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1000 results found for “tropomyosin”
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Name :
THBS1 HumanDescription:
Thrombospondin-1 Human Recombinant
Thrombospondin-1, THBS1, TSP, TSP1, THBS, THBS-1.
Product # :
PRO-288Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human THBS1 is glycosylated with N-linked sugars and produced using baculovirus vectors in insect cells. Recombinant Human THBS1 is Reactive with A4.1 anti-TSP mAb and its Mw is 140,000 Dalton.
Source
Baculovirus Insect Cells.
Formulation
The sterile protein solution contains 20mM Sodium phosphate, pH 6.0 and 300mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Thrombospondin-1 (TSP1) is a member of the Thrombospondin family and is encoded by the gene THBS1 which is a subunit of a disulfide-linked homotrimeric protein. Thrombospondin-1 is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Thrombospondin-1 can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1. TSP1 has been shown to play roles in platelet aggregation, angiogenesis, and tumorigenesis. TSP1 has been shown to be a natural inhibitor of neovascularization and tumorigenesis in healthy tissue. TSP1 interacts with no less than 12 cell adhesion receptors, including CD36, av integrins, b1 integrins, syndecan, and integrin-associated protein (IAP or CD47). It also interacts with various proteases involved in angiogenesis, including plasminogen, matrix metalloproteinase, thrombin, cathepsin, and elastase. Positive and negative modulation of endothelial cell adhesion, motility, and growth are attributed to TSP1. Recently, thrombospondin-1 was found to bind to the reelin receptors, ApoER2 and VLDLR, in so doing affecting neuronal migration in the rostral migratory stream.
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Synonyms
Thrombospondin-1, THBS1, TSP, TSP1, THBS, THBS-1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Recombinant Human TSP should be stored between 2°C- 8°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
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 :
TRAPPC2L HumanDescription:
Trafficking Protein Particle Complex 2-Like Human Recombinant
Trafficking protein particle complex subunit 2-like protein, TRAPPC2L.
Product # :
PRO-1543Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TRAPPC2L Human Recombinant produced in E. coli is a single polypeptide chain containing 162 amino acids (1-139) and having a molecular mass of 18.4kDa. TRAPPC2L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TRAPPC2L solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Trafficking Protein Particle Complex 2-Like (TRAPPC2L) takes part in vesicular transport from endoplasmic reticulum to Golgi. TRAPPC2L is a part of the TRAPP small subunits family and is expressed in various organs like testis, liver, bladder, lung, spleen and brain.
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Synonyms
Trafficking protein particle complex subunit 2-like protein, TRAPPC2L.
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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 MGSMAVCIAV IAKENYPLYI RSTPTENELK FHYMVHTSLD VVDEKISAMG KALVDQRELY LGLLYPTEDY KVYGYVTNSK VKFVMVVDSS NTALRDNEIR SMFRKLHNSY TDVMCNPFYN PGDRIQSRAF DNMVTSMMIQ VC.
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 :
TRIAP1 HumanDescription:
TP53 Regulated Inhibitor Of Apoptosis 1 Human Recombinant
TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.
Product # :
PRO-1771Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TRIAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 99 amino acids (1-76 a.a) and having a molecular mass of 11.2kDa.TRIAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TRIAP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TRIAP1 has a p53-binding site in its second exon. TRIAP1 expression is reduced by small interfering RNA enhanced apoptosis, while overexpression of TRIAP1 protects cells from apoptosis triggered by DNA damage. TRIAP1 is highly induced when cells have low levels of genotoxic stresses, but not when DNA damage is severe. TRIAP1 is able to control apoptotic pathways by interacting with Hsp70 which inhibits activity of apoptosis protease activating factor-1.
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Synonyms
TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNSVGEA CTDMKREYDQ CFNRWFAEKF LKGDSSGDPC TDLFKRYQQC VQKAIKEKEI PIEGLEFMGH GKEKPENSS
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 :
PTHrP N15 HumanDescription:
Parathyroid Hormone Related Protein N15 Labeled Human Recombinant
Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.
Product # :
HOR-005Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PTHrP N15 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids, having an MW of 10033 Da labeled by the stable isotope N15.The PTHrP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PthRp N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS,
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
PTHrP is a powerful and discriminating agonist of PTH2R which takes part in adenyl cyclase activation and intracellular calcium levels elevation. PTHrP encourages protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. Additionally, PTHrP inhibits cell proliferation through its contribution to PTH2R activation, activates nociceptors and nociceptive circuits and acts as a neuropeptide in spermatogenesis.
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Synonyms
Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PTHrP N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTHrP N15 should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
AVSEHQLLHD KGKSIQDLRR RFFLHHLIAE IHTAEIRATS EVSPNSKPSP NTKNHPVRFG SDDEGRYLTQ ETNKVETYKE QPLKTP.
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 :
Vimentin AntibodyDescription:
Vimentin, Mouse Anti Human Antibody
Product # :
ANT-245Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
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Introduction
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines.
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Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
Purified Human Vimentin.
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Ig Subclass
mouse IgG1.
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Clone
hVimentin.
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Applications
Direct ELISA, Western Blot, Immuneprecipitation, immunohistochemistry.
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Cross reactivity
Vimentin antibody will recognize most mammalian Vimentin except mouse and rat.
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Titer
For intra-cellular staining, use 5-10µl/1,000,000 cells. Wash twice with PBS/Azide before adding the appropriate amount of secondary fluorescent reagent.
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Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Available Conjugates
This antibody is also available conjugated to biotin and FITC.
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Type
Mouse Anti Human Monoclonal Antibody.
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Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
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Purification Method
Ion exchange column.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Vimentin HumanDescription:
Vimentin Human Recombinant
Vimentin, Vim, FLJ36605.
Product # :
PRO-309Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vimentin Human Recombinant produced in E.coli cells is a single non-glycosylated protein containing 465 amino acids chain and having a molecular mass of 53.5kDa. The Vimentin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Vimentin was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
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
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.
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Synonyms
Vimentin, Vim, FLJ36605.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vimentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vimentin 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 Vimentin in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
STRSVSSSSY RRMFGGPGTA SRPSSSRSYV TTSTRTYSLG SALRPSTSRS LYASSPGGVY ATRSSAVRLR SSVPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED IMRLREKLQE EMLQREEAEN TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHEEE IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA ANRNNDALRQ AKQESTEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF AVEAANYQDT IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL NLRETNLDSL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE.
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 :
PTX2 MouseDescription:
Pentraxin-2 Mouse Recombinant
Serum amyloid P-component, SAP, Apcs, Sap, Ptx2.
Product # :
PRO-2598Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PTX2 Mouse Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 210 amino acids (21-224 a.a) and having a molecular mass of 24.6kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). PTX2 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293.
Formulation
PTX2 protein solution (0.25mg/ml) contains 10% glycerol in Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PTX-2 or Pentraxin-2 is a phylogenetically conserved protein, commonly moving with homopentameric blood protein or with a protein that recognizes receptors of the innate immune system. The protein’s specific binding abilities may show that PTX-2 is specially bound in sites where injury accrued, therefore helps to eliminate damaged tissue by ways that are not phlogistics.
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Synonyms
Serum amyloid P-component, SAP, Apcs, Sap, Ptx2.
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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
QTDLKRKVFV FPRESETDHV KLIPHLEKPL QNFTLCFRTY SDLSRSQSLF SYSVKGRDNE LLIYKEKVGE YSLYIGQSKV TVRGMEEYLS PVHLCTTWES SSGIVEFWVN GKPWVKKSLQ REYTVKAPPS IVLGQEQDNY GGGFQRSQSF VGEFSDLYMW DYVLTPQDIL FVYRDSPVNP NILNWQALNY EINGYVVIRP RVWDHHHHHH.
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 :
T.Vaginalis P65 AntibodyDescription:
Polyclonal Rabbit Anti Trichomonas Vaginalis P65 Antibody
Product # :
ANT-494Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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.
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Name :
TFF1 Human, HisDescription:
Trefoil Factor-1 Human Recombinant, His Tag
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
Product # :
CYT-610Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TFF-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids (25-84) which includes a 10 amino acid His Tag and having a total molecular mass of 7.9 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TFF1 His Tag protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5 and 20mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.
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Synonyms
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TFF1 His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 His Tag 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 deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS EAQTETCTVA PRERQNCGFP GVTPSQCANK GCCFDDTVRG VPWCFYPNTI DVPPEEECEF.
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 :
TRAPPC3 HumanDescription:
Trafficking Protein Particle Complex 3 Human Recombinant
Trafficking protein particle complex subunit 3, BET3, BET3 homolog, 1110058K12Rik.
Product # :
PRO-1056Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TRAPPC3 Human Recombinant produced in E. coli is a single polypeptide chain containing 200 amino acids (1-180) and having a molecular mass of 22.4kDa.TRAPPC3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TRAPPC3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TRAPPC3 is a part of the TRAPP complex that takes part in connection of transport vesicles to the cis-Golgi membrane. Additionally, TRAPPC3 is involved in vesicular transport from endoplasmic reticulum to Golgi.
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Synonyms
Trafficking protein particle complex subunit 3, BET3, BET3 homolog, 1110058K12Rik.
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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 MSRQANRGTE SKKMSSELFT LTYGALVTQL CKDYENDEDV NKQLDKMGFN IGVRLIEDFL ARSNVGRCHD FRETADVIAK VAFKMYLGIT PSITNWSPAG DEFSLILENN PLVDFVELPD NHSSLIYSNL LCGVLRGALE MVQMAVEAKF VQDTLKGDGV TEIRMRFIRR IEDNLPAGEE
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 :
VAMP5 HumanDescription:
Vesicle-associated membrane protein 5 Human Recombinant
VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.
Product # :
PRO-681Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VAMP5 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 109 amino acids (1-72 a.a.) and having a molecular mass of 12.7 kDa.VAMP5 is fused to 37 amino acids His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The VAMP5 (0.5mg/ml) protein solution contains 20mM Tris-HCl (pH 8.0), 0.2M NaCl, 5mM DTT, 0.5mM EDTA and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
VAMP5 is part of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily. VAMP5 is involved is vesicle trafficking events that are associated with myogenesis.
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Synonyms
VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAG IELERCQQQA NEVTEIMRNN FGKVLERGVK LAELQQRSDQ LLDMSSTFNK TTQNLAQKKC WENIRYRIC.
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 :
GDF15 MouseDescription:
Growth and Differentiation factor 15 Mouse Recombinant
Growth/differentiation factor 15, GDF-15.
Product # :
CYT-857Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
GDF15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (189-303 a.a) and having a molecular mass of 14.9kDa. GDF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF15 protein solution (1.0mg/ml) containing 20mM Phosphate buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
GDF15 is part of the TGF-Beta superfamily which is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
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Synonyms
Growth/differentiation factor 15, GDF-15.
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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 MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.
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Background
What is the molecular weight/Mw of GDF15 MOUSE Protein?
GDF15 MOUSE Protein has a total Mw of 14.9kDa.
What is the source or expression system of GDF15 MOUSE Protein?
Escherichia Coli.
What is the Purity of GDF15 MOUSE Protein?
GDF15 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 MOUSE Protein?
The biological functionality of GDF15 MOUSE Protein will be determined in the future.
What is the amino acid sequence of GDF15 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.
What applications can GDF15 MOUSE Protein be used in?
GDF15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF15 MOUSE Protein?
The endotoxin level is minimal, GDF15 MOUSE 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 :
Desmin ChickenDescription:
Desmin Chicken Gizzard
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
Product # :
PRO-2783Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
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- More Info
Description
Desmin Chicken having a calculated molecular mass of 53 kDa, pI-5.4.
Source
Chicken gizzard.
Formulation
Desmin was lyophilized from a 1mg/ml solution containing 10 mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
-
Synonyms
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Desmin 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
Desmin, an intermediate filament protein, plays a fundamental role in maintaining the structural integrity and function of muscle cells. While extensive research has been conducted on desmin in mammals, the study of desmin in chickens is an emerging area with considerable potential for advancing our understanding of muscle biology. Chickens are valuable model organisms for studying muscle development, growth, and regeneration due to their relatively simple muscular system and economic significance in poultry production. This research aims to provide a comprehensive exploration of desmin in chickens, shedding light on its functions and implications for muscle structure and function.
The primary objective of this research is to elucidate the role of desmin in chicken muscle structure and development. In vitro and in vivo experiments, utilizing chicken cell cultures and embryonic models, will be conducted to investigate how desmin contributes to the organization of muscle fibers, sarcomere assembly, and myofibrillogenesis. Understanding these mechanisms is fundamental for deciphering the complexities of muscle development in chickens.
The second objective is to assess the clinical and economic relevance of desmin in poultry production. Studies involving broiler chickens will be conducted to evaluate the impact of desmin mutations or variations on muscle growth, meat quality, and disease susceptibility. These investigations may provide valuable insights into potential strategies for enhancing poultry production efficiency and meat quality.
The third objective is to explore the potential applications of desmin in biotechnology and tissue engineering. Research will investigate the use of desmin-expressing chicken cells as models for studying muscle-related diseases and for developing tissue engineering approaches for muscle repair and regeneration.
By delving into the functions and roles of desmin in chickens, this research aims to expand our knowledge of muscle biology, its implications for poultry production, and its potential applications in biotechnology and regenerative medicine.
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 :
BEST1 HumanDescription:
Bestrophin 1 Human Recombinant
Bestrophin-1, TU15B, Vitelliform macular dystrophy protein 2, BEST1, VMD2, ARB, BEST, BMD, RP50, TU15B, Bestrophin-1 isoform 1, Bestrophin 1.
Product # :
PRO-1900Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
BEST1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (292-585) and having a molecular mass of 36 kDa.BEST1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BEST1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Bestrophin 1 (BEST1) is a part of the bestrophin gene family and is also forms calcium-activated chloride-ion channels in epithelial. This small gene family is characterized by proteins with a highly conserved N-terminus with 4-6 transmembrane domains. BEST1 is extremely permeable to bicarbonate.
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Synonyms
Bestrophin-1, TU15B, Vitelliform macular dystrophy protein 2, BEST1, VMD2, ARB, BEST, BMD, RP50, TU15B, Bestrophin-1 isoform 1, Bestrophin 1.
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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 MGSEQLINPF GEDDDDFETN WIVDRNLQVS LLAVDEMHQD LPRMEPDMYW NKPEPQPPYT AASAQFRRAS FMGSTFNISL NKEEMEFQPN QEDEEDAHAG IIGRFLGLQS HDHHPPRANS RTKLLWPKRE SLLHEGLPKN HKAAKQNVRG QEDNKAWKLK AVDAFKSAPL YQRPGYYSAP QTPLSPTPMF FPLEPSAPSK LHSVTGIDTK DKSLKTVSSG AKKSFELLSE SDGALMEHPE VSQVRRKTVE FNLTDMPEIP ENHLKEPLEQ SPTNIHTTLK DHMDPYWALE NRDEAHS.
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 :
TXNDC17 HumanDescription:
Thioredoxin Domain Containing 17 Human Recombinant
Thioredoxin domain containing 17, Thioredoxin-like protein 5, Protein 42-9-9, thioredoxin (Trx)-related protein 14 kDa, TRP14, TXNL5, MGC14353.
Product # :
PRO-1055Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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- More Info
Description
TXNDC17 Human Recombinant produced in E. coli is a single polypeptide chain containing 147 amino acids (1-123) and having a molecular mass of 16.5kDa.TXNDC17 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TXNDC17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM Nacl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
TXNDC17 is a disulfide reductase that takes part in several redox reactions using the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. TXNDC17 has peroxidase activity and assists to eliminate cellular hydrogen peroxide.
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Synonyms
Thioredoxin domain containing 17, Thioredoxin-like protein 5, Protein 42-9-9, thioredoxin (Trx)-related protein 14 kDa, TRP14, TXNL5, MGC14353.
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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 MGSHMARYEE VSVSGFEEFH RAVEQHNGKT IFAYFTGSKD AGGKSWCPDC VQAEPVVREG LKHISEGCVF IYCQVGEKPY WKDPNNDFRK NLKVTAVPTL LKYGTPQKLV ESECLQANLV EMLFSED
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 :
CXCL3 Mouse, HisDescription:
GRO-Gamma Mouse Recombinant (CXCL3), His Tag
C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.
Product # :
CHM-283Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
GRO-g Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (28-100 a.a.) and having a molecular mass of 10.6kDa.CXCL3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GRO-gamma protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.15M NaCl and 5mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
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Synonyms
C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.
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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 MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.
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Background
What is the molecular weight/Mw of CXCL3 MOUSE, HIS Protein?
CXCL3 MOUSE, HIS Protein has a total Mw of 10.6kDa.
What is the source or expression system of CXCL3 MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL3 MOUSE, HIS Protein?
CXCL3 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 MOUSE, HIS Protein?
The biological functionality of CXCL3 MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL3 MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.
What applications can CXCL3 MOUSE, HIS Protein be used in?
CXCL3 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 MOUSE, HIS Protein?
The endotoxin level is minimal, CXCL3 MOUSE, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Vimentin BovineDescription:
Bovine Vimentin
Vimentin, Vim, FLJ36605.
Product # :
PRO-525Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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Description
Bovine Vimentin protein produced in Bovine Lens, having a molecular weight of 57 kDa.
Source
Bovine Lens.
Formulation
The protein (1mg/ml) was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate pH 7.5, 6M urea, 2mM DTT, 1mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
-
Introduction
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.
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Synonyms
Vimentin, Vim, FLJ36605.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Bovine Vimentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BovineVimentin 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 Bovine Vimentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
After vimentin is dissolved in 6M urea buffer (see above), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Sodium Phosphate, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco''s PBS).- Hatzfeld M. and Franke W.W. (1985). J. Cell Biol. 101, 1826-1841.- Hatzfeld M. et al. (1987). J. Mol. Biol. 197, 237-255.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TROVE2 Bovine, BiotinDescription:
TROVE Domain Family Member 2 Human Recombinant, Biotinlyated
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-2561Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TROVE2 is a biotinlyated natural protein having a molecular mass of 58kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.
Source
Bovine tissues.
Formulation
TROVE2 is supplied in 20mM HEPES buffer pH-8.0, 150mM NaCl and 20% glycerol.
Purity
Greater than 83.0% as determined by SDS-PAGE.
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TNNT1 HumanDescription:
Slow Skeletal Troponin T Human Recombinant
Troponin T, slow skeletal muscle, TnTs, Slow skeletal muscle troponin T (sTnT), TNNT1, TNT.
Product # :
PRO-2791Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNNT1 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 278 a.a and having a molecular mass of 32948 Dalton.
Source
Escherichia Coli.
Formulation
TNNT1 was lyophilized in 0.01M HCl, pH 2.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Synonyms
Troponin T, slow skeletal muscle, TnTs, Slow skeletal muscle troponin T (sTnT), TNNT1, TNT.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Slow Skeletal Troponin T although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNT1 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 TNNT1 in buffer containing 0.01M HCl, pH 2.0 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
The Troponin T1 Slow Skeletal Type (TNNT1) human recombinant protein has emerged as a focal point in biomedical research, offering a key to unraveling the complexities of muscle contraction and its implications in neuromuscular disorders. TNNT1 is a critical component of the troponin complex, which regulates striated muscle contraction by controlling the interaction between actin and myosin. The TNNT1 human recombinant, synthesized through advanced biotechnological techniques, provides a valuable tool to explore the intricate molecular characteristics and functional roles of this essential protein.
Understanding the molecular characteristics of TNNT1 is fundamental to comprehending its role in muscle physiology and pathology. TNNT1, a slow skeletal muscle isoform, possesses unique structural features that enable its binding to tropomyosin, a key regulator of muscle contraction. The interactions between TNNT1, tropomyosin, and other troponin subunits are central to the fine-tuned regulation of muscle contraction.
TNNT1 is primarily expressed in slow-twitch skeletal muscles, which are responsible for sustained, endurance-type activities. The functional significance of TNNT1 lies in its role in modulating muscle contraction kinetics, allowing for prolonged muscle activity without fatigue. Moreover, TNNT1 mutations have been associated with congenital myopathies and neuromuscular disorders, emphasizing its crucial role in muscle health.
The TNNT1 human recombinant has promising implications for both research and potential therapeutic applications. Researchers can utilize this recombinant protein to investigate the structural and functional properties of TNNT1, shedding light on its interactions with other muscle proteins and its role in muscle diseases. Additionally, TNNT1-based therapies may hold the key to addressing neuromuscular disorders, providing hope for improved treatments and patient outcomes.
This research aims to provide a comprehensive analysis of the TNNT1 human recombinant, focusing on its molecular characteristics, functional significance, and potential therapeutic implications. By delving into the intricate nature of TNNT1, we aim to contribute to a deeper understanding of muscle biology and pave the way for future research and therapeutic advancements in the realm of neuromuscular disorders.
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 :
Adiponectin Mouse, TrimericDescription:
Adiponectin Mouse Recombinant, Trimeric form
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-247Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.
Source
HEK293 (Human embryonic kidney cell line).
Formulation
Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.
Purity
Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered white lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
BDNF HumanDescription:
Brain-Derived Neurotrophic Factor Human Recombinant
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-207Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
- More Info
- Activity
Description
BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.
Purity
BDNF is greater than 950% as determined SDS-PAGE.
Biological Activity
The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mLActivity
More Info
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Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
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Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF 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
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
Escherichia Coli.
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.
What is the amino acid sequence of BDNF Protein?
MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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Protein content
BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PSPN MouseDescription:
Persephin Mouse Recombinant
Persephin, PSPN.
Product # :
CYT-802Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- More Info
Description
PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.More Info
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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
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Synonyms
Persephin, PSPN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN 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 PSPN 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
ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG
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 :
CALM BovineDescription:
Calmodulin Bovine
Calmodulin, CaM, CALM.
Product # :
PRO-2800Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- source
- formulation
- purity
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Source
Bovine brain tissue.
Formulation
CALM was lyophilized with 2mM EDTA.
Purity
Greater than 95.0%.
More Info
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Synonyms
Calmodulin, CaM, CALM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin 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 CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Biochemical and immunochemical investigations.
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Background
Role in Muscle Contraction and Relaxation:
In muscle cells, calmodulin plays a pivotal role in the regulation of contraction and relaxation. It interacts with myosin light-chain kinase during muscle contraction, initiating the process of cross-bridge cycling. Conversely, during muscle relaxation, calmodulin activates the enzyme myosin light-chain phosphatase, leading to the dephosphorylation of myosin and muscle relaxation. This delicate balance is crucial for proper muscle function.
Neuronal Signalling and Synaptic Plasticity:
In neurons, calmodulin is essential for neurotransmitter release and synaptic plasticity. It modulates the activity of proteins involved in vesicle fusion and neurotransmitter release. Additionally, calmodulin-dependent protein kinases (CaMKs) are critical for synaptic plasticity, learning, and memory. The intricate interplay between calmodulin and neuronal proteins underpins the fundamental processes of learning and cognition.
Implications in Disease and Therapeutics:
Dysregulation of calmodulin has been implicated in various diseases, including cardiac arrhythmias and neurodegenerative disorders. Mutations in calmodulin genes can lead to aberrant calcium signalling and cellular dysfunction. Consequently, understanding these molecular mechanisms offers potential therapeutic targets. Researchers are exploring calmodulin inhibitors and modulators for conditions like cardiac arrhythmias, aiming to restore normal cellular function.
Conclusion:
Calmodulin, with its remarkable structural versatility and central role in cellular signalling, epitomizes the complexity of biological regulation. Its influence spans from the fundamental processes of muscle contraction to the intricacies of neuronal signalling. Unravelling the mysteries of calmodulin not only deepens our understanding of basic biological phenomena but also holds the promise of innovative therapeutic interventions. This research illuminates calmodulin's significance, emphasizing its position as a master regulator in the orchestra of cellular life.
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 :
SERPINF2 MouseDescription:
Serpin Peptidase Inhibitor, Clade F Member 2 Mouse Recombinant
Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.
Product # :
PRO-2240Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
SERPINF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 470 amino acids (28-491 a.a.) and having a molecular mass of 52.9kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). SERPINF2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SERPINF2 protein solution (1mg/ml) contains 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
Alpha-2-antiplasmin (SERPINF2) is a serine protease inhibitor. The main targets of SERPINF2 are plasmin and trypsin; however SERPINF2 also inactivates matriptase-3/TMPRSS7 and chymotrypsin.
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Synonyms
Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.
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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
VDLPGQQPVS EQAQQKLPLP ALFKLDNQDF GDHATLKRSP GHCKSVPTAE ETRRLAQAMM AFTTDLFSLV AQTSTSSNLV LSPLSVALAL SHLALGAQNQ TLHSLHRVLH MNTGSCLPHL LSHFYQNLGP GTIRLAARIY LQKGFPIKDD FLEQSERLFG AKPVKLTGKQ EEDLANINQW VKEATEGKIE DFLSELPDST VLLLLNAIHF HGFWRTKFDP SLTQKDFFHL DERFTVSVDM MHAVSYPLRW FLLEQPEIQV AHFPFKNNMS FVVVMPTYFE WNVSEVLANL TWDTLYHPSL QERPTKVWLP KLHLQQQLDL VATLSQLGLQ ELFQGPDLRG ISEQNLVVSS VQHQSTMELS EAGVEAAAAT SVAMNRMSLS SFTVNRPFLF FIMEDTIGVP LFVGSVRNPN PSALPQLQEQ RDSPDNRLIG QNDKADFHGG KTFGPDLKLA PRMEEDYPQF SSPKHHHHHH.
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.