founded in several species (Fasciclin domain).
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Synonyms
Transforming growth factor-beta-induced protein ig-h3, Beta ig-h3, Kerato-epithelin, RGD-containing collagen-associated protein, RGD-CAP, TGFBI, BIGH3, CSD, CDB1, CDG2, CSD1, CSD2, CSD3, EBMD, LCD1, CDGG1.
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Physical Appearance
Sterile filtered liquid formulation.
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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
MGTVMDVLKG DNRFSMLVAA IQSAGLTETL NREGVYTVFA PTNEAFRALP PRERSRLLGD AKELANILKY HIGDEILVSG GIGALVRLKS LQGDKLEVSL KNNVVSVNKE PVAEPDIMAT NGVVHVITNV LQPPA.
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 :
TIAL1 HumanDescription:
TIAL1 Human Recombinant
TCBP, TIAR, TIA1 cytotoxic granule-associated RNA binding protein-like 1, TIA-1-related protein.
Product # :
PRO-2139Price :
Quantity :
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Shipped with Ice Packs
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Description
TIAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-375 a.a) and having a molecular mass of 44.0kDa.TIAL1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TIAL1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 50% glycerol, 2mM DTT and 1mM EDTA .
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TIAL1 belongs to a family of RNA-binding proteins, it has 3 RNA recognition motifs (RRMs), and binds adenine and uridine-rich elements in mRNA and pre-mRNAs of a extensive range of genes. TIAL1 regulates a variety of activities including translational control, splicing and apoptosis. TIAL1 different isoforms function differently with respect to post-transcriptional silencing.
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Synonyms
TCBP, TIAR, TIA1 cytotoxic granule-associated RNA binding protein-like 1, TIA-1-related protein.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMMEDDGQ PRTLYVGNLS RDVTEVLILQ LFSQIGPCKS CKMITEHTSN DPYCFVEFYE HRDAAAALAA MNGRKILGKE VKVNWATTPS SQKKDTSNHF HVFVGDLSPE ITTEDIKSAF APFGKISDAR VVKDMATGKS KGYGFVSFYN KLDAENAIVH MGGQWLGGRQ IRTNWATRKP PAPKSTQENN TKQLRFEDVV NQSSPKNCTV YCGGIASGLT DQLMRQTFSP FGQIMEIRVF PEKGYSFVRF STHESAAHAI VSVNGTTIEG HVVKCYWGKE SPDMTKNFQQ VDYSQWGQWS QVYGNPQQYG QYMANGWQVP PYGVYGQPWN QQGFGVDQSP SAAWMGGFGA QPPQGQAPPP VIPPPNQAGY GMASYQTQ.
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 :
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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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
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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.
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Synonyms
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
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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 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.
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Name :
TSSK6 HumanDescription:
Testis Specific Serine Kinase 6 Human Recombinant
TSSK6, Testis-Specific Serine Kinase 6, Cancer/Testis Antigen 72, SSTK, Small Serine/Threonine Kinase, CT72, TSK-6, TSSK4, Serine/Threonine Protein Kinase SSTK, Testis-Specific Serine/Threonine-Protein Kinase 6, EC 2.7.11.1, TSSK-6, Serine/Threonine-Protein Kinase SSTK, Testis-Specific Kinase 6.
Product # :
PKA-220Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TSSK6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273) and having a molecular mass of 32.7kDa.TSSK6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TSSK6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Testis-specific serine/threonine-protein kinase 6 (TSSK6) is an intronless gene, which belongs to the CAMK Ser/Thr protein kinase family. The TSSK6 protein contains one protein kinase domain. TSSK6 is highly expressed in the testis and lowly expressed in the colon, prostate, thymus, small intestine, and peripheral blood leukocytes. TSSK6 interacts with the heatshock proteins HSPA8, HSPCB, and HAPA1A; these interactions seem to be essential for TSSK6 kinase activity. TSSK6 plays a role in DNA condensation during postmeiotic chromatin remodeling. In addition, TSSK6 is required for sperm production and function.
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Synonyms
TSSK6, Testis-Specific Serine Kinase 6, Cancer/Testis Antigen 72, SSTK, Small Serine/Threonine Kinase, CT72, TSK-6, TSSK4, Serine/Threonine Protein Kinase SSTK, Testis-Specific Serine/Threonine-Protein Kinase 6, EC 2.7.11.1, TSSK-6, Serine/Threonine-Protein Kinase SSTK, Testis-Specific Kinase 6.
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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 MGSMSGDKLL SELGYKLGRT IGEGSYSKVK VATSKKYKGT VAIKVVDRRR APPDFVNKFL PRELSILRGV RHPHIVHVFE FIEVCNGKLY IVMEAAATDL LQAVQRNGRI PGVQARDLFA QIAGAVRYLH DHHLVHRDLK CENVLLSPDE RRVKLTDFGF GRQAHGYPDL STTYCGSAAY ASPEVLLGIP YDPKKYDVWS MGVVLYVMVT GCMPFDDSDI AGLPRRQKRG VLYPEGLELS ERCKALIAEL LQFSPSARPS AGQVARNCWL RAGDSG.
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 :
CHGA HumanDescription:
Chromogranin-A Human Recombinant
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-692Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (19-131 a.a) and having a molecular mass of 12.8 kDa. Chromgranin-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein contains 20mM Tris-HCl buffer pH-8, and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
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Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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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
MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVME.
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 :
TNNI3 Human, HisDescription:
Cardiac Troponin-I Human Recombinant, His Tag
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Product # :
PRO-2266Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Human TNNI3 protein produced in E.Coli is a full length protein containing a total of 260 amino acids and fused to a 6 His Tag at C-terminus, migrating as a 27kDa band on SDS-PAGE.Purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
TNNI3 protein solution in PBS and 25mM arginine.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
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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).
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
TNNI3 although stable at 4°C for 1 week, 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.
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Name :
TMOD3 HumanDescription:
Tropomodulin 3 Human Recombinant
Tropomodulin-3, Ubiquitous tropomodulin, U-Tmod, TMOD3, UTMOD.
Product # :
PRO-1165Price :
Quantity :
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Shipped with Ice Packs
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Description
TMOD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (1-352 a.a) and having a molecular mass of 42kDa.TMOD3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TMOD3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Tropomodulin 3 (TMOD3) is a member of the tropomodulin family. TMOD3 prevents the elongation and depolymerization of the actin filaments at the pointed end. Actin cytoskeleton regulation by filament capping proteins is essential to many dynamic cellular functions. TMOD3 functions as a negative regulator of cell migration; nevertheless the processes behind its cellular functions are unknown. The Tmod/TM complex influences the formation of the short actin protofilament, which sequentially outlines the geometry of the membrane skeleton.
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Synonyms
Tropomodulin-3, Ubiquitous tropomodulin, U-Tmod, TMOD3, UTMOD.
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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 MGSHMALPFR KDLEKYKDLD EDELLGNLSE TELKQLETVL DDLDPENALL PAGFRQKNQT SKSTTGPFDR EHLLSYLEKE ALEHKDREDY VPYTGEKKGK IFIPKQKPVQ TFTEEKVSLD PELEEALTSA SDTELCDLAA ILGMHNLITN TKFCNIMGSS NGVDQEHFSN VVKGEKILPV FDEPPNPTNV EESLKRTKEN DAHLVEVNLN NIKNIPIPTL KDFAKALETN THVKCFSLAA TRSNDPVATA FAEMLKVNKT LKSLNVESNF ITGVGILALI DALRDNETLA ELKIDNQRQQ LGTAVELEMA KMLEENTNIL KFGYQFTQQG PRTRAANAIT KNNDLVRKRR VEGDHQ.
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 :
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.
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.
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 :
EREG Human, HEKDescription:
Epiregulin Human Recombinant, HEK
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
Product # :
CYT-1206Price :
Quantity :
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Shipped with Ice Packs
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Description
EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
EREG protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
More Info
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Introduction
"Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."
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Synonyms
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
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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
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 32.6kDa.
What is the source or expression system of EREG Protein?
HEK293 cells.
What is the Purity of EREG Protein?
EREG Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
What is the amino acid sequence of EREG Protein?
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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 :
TNFRSF10D HumanDescription:
TRAIL Receptor-4 Human Recombinant
Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.
Product # :
CYT-1045Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFRSF10D produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 395 amino acids (56-211a.a.) and having a molecular mass of 73.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TNFRSF10D is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFRSF10D protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a neutralizing assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 10 ng/ml in the presence of 2ng/ml TRAIL.
More Info
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Introduction
TRAIL Receptor-4 Human Recombinant or TNFRSF10D, is part of the TNF-receptor superfamily. TNFRSF10D has atruncated cytoplasmic death domai , an extracellular TRAIL-binding domain and a transmembrane domain. The protein can prevent from TRAIL-mediated apoptosis on cells with TRAIL R1 and/or TRAIL R2.
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Synonyms
Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.
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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
ATIPRQDEVP QQTVAPQQQR RSLKEEECPA GSHRSEYTGA CNPCTEGVDY TIASNNLPSC LLCTVCKSGQ TNKSSCTTTR DTVCQCEKGS FQDKNSPEMC RTCRTGCPRG MVKVSNCTPR SDIKCKNESA ASSTGKTPAA EETVTTILGM LASPYHVEPK SCDKTHTCPP CPAPELLGGP
SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ
QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TTC33 HumanDescription:
Tetratricopeptide Repeat Domain 33 Human Recombinant
Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.
Product # :
PRO-1217Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TTC33 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-262) and having a molecular mass of 31.8 kDa.TTC33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TTC33 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Tetratricopeptide repeat protein 33 (TTC33) is comprised of 3 TPR repeats.
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Synonyms
Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.
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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 MGS MASFGWK RKIGEKVSKV TSQQFEAEAA DEKDVVDNDE GNWLHAIKRR KEILLEGCAE KSKQLKDEGA SLAENKRYRE AIQKWDEALQ LTPNDATLYE MKSQVLMSLH EMFPAVHAAE MAVQQNPHSW ESWQTLGRAQ LGLGEIILAI RSFQVALHIY
PMNPEIWKED LSWARTLQEQ QKVAQRIKKS EAPAEVTHFS PKSIPDYDFE SDEIVAVCAA IAEKEKTVSA NKTMVIVSAS GAIETVTEKE DGATPPDGSV FIKAR
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 :
ProInsulin HumanDescription:
ProInsulin C-Peptide Analogue Human Recombinant
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Product # :
CYT-1120Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
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Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized ProInsulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProInsulin C-Peptide Analogue 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 ProInsulin C-Peptide Analogue 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
RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.
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 :
TLR2 HumanDescription:
Toll Like Receptor 2 Human Recombinant
Toll Like Receptor 2, Toll/Interleukin-1 Receptor-Like Protein 4, Toll-Like Receptor 2, TIL4, CD282 Antigen, CD282, TLR2.
Product # :
PRO-2337Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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Description
TLR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 578 amino acids (21-588 aa) and having a molecular mass of 65.2kDa. TLR2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TLR2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TLR2 belongs to the Toll-like receptor (TLR) family that plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) which are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. TLR2 is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria and yeast via stimulation of NF-kappaB.
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Synonyms
Toll Like Receptor 2, Toll/Interleukin-1 Receptor-Like Protein 4, Toll-Like Receptor 2, TIL4, CD282 Antigen, CD282, TLR2.
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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
KEESSNQASL SCDRNGICKG SSGSLNSIPS GLTEAVKSLD LSNNRITYIS NSDLQRCVNL QALVLTSNGI NTIEEDSFSS LGSLEHLDLS YNYLSNLSSS WFKPLSSLTF LNLLGNPYKT LGETSLFSHL TKLQILRVGN MDTFTKIQRK DFAGLTFLEE LEIDASDLQS YEPKSLKSIQ NVSHLILHMK QHILLLEIFV DVTSSVECLE LRDTDLDTFH FSELSTGETN SLIKKFTFRN VKITDESLFQ VMKLLNQISG LLELEFDDCT LNGVGNFRAS DNDRVIDPGK VETLTIRRLH IPRFYLFYDL STLYSLTERV KRITVENSKV FLVPCLLSQH LKSLEYLDLS ENLMVEEYLK NSACEDAWPS LQTLILRQNH LASLEKTGET LLTLKNLTNI DISKNSFHSM PETCQWPEKM KYLNLSSTRI HSVTGCIPKT LEILDVSNNN LNLFSLNLPQ LKELYISRNK LMTLPDASLL PMLLVLKISR NAITTFSKEQ LDSFHTLKTL EAGGNNFICS CEFLSFTQEQ QALAKVLIDW PANYLCDSPS HVRGQQVQDV RLSVSECHRT LEHHHHHH
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 :
ATF HumanDescription:
Apo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Human Apo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.
Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
More Info
-
Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be <6 ppm.
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 :
TXN MouseDescription:
Thioredoxin Mouse Recombinant
TRX1, TRX2, Thioredoxin-1, Thioredoxin I, TR-I, Thioredoxin-2, Thioredoxin-1, ADF, Surface associated sulphydryl protein, TXN protein, ATL derived factor, DKFZp686B1993, MGC61975, SASP, Thioredoxin, TRDX, TRX, TRX 1, TXN.
Product # :
PRO-2607Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
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- biological activity
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Description
TXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-105 a.a.) and having a molecular mass of 14.1kDa. TXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TXN protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >60 A650/cm/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.
More Info
-
Introduction
Thioredoxin or TRX contains a single disulfide active site and serves as a general protein disulphide oxidoreductase.Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that are found in all the kingdoms of living organisms. The proteinis involved in the first unique step in DNA synthesis; It interacts with a wide range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, along with the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant.
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Synonyms
TRX1, TRX2, Thioredoxin-1, Thioredoxin I, TR-I, Thioredoxin-2, Thioredoxin-1, ADF, Surface associated sulphydryl protein, TXN protein, ATL derived factor, DKFZp686B1993, MGC61975, SASP, Thioredoxin, TRDX, TRX, TRX 1, TXN.
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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 MGSMVKLIES KEAFQEALAA AGDKLVVVDF SATWCGPCKM IKPFFHSLCD KYSNVVFLEV DVDDCQDVAA DCEVKCMPTF QFYKKGQKVG EFSGANKEKL EASITEYA.
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 :
Treponema p17 16.4kDaDescription:
Treponema pallidum p17, 16.4kDa Recombinant
Product # :
TRP-252Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Treponema p17 produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 16.4kDa and fused to a His tag at N-terminus.
Source
Escherichia Coli.
Formulation
Lyophilized from 1mg/ml in 20mM sodium carbonate pH-10.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Treponema p17 although stable at room temperature for 4 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Treponema p17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TNNI3 Human ChimericDescription:
Cardiac Troponin-I Chimeric Human Recombinant
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Product # :
PRO-2790Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
- formulation
- purity
- More Info
Description
TNNI3 Human Chimeric produced in E.Coli is a single, non-glycosylated polypeptide chain (28-110 a.a.) and having a molecular mass of 29072 Dalton.
Source
Escherichia Coli.
Formulation
TNNI3 was lyophilized in 50mM Tris-HCl, 5mM Calcium chloride, 0.7M KCl and 0.1% 2-mercaptoethanol, pH 7.5
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Cardiac Troponin-I Chimeric although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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 in buffer containing BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
Troponin I (TNNI3) is a crucial regulatory protein in cardiac muscle, playing a central role in the regulation of muscle contraction. Understanding the structure and function of TNNI3 is essential for unraveling the complexities of cardiac muscle physiology and exploring therapeutic interventions for cardiac diseases. Chimeric TNNI3 proteins, which combine segments from different isoforms or species, offer a unique opportunity to investigate the role of specific regions in TNNI3 function and to potentially develop novel therapies. This research aims to provide a comprehensive exploration of chimeric TNNI3 proteins, elucidating their functions, structural significance, and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the functional significance of chimeric TNNI3 proteins in cardiac muscle. In vitro and ex vivo experiments, utilizing engineered chimeric TNNI3 constructs and cardiac tissue models, will be conducted to investigate how these proteins influence muscle contractility, calcium sensitivity, and response to pathological conditions. Understanding these mechanisms is fundamental for deciphering the roles of specific TNNI3 regions in cardiac muscle function.
The second objective is to assess the therapeutic potential of chimeric TNNI3 proteins in cardiac diseases. Experimental studies involving animal models and cellular systems will explore the use of chimeric TNNI3 proteins as potential therapeutic agents for heart conditions. These investigations may provide valuable insights into novel treatment strategies targeting cardiac muscle function.
The third objective is to explore the broader applications of chimeric TNNI3 proteins in biotechnology and drug development. Research will investigate the use of chimeric TNNI3-expressing cells and tissues as models for studying cardiac disorders and for developing innovative approaches in regenerative medicine and pharmacology.
By delving into the functions and roles of chimeric TNNI3 proteins, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology, biotechnology, and drug development
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 Human NativeDescription:
Cardiac Troponin-I Human
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Product # :
PRO-2788Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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Description
TNNI3 Native produced in Human heart tissue is a full length protein which has an additional amino acid residues on its N terminus that are not present on the skeletal form, making this protein a promising analyte for indicating cardiac specificity.TNNI3 Native is purified by proprietary chromatographic technique.
Source
Human heart tissue.
Formulation
TNNI3 was lyophilized from 0.01M HCl.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Cardiac Troponin-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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 TNNI3 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Troponin I, encoded by the TNNI3 gene, is a critical component of the troponin complex in cardiac muscle cells. It plays a central role in the regulation of cardiac muscle contraction by modulating the interaction between actin and myosin filaments.
While extensive research has been conducted on troponin I in the context of cardiac diseases, there is a growing need to investigate native human troponin I (TNNI3) in its unmodified form to gain a deeper understanding of its functions, structural significance, and implications for heart health. This research aims to provide a comprehensive exploration of TNNI3 in its native state, shedding light on its various roles and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the physiological role of native human TNNI3 in cardiac muscle contraction. Experiments involving human cardiac tissue samples and isolated myocytes will be conducted to investigate how TNNI3 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of cardiac muscle physiology and its implications for heart health.
The second objective is to assess the clinical relevance of native TNNI3 in cardiac diseases. Clinical studies involving patients with various cardiac conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI3 as a biomarker. These investigations may provide valuable insights into the use of native TNNI3 in the early detection and management of heart diseases.
The third objective is to explore the potential applications of native TNNI3 in biomedical research and drug development. Research will investigate the use of native TNNI3-expressing cells as models for studying cardiac disorders and for developing novel therapeutic interventions targeting the troponin complex.
By delving into the functions and roles of native human TNNI3, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology and biomedical research.
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 :
Placental Lactogen HumanDescription:
Placental Lactogen Human Recombinant
Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407.
Product # :
CYT-656Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
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Description
Placental Lactogen Human Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of approximately 22.4 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Placental Lactogen Human is biologically active as evidenced by inducing proliferation of Nb2 cells.More Info
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Introduction
Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both GH and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an ins. antagonist.
Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors. -
Synonyms
Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Placental Lactogen Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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 Placental Lactogen in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
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Amino Acid Sequence
The sequence of the first 6 N-terminal amino acids was determined and was found to be Ala-Val-Gln-Thr-Val-Pro.
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Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.73 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ATF BovineDescription:
Apo Transferrin Bovine
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-511Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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- More Info
Description
Bovine Apo Transferrin is a glycoprotein of approximately 77kDa.
Source
Bovine Serum.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Bovine Transferrin is a crucial component for the cultivation of mammalian cells in- vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin are Molecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered off-white lyophilized (freeze-dried) powder.
-
Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze.
-
Solubility
It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 1gr/30ml in 20min. at 20-25C.
-
Iron Content
The Iron content was estimated by ICP-OES and was found to be less than 40 ppm.
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
More Info
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- formulation
- purity
- biological activity
- More Info
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.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 :
PTH (7-34) HumanDescription:
Parathyroid Hormone (7-34) Human Recombinant
PTH/PTHrP receptor antagonist, PTHrP analog, PTHR, MGC138426, MGC138452.
Product # :
HOR-266Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Parathyroid Hormone Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 28 amino acids and having a molecular mass of 3.4kDa. The PTH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 10,000 Units/mg.More Info
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Introduction
Polypeptide hormones secreted by the parathyroid glands, which promote release of calcium from bone to extracellular fluid by activating osteoblasts and inhibiting osteoclasts, indirectly promote increased intestinal absorption of calcium, and promote renal tubular reabsorption of calcium and increased renal excretion of phosphates. It is a major regulator of bone metabolism. Secretion of parathyroid hormone increases when the level of calcium in the extracellular fluid is low. Its action is opposed by calcitonin.
PTH (7-34), which is a PTH/PTHrP receptor antagonist, can stimulate hair growth and epidermal proliferation in mice. -
Synonyms
PTH/PTHrP receptor antagonist, PTHrP analog, PTHR, MGC138426, MGC138452.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Parathyrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH 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 PTH 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
LMHNLGKHLN SMERVEWLRK KLQDVHNF.
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 :
EGFPDescription:
Enhanced Green Fluorescent Protein Recombinant
Green fluorescent protein, GFP.
Product # :
PRO-1606Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant EGFP produced in E.coli cells is a single non-glycosylated protein containing 239 amino acid chain and having a molecular mass of 26.9kDa. EGFP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGFP was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
GFP, also known as Green Fluorescent Protein, is a protein produced by the jellyfish (Aequorea Victoria) that produces bioluminescence in the green zone of the noticeable spectrum. Green Fluorescent Protein is a useful and ubiquitous instrument for producing chimeric proteins, where it functions as a fluorescent protein tag. GFP is expressed in most known cell types and is used as a noninvasive fluorescent marker in living cells and organisms. Green Fluorescent Protein permits a broad range of applications where it has functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions. Enhanced GFP (eGFP) has F64L and S65T mutations, which make GFP show increased fluorescence and fold more efficiently under 370.
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Synonyms
Green fluorescent protein, GFP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGFP although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution EGFP should be stored at 40C between 2-7 days and for future use below -180C.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 EGFP in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH KLEYNYNSHN VYIMADKQKN GIKVNFKIRH NIEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMV LLEFVTAAGI TLGMDELYK
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 :
T.Vaginalis P65 AntibodyDescription:
Polyclonal Rabbit Anti Trichomonas Vaginalis P65 Antibody
Product # :
ANT-494Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- formulation
- purity
- More Info
Description
The polyclonal antibody to Trichomonas vaginalis was collected from the rabbit igG and immunized with recombinant T. Vaginalis P65.
Formulation
50mM mg glycine, pH8.0.
Purity
Pure Rabbit IgG.
More Info
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Introduction
Trichomonas vaginalis, an anaerobic, flagellated protozoan parasite, is most dominant protozoan causing sexual transmitted disease. T. vaginalis induced vaginal tract infection occurs as multiple steps involving interactions between host macromolecules and protozoan virulent factor. Adhension protein P65 of T. vaginalis has a vital part in assisting the penetration into vaginal tract surface.
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Physical Appearance
Sterile Filtered clear 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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Purification Method
Purified by affinity chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.