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Search results

1000 results found for “Avidin”

Name

Description

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  • View Data Sheet

    Name :

    IL 33 Rat

    Description:

    Interleukin-33 Rat Recombinant

    Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.

    Product # :

    CYT-150

    Price :

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    • source
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    Description

    IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a molecular mass of 17.4kDa.The IL 33 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 SDS-PAGE.

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of murine D10S cells is <0.5ng/ml, corresponding to a specific activity of >2,000,000units/mg.

    Citations

    More Info

    • Introduction

      Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.

    • Synonyms

      Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-33 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 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 IL-33 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SIQGTSLLTE SCALSTYNDQ SVSFVLENGC YVINVEDCGK NQEKDKVLLR YYESSFPAQS GDGVDGKKLM VNMSPIKDTD IWLNANDKDY SVELQKGDVS PPDQAFFVLH KKSSDFVSFE CKNLPGTYIG VKDNQLALVE ENDESCNNIM FKLSKM

    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.

    Il 33 Rat
  • View Data Sheet

    Name :

    LIF Rat

    Description:

    Leukemia Inhibitory Factor Rat Recombinant

    Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.

    Product # :

    CYT-731

    Price :

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    Description

    Leukemia Inhibitory Factor (LIF) Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.8 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LIF Rat was lyophilized from 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity of rat LIF is determined by the ability to induce differentiation of M1 myeloid leukemic cells. The minimum detectable concentration of rat LIF in this assay is 0.5ng/mL.

    Citations

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPLPITPVNA TCAIRHPCHG NLMNQIKSQL AQLNGSANAL FISYYTAQGE PFPNNVDKLC APNMTDFPPF HANGTEKTKL VELYRMVTYL GASLTNITWD QKNLNPTAVS LQIKLNATTD VMRGLLSSVL CRLCNKYHVG HVDVPCVPDN SSKEAFQRKK LGCQLLGTYK QVISVLAQAF .

    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.

    Lif Rat
  • View Data Sheet

    Name :

    IL17D Human

    Description:

    Interleukin-17D Human Recombinant

    Interleukin 17D, Interleukin 27, IL-17D, IL-27, IL27, Interleukin-17D, Interleukin-27, IL17D.

    Product # :

    CYT-876

    Price :

    Quantity :

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    Description

    Interleukin-17D Human Recombinant (18-202) produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 polypeptide chains of 185 amino acids each and having a molecular mass of 40kDa.The IL-17D is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Immobilized rHuIL-17D binds to rHuIL-17BR with EC50 less than 2µg/ml.

    Citations

    More Info

    • Introduction

      IL17D modulates immune responses indirectly by stimulating the production of myeloid growth factors and chemokines, as well as suppressing the proliferation of myeloid progenitors. IL17D is expressed in the skeletal muscle, heart, adipose tissue, lung, pancreas, and nervous system. Among IL-17 family members, IL17D is most closely related to IL17B, sharing 27% aa sequence identity. The treatment of endothelial cells with IL17D cytokine stimulates the production of other cytokines including IL6, IL8 and CSF2/ GM-CSF. The increased expression of IL8 induced by IL17D cytokine is NF-kappa B-dependent.

    • Synonyms

      Interleukin 17D, Interleukin 27, IL-17D, IL-27, IL27, Interleukin-17D, Interleukin-27, IL17D.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL17D although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-17D 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 IL-17D in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APRAGRRPAR PRGCADRPEE LLEQLYGRLA AGVLSAFHHT LQLGPREQAR NASCPAGGRP ADRRFRPPTN LRSVSPWAYR ISYDPARYPR YLPEAYCLCR GCLTGLFGEE DVRFRSAPVY MPTVVLRRTP ACAGGRSVYT EAYVTIPVGC TCVPEPEKDA DSINSSIDKQ GAKLLLGPND APAGP.

    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.

    Il17D Human
  • View Data Sheet

    Name :

    Leptin qA Human, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Human Recombinant

    Product # :

    CYT-1251

    Price :

    Quantity :

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    Description

    Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Human Qa Peg
  • View Data Sheet

    Name :

    IFNG Rat

    Description:

    IFN-Gamma Rat Recombinant

    Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    Product # :

    CYT-359

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    Description

    IFN-gamma Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids and having a molecular mass of 15609 Dalton.The IFN-gamma is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by the cytopathic affect inhibition assay with murine L929 cells chalenged with EMC virus was < 0.1 ng/ml, corresponding to a specific activity of 10,000,000units/mg.

    Citations

    More Info

    • Introduction

      IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
      IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs.

    • Synonyms

      Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Gln-Gly-Tyr-Leu.

    • Background

      What is the molecular weight/Mw of IFNG RAT Protein?
      IFNG RAT Protein has a total Mw of 15.6kDa.

      What is the source or expression system of IFNG RAT Protein?
      Escherichia Coli.

      What is the Purity of IFNG RAT Protein?
      IFNG RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNG RAT Protein?
      The specific activity as determined by the cytopathic affect inhibition assay with murine L929 cells chalenged with EMC virus was < 0.1 ng/ml, corresponding to a specific activity of 10,000,000units/mg.

      What is the amino acid sequence of IFNG RAT Protein?
      he sequence of the first five N-terminal amino acids was determined and was found to be Met-Gln-Gly-Tyr-Leu.

      What applications can IFNG RAT Protein be used in?
      IFNG RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNG RAT Protein?
      The endotoxin level is minimal, IFNG RAT Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Interferon Gamma Rat
  • View Data Sheet

    Name :

    IFN a 2b Human

    Description:

    IFN-Alpha 2b Human Recombinant

    IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

    Product # :

    CYT-205

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    Description

    IFN-a 2b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids and having a molecular mass of 19400 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine. The IFN-alpha 2b gene was obtained from human leukocytes. The IFN-a 2b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a (1 mg/ml) solution in containing 2.3 mg Sodium phosphate dibasic and 0.55 mg sodium phosphate monobasic buffer.

    Purity

    Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

    Citations

    More Info

    • Introduction

      IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

    • Synonyms

      IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN alpha 2b 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 IFN-alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE

    • Background

      IFN-alpha forms are produced by monocytes/macrophages, lymphoblastoid cells, fibroblasts, and a number of different cell types following induction by viruses, nucleic acids, glucocorticoid hormones, and low-molecular weight substances (n-butyrate, 5-bromodeoxy uridine). At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end. Disulfide bonds are formed between cysteines at positions 1/98 and 29/138. The disulfide bond 29/138 is essential for biological activity while the 1/98 bond can be reduces without affecting biological activity. All IFN-alpha forms contain a potential glycosylation site but most subtypes are not glycosylated. In contrast to IFN-gamma IFN-alpha proteins are stable at pH2.

      There are at least 23 different IFN-alpha genes. They have a length of 1-2 kb and are clustered on human chromosome 9p22. It is not known whether all these genes are expressed following stimulation of the cells. In some cell systems expression of some subtypes (IFN-alpha-1, IFN-alpha-2, IFN-alpha-4) is stronger than those of others. IFN-alpha genes do not contain intron sequences found in many other eukaryotic genes (see also: gene expression). Based upon the structures two types of IFN-alpha genes, designated class 1 and II, are distinguished. They encode proteins of 156-166 and172 amino acids, respectively. Deletions covering 9p22 are observed frequently in cells of lymphoblastoid leukemias. It is not known to date whether this is of significance with respect to IFN expression.

      The gene encoding the IFN-alpha receptor maps to human chromosome 21q22.1. IFN-alpha and IFN-beta are thought to bind to the same IFN binding subunit which is expressed in 100-5000 copies in IFN-alpha sensitive and -resistant cells and is associated with other as yet unidentified proteins. The IFN-omega (Omega IFN) also binds to the IFN-alpha/IFN-beta receptor. Another receptor expressed on B-lymphocytes is identical with CD21. This receptor also binds Epstein-Barr virus through its gp350/220 coat protein.Signal transduction mechanisms elicited after binding of IFN-alpha to its receptors involves tyrosine phosphorylation (see also: PTK; protein tyrosine kinase) of various non-receptor tyrosine kinases belonging to the Janus kinases. Soluble forms of the IFN-alpha receptor, corresponding to truncated forms of the extracellular domain of the cell surface IFN-alpha receptor, have been found in human serum and in normal human urine.

      All known subtypes of IFN-alpha show the same antiviral antiparasitic, antiproliferative activities in suitable bioassays although they may differ in relative activities. Human IFN-alpha is also a potent antiviral substance in murine, porcine, and bovine cell systems. Human IFN-alpha is less active in rodent cells. Site-directed mutagenesis techniques have been used to create some variants of certain subtypes (IFN-alpha-2) that display approximately 100-fold enhanced antiviral activities in mouse cells.

      What is the molecular weight/Mw of IFN A 2B HUMAN Protein?
      IFN A 2B HUMAN Protein has a total Mw of 19.4kDa.

      What is the source or expression system of IFN A 2B HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IFN A 2B HUMAN Protein?
      IFN A 2B HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFN A 2B HUMAN Protein?
      The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

      What is the amino acid sequence of IFN A 2B HUMAN Protein?
      MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
      What applications can IFN A 2B HUMAN Protein be used in?
      IFN A 2B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFN A 2B HUMAN Protein?
      The endotoxin level is minimal, IFN A 2B HUMAN Protein was purified using conventional chromatography techniques.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.924 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IFN alpha 2b 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.

    Interferon Alpha 2B Human
  • View Data Sheet

    Name :

    ACTH

    Description:

    Adrenocorticotropic Hormone

    Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.

    Product # :

    HOR-279

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    Description

    The Molecular formula of Adrenocorticotropic Hormone is C136H210N40O31S and the molecular weight is 2933.5 Dalton.

    Formulation

    The ACTH hormone was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adrenocorticotropic hormone, as its name implies, stimulates the adrenal cortex. More specifically, it stimulates secretion of glucocorticoids such as cortisol, and has little control over secretion of aldosterone, the other major steroid hormone from the adrenal cortex. Stimulates secretion of adrenal corticosteroids and induces growth of adrenal cortex. ACTH also called Tetracosactide directly activates G-proteins. A stimulator of adenylate cyclase and cAMP formation.

    • Synonyms

      Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Adrenocorticotropic Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ACTH 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 ACTH in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-OH.

    • Background

      What is the molecular weight/Mw of ACTH Protein?
      ACTH Protein has a total Mw of 2.9kDa.

      What is the Purity of ACTH Protein?
      ACTH Protein is >98 % pure as determined by SDS-PAGE.

      What is the Biological Activity of ACTH Protein?
      The biological functionality of ACTH Protein will be determined in the future.

      What is the amino acid sequence of ACTH Protein?
      Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-OH.

      What applications can ACTH Protein be used in?
      ACTH Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ACTH Protein?
      The endotoxin level is minimal, ACTH Protein was purified using conventional chromatography techniques.

      Who supplies ACTH that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of ACTH?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Acth
  • View Data Sheet

    Name :

    Vimentin PAT5H8AT Antibody

    Description:

    Vimentin PAT5H8AT, Mouse Anti Human

    Vimentin, Vim, FLJ36605.

    Product # :

    ANT-682

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    Citations

    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.

    • Synonyms

      Vimentin, Vim, FLJ36605.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human Vimentin mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human Vimentin protein 1-466 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT5H8AT.

    • Applications

      Vimentin antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      Vimentin antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Vimentin Pat5H8At Antibody
  • View Data Sheet

    Name :

    OSM Human, His

    Description:

    Oncostatin-M Human Recombinant, His Tag

    OSM, MGC20461.

    Product # :

    CYT-060

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    Description

    OSM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (26-234) and having a molecular mass of 25.9 kDa.The OSM is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSM protein (0.5mg/ml) is supplied in 20mM Tris-HCl, pH-8, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      POU2AF1 is a lymphocyte specific transcription coactivator protein. POU2AF1 cooperates only with the Oct1/2 proteins using sub domains in the POU domain of the Oct1/2 proteins, increasing their transcriptional efficiency. Even though POU2AF1 have no basic ability to bind DNA, it links firmly with the octomer motif in the presence of Oct1 and Oct2. POU2AF1 is expressed at maximum levels in spleen and peripheral blood leukocytes.

    • Synonyms

      OSM, MGC20461.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAAIGSCSKE YRVLLGQLQK QTDLMQDTSR LLDPYIRIQG LDVPKLREHC RERPGAFPSE ETLRGLGRRG FLQTLNATLG CVLHRLADLE QRLPKAQDLE RSGLNIEDLE KLQMARPNIL GLRNNIYCMA QLLDNSDTAE PTKAGRGASQ PPTPTPASDA FQRKLEGCRF LHGYHRFMHS VGRVFSKWGE SPNRSRRHSP HQALRKGVRR.

    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.

    Osm Human His
  • View Data Sheet

    Name :

    CRADD Human

    Description:

    Caspase and RIP Adapter with Death Domain Human Recombinant

    RAIDD, MGC9163, CRADD, Death domain-containing protein CRADD, Caspase and RIP adapter with death domain, RIP-associated protein with a death domain, CASP2 and RIPK1 domain containing adaptor with death domain.

    Product # :

    PRO-465

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    Description

    CRADD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.9 kDa. CRADD is fused to a 20 amino acids His-Tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The CRADD protein solution (1mg/ml) contains 20mM Tris-HCl pH-8 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CRADD is a 22kDa, widely-expressed cytosolic adaptor/signaling protein that induces cell apoptosis/cell death in numerous tissues. CRADD is a death domain (CARD) that recruits, caspase 2/ICH1 to the cell death signal transduction complex that includes TNFR1A, RIPK1/RIP kinase, and numbers of other CARD domain-containing proteins.

    • Synonyms

      RAIDD, MGC9163, CRADD, Death domain-containing protein CRADD, Caspase and RIP adapter with death domain, RIP-associated protein with a death domain, CASP2 and RIPK1 domain containing adaptor with death domain.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEARDKQVLR SLRLELGAEV LVEGLVLQYL YQEGILTENH IQEINAQTTG LRKTMLMLDI LPSRGPKAFD TFLDSLQEFP WVREKLKKAR EEAMTDLPAG DRLTGIPSHI LNSSPSDRQI NQLAQRLGPE WEPMVLSLGL SQTDIYRCKA NHPHNVQSQV VEAFIRWRQR FGKQATFQSL HNGLRAVEVD PSLLLHMLE.

    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.

    Cradd Human
  • View Data Sheet

    Name :

    TAGLN Human

    Description:

    Transgelin Human Recombinant

    SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.

    Product # :

    PRO-851

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    Description

    TAGLN Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-201 a.a.) and having a molecular mass of 24.8 kDa. The TAGLN is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TAGLN Human solution containing 20mM Tris-HCl pH-7.5, 1mM DTT & 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TAGLN is a transformation and form-change responsive actin cross-linking/gelling protein that is part of the calponin family. TAGLN is expressed abundantly in fibroblasts and smooth muscle. TAGLN participates in calcium interactions and contractile properties of the cell that contribute to replicative senescence. Throughout embryogenesis, TAGLN is expressed in smooth, cardiac and skeletal muscle, but is limited during late fetal growth and adulthood to all vascular and visceral smooth muscle cells and low levels of expression in heart. TAGLN is downregulated in several transformed cell lines, showing that a decrease of TAGLN expression is an premature indicator of the onset of transformation.

    • Synonyms

      SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIIVQCGP DVGRPDRGRL GFQVWLKNGV ILSKLVNSLY PDGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVIKTD MFQTVDLFEG KDMAAVQRTL MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTESQLQE GKHVIGLQMG SNRGASQAGM TGYGRPRQII S.

    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.

    Tagln Human
  • View Data Sheet

    Name :

    Leptin Protein

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

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    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by Gel filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    Citations

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile water or 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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).

    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.

    Leptin Human
  • View Data Sheet

    Name :

    SCGB1D1 Human

    Description:

    Secretoglobin Family 1D, Member 1 Human Recombinant

    Secretoglobin family 1D member 1, Lipophilin-A, SCGB1D1, LIPHA, LPNA, LIPA, LPHA.

    Product # :

    PRO-1602

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    Description

    SCGB1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-90) containing 79 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 8.8kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    SCGB1D1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Secretoglobin Family 1D, Member 1 (SCGB1D1) belongs to the lipophilin subfamily, part of the uteroglobin superfamily, and is an ortholog of prostatein (which is the major secretory glycoprotein of the rat ventral prostate gland). SCGB1D1 binds androgens and other steroids. In addition SCGB1D1 binds chemotherapeutic drugs during the prostate cancer treatment. Steroid hormones regulate the SCGB1D1 transcription. SCGB1D1 is secreted into extracellular space. SCGB1D1 gene product represents one component of a heterodimeric molecule found in human tears whose elution profile is consistent with prostatein (which is a tetrameric molecule comprised of 3 peptide components in heterodimers).

    • Synonyms

      Secretoglobin family 1D member 1, Lipophilin-A, SCGB1D1, LIPHA, LPNA, LIPA, LPHA.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • 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. SCGB1D1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS VVCQALGSEI TGFLLAGKPV FKFQLAKFKA PLEAVAAKME VKKCVDTMAY EKRVLITKTL GKIAEKCDR.

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    Scgb1D1 Human
  • View Data Sheet

    Name :

    SCGN Human

    Description:

    Secretagogin Human Recombinant

    SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.

    Product # :

    PRO-599

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    Description

    SCGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-276 a.a.) and having a molecular mass of 34.2kDa. SCGN is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    SCGN His-Tag (1mg/ml) protein is supplied in 20mM Tris HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
      Secretagogin plays a role in human non-functional pituitary adenomas.

    • Synonyms

      SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MDSSREPTLG RLDAAGFWQV WQRFDADEKG YIEEKELDAF FLHMLMKLGT DDTVMKANLH KVKQQFMTTQ DASKDGRIRM KELAGMFLSE DENFLLLFRR ENPLDSSVEF MQIWRKYDAD SSGFISAAEL RNFLRDLFLH HKKAISEAKL EEYTGTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DACSTEERKR DFEKIFAYYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCL GLKINP.

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    Scgn Human
  • View Data Sheet

    Name :

    Myostatin Human, HEK

    Description:

    Myostatin Human Recombinant, HEK

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-833

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    Description

    Myostatin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Ser375) containing a total of 360 amino acids, having a calculated molecular mass of 41.1kDa. Myostatin is fused to a 2 aa N-terminal linker and a 6 aa His tag at N-Terminus.

    Source

    HEK 293.

    Formulation

    Myostatin solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • Physical Appearance

      Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      HHHHHHASNE NSEQKENVEK EGLCNACTWR QNTKSSRIEA IKIQILSKLR LETAPNISKD VIRQLLPKAP PLRELIDQYD VQRDDSSDGS LEDDDYHATT ETIITMPTES DFLMQVDGKP KCCFFKFSSK IQYNKVVKAQ LWIYLRPVET PTTVFVQILR LIKPMKDGTR YTGIRSLKLD MNPGTGIWQS IDVKTVLQNW LKQPESNLGI EIKALDENGH DLAVTFPGPG EDGLNPFLEV KVTDTPKRSR RDFGLDCDEH STESRCCRYP LTVDFEAFGW DWIIAPKRYK ANYCSGECEF VFLQKYPHTH LVHQANPRGS AGPCCTPTKM SPINMLYFNG KEQIIYGKIP AMVVDRCGCS.

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    Myostatin Human Hek
  • View Data Sheet

    Name :

    ARL5A Human

    Description:

    ADP-Ribosylation Factor-Like 5A Human Recombinant

    ARL5, ARFLP5, ADP-ribosylation factor-like 5A.

    Product # :

    PRO-040

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    Description

    ARL5A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203amino acids (1-179a.a.) and having a molecular mass of 23.3kDa.ARL5A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARL5A protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2mM PMSF and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARL5A is a member of the ARF family of GTP-binding proteins. ARFs are vital in eukaryotic vesicular trafficking pathways and have a crucial part in the activation of phospholipase D. Different from ARF family members, ARL5 is believed to lack ADP-ribosylation enhancing activity. ARL5A is developmentally regulated and has a role in nuclear dynamics and signaling cascades during embryonic development.

    • Synonyms

      ARL5, ARFLP5, ADP-ribosylation factor-like 5A.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMGILFT RIWRLFNHQE HKVIIVGLDN AGKTTILYQF SMNEVVHTSP TIGSNVEEIV INNTRFLMWD IGGQESLRSS WNTYYTNTEF VIVVVDSTDR ERISVTREEL YKMLAHEDLR KAGLLIFANK QDVKECMTVA EISQFLKLTS IKDHQWHIQA CCALTGEGLC QGLEWMMSRL KIR

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    Arl5A Human
  • View Data Sheet

    Name :

    BCAR1 Human

    Description:

    Breast Cancer Anti-Estrogen Resistance 1 Human Recombinant

    CAS, CAS1, CASS1, CRKAS, P130Cas, Breast cancer anti-estrogen resistance protein 1, CRK-associated substrate, Cas scaffolding protein family member 1, BCAR1.

    Product # :

    PRO-1858

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    Description

    BCAR1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 407 amino acids (465-848) and having a molecular mass of 43.9kDa. BCAR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCAR1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Breast Cancer Anti-Estrogen Resistance 1 (BCAR1) is a Src family kinase substrate which takes part in a range of cellular events such as migration, survival, transformation, and invasion. BCAR1 plays a vital role for tyrosine kinase-based signaling related to cell adhesion.

    • Synonyms

      CAS, CAS1, CASS1, CRKAS, P130Cas, Breast cancer anti-estrogen resistance protein 1, CRK-associated substrate, Cas scaffolding protein family member 1, BCAR1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSRLQQGVS ATVAHLLDLA GSAGATGSWR SPSEPQEPLV QDLQAAVAAV QSAVHELLEF ARSAVGNAAH TSDRALHAKL SRQLQKMEDV HQTLVAHGQA LDAGRGGSGA TLEDLDRLVA CSRAVPEDAK QLASFLHGNA SLLFRRTKAT APGPEGGGTL HPNPTDKTSS IQSRPLPSPP KFTSQDSPDG QYENSEGGWM EDYDYVHLQG KEEFEKTQKE LLEKGSITRQ GKSQLELQQL KQFERLEQEV SRPIDHDLAN WTPAQPLAPG RTGGLGPSDR QLLLFYLEQC EANLTTLTNA VDAFFTAVAT NQPPKIFVAH SKFVILSAHK LVFIGDTLSR QAKAADVRSQ VTHYSNLLCD LLRGIVATTK AAALQYPSPS AAQDMVE.

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    Bcar1 Human
  • View Data Sheet

    Name :

    NTS Human, sf9

    Description:

    Neurotensin Human Recombinant, sf9

    Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.

    Product # :

    PRO-2374

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    Description

    NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.

    • Synonyms

      Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.

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    Nts Human Sf9
  • View Data Sheet

    Name :

    STX17 Human

    Description:

    Syntaxin-17 Human Recombinant

    Syntaxin 17

    Product # :

    PRO-1712

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    Description

    STX17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229) and having a molecular mass of 28.6kDa.STX17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STX17 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      STX17 is a member of to the syntaxin family and contains 1 t-SNARE coiled-coil homology domain. STX17 is involved in vesicle trafficking to lysosomes and takes part in procedures associated with cell division.

    • Synonyms

      Syntaxin 17

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSEDEEK VKLRRLEPAI QKFIKIVIPT DLERLRKHQI NIEKYQRCRI WDKLHEEHIN AGRTVQQLRS NIREIEKLCL KVRKDDLVLL KRMIDPVKEE ASAATAEFLQ LHLESVEELK KQFNDEETLL QPPLTRSMTV GGAFHTTEAE ASSQSLTQIY ALPEIPQDQN AAESWETLEA DLIELSQLVT DFSLLVNSQQ EKIDSIADHV NSAAVNVEEG TKNLGKAAKY KL

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    Stx17 Human
  • View Data Sheet

    Name :

    ESAT6

    Description:

    Early Secretory Target Mycobacterium Tuberculosis Recombinant

    Early Secretory Target Mycobacterium Tuberculosis, ESAT-6.

    Product # :

    PRO-291

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    Description

    ESAT-6 Recombinant produced in Baculovirus is a single, glycosylated, polypeptide chain containing 104 amino acids (1-95 a.a) having a total molecular mass of 11kDa.The ESAT-6 fused to a 6 amino acid His-tag & purified by proprietary chromatographic techniques.

    Source

    Baculovirus.

    Formulation

    ESAT-6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Mycobacterium antigen ESAT-6 has been isolated from low molecular weight fractions of the shot-term-culture filtrate (ST-CF) and it can easily be detected in tuberculosis patients.
      The export of ESAT-6 which is a potent T-cell antigen, and related proteins requires a dedicated secretory apparatus that is encoded by a group of genes, several of which also code for proteins that are recognized strongly by T cells. The ESAT-6 systems can consequently be considered as immunogenicity islands and there is mounting evidence that the equivalent genes are subject to selective pressure imposed by the immune system of the host.
      This antigen includes many epitopes detectable in the serum of most patients with tuberculosis (more than 90%). By the attempts to obtain the vaccine on the basis of ESAT-6 it was demonstrated that the optimization of adjuvant is very important when using the combination of dioctadecylammonium bromide and monophosphoryllipide.
      Recently it was shown that ESAT-6 is very potential as diagnostic for differentiation between the mycobacterial infection and BCG vaccination. The main topic in ESAT-6 using is in antibody production and in test-systems for tuberculosis elaboration.

    • Synonyms

      Early Secretory Target Mycobacterium Tuberculosis, ESAT-6.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPMTEQQWN FAGIEAAASA IQGNVTSIHS LLDEGKQSLT KLAAAWGGSG SEAYQGVQQK WDATATELNN ALQNLARTIS EAGQAMASTE GNVTGMFAHH HHHH.

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    Esat6
  • View Data Sheet

    Name :

    FLT1 Mouse

    Description:

    Vascular Endothelial Growth Factor receptor-1 Mouse Recombinant

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-139

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    Description

    FLT1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (23-759 a.a) containing a total of 970 amino acids, having a molecular mass of 108.9kDa. FLT1 is fused to a 233 amino acid hIgG-his tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    FLT1 protein solution (1mg/ml) containing 10% glycerol and PBS.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 50ng/ml and is measured by its ability to inhibit proliferation using HUVEC human umbilical vein endothelial cells in the presence of Human VEGF165.

    Citations

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    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      YGSGSKLKVP ELSLKGTQHV MQAGQTLFLK CRGEAAHSWS LPTTVSQEDK RLSITPPSAC GRDNRQFCST LTLDTAQANH TGLYTCRYLP TSTSKKKKAE SSIYIFVSDA GSPFIEMHTD IPKLVHMTEG RQLIIPCRVT SPNVTVTLKK FPFDTLTPDG QRITWDSRRG FIIANATYKE IGLLNCEATV NGHLYQTNYL THRQTNTILD VQIRPPSPVR LLHGQTLVLN CTATTELNTR VQMSWNYPGK ATKRASIRQR IDRSHSHNNV FHSVLKINNV ESRDKGLYTC RVKSGSSFQS FNTSVHVYEK GFISVKHRKQ PVQETTAGRR SYRLSMKVKA FPSPEIVWLK DGSPATLKSA RYLVHGYSLI IKDVTTEDAG DYTILLGIKQ SRLFKNLTAT LIVNVKPQIY EKSVSSLPSP PLYPLGSRQV LTCTVYGIPR PTITWLWHPC HHNHSKERYD FCTENEESFI LDPSSNLGNR IESISQRMTV IEGTNKTVST LVVADSQTPG IYSCRAFNKI GTVERNIKFY VTDVPNGFHV SLEKMPAEGE DLKLSCVVNK FLYRDITWIL LRTVNNRTMH HSISKQKMAT TQDYSITLNL VIKNVSLEDS GTYACRARNI YTGEDILRKT EVLVRDSEAP HLLQNLSDYE VSISGSTTLD CQARGVPAPQ ITWFKNNHKI QQEPGIILGP GNSTLFIERV TEEDEGVYRC RATNQKGAVE

    • Background

      Endothelial cells express 3 different vascular endothelial growth factor receptors: VEGFR-1 (Flt1), VEGFR-2 (KDR/Flk1), VEGFR-3 (Flt4) which are a part of the receptor tyrosine kinases family. Those receptors express mostly in endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. Flt1 contains 7 immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Flt-1, when compared to VEGFR-2 receptor has a higher affinity for VEGF but a weaker signalling activity. VEGFR-1 also mediates signals for differentiation.

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    Flt1 Mouse
  • View Data Sheet

    Name :

    FLT4 Human

    Description:

    Vascular Endothelial Growth Factor Receptor-3 Human Recombinant

    Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

    Product # :

    PKA-244

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    Description

    Soluble FLT4 Human Recombinant fused with a carboxy-terminal 6X histidine-tag produced in baculovirus is a monomeric, glycosylated, polypeptide containing the extracellular part, 25-774 amino acids and having a total molecular mass of 120 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding. The FLT4 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT4 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to bind recombinant rat VEGF-C in a functional solid phase binding assay. Immobilised recombinant human VEGFR-3/FLT-4 at 5 µg/ml can bind recombinant rat VEGF-C in a linear range of 8-500 ng/ml.

    Citations

    More Info

    • Introduction

      All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

    • Synonyms

      Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT4 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 FLT4 in sterile water not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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    Flt4 Human
  • View Data Sheet

    Name :

    PLCXD3 Human

    Description:

    Phosphatidylinositol Specific Phospholipase C X Domain Human Recombinant

    PI-PLC X domain-containing protein 3, phosphatidylinositol-specific phospholipase C X domain containing 3, phosphatidylinositol-specific phospholipase C, X domain containing 3

    Product # :

    PRO-2651

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    Description

    PLCXD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a.) and having a molecular mass of 38.7 kDa. PLCXD3 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PLCXD3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PLCXD3, also referred to asphosphatidylinositol Specific Phospholipase C X Domain Containing 3, contains 1 PI-PLC X-box domain. Creutzfeldt-Jakob Disease, is one of the diseases linked with PLCXD3. It is related to Ectoderm Differentiation, obsolete signal transducer activity and phosphoric diester hydrolase activity.

    • Synonyms

      PI-PLC X domain-containing protein 3, phosphatidylinositol-specific phospholipase C X domain containing 3, phosphatidylinositol-specific phospholipase C, X domain containing 3

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMASSQGK NELKLADWMA TLPESMHSIP LTNLAIPGSH DSFSFYIDEA SPVGPEQPET VQNFVSVFGT VAKKLMRKWL ATQTMNFTGQ LGAGIRYFDL RISTKPRDPD NELYFAHGLF SAKVNEGLEE INAFLTDHHK EVVFLDFNHF YGMQKYHHEK LVQMLKDIYG NKMCPAIFAQ EVSLKYLWEK DYQVLVFYHS PVALEVPFLW PGQMMPAPWA NTTDPEKLIQ FLQASITERR KKGSFFISQV VLTPKASTVV KGVASGLRET ITERALPAMM QWVRTQKPGE SGINIVTADF VELGDFISTV IKLNYVFDEG EANT

    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.

    Plcxd3 Human
  • View Data Sheet

    Name :

    GEMIN6 Human

    Description:

    Gem-Associated Protein 6 Human Recombinant

    Gem-associated protein 6, Gemin-6, SIP2, GEMIN6.

    Product # :

    PRO-1394

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    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    GEMIN6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167a.a) and having a molecular mass of 21.9kDa. GEMIN6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GEMIN6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Gem-Associated Protein 6 (GEMIN6) is a member of a large macromolecular complex, localized to both the cytoplasm and the nucleus, which takes part in the cytoplasmic assembly of small nuclear ribonucleoproteins (snRNPs). SMN, GEMIN2, GEMIN3, GEMIN4, and GEMIN5 are additional members of this complex.

    • Synonyms

      Gem-associated protein 6, Gemin-6, SIP2, GEMIN6.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSEWMKK GPLEWQDYIY KEVRVTASEK NEYKGWVLTT DPVSANIVLV NFLEDGSMSV TGIMGHAVQT VETMNEGDHR VREKLMHLFT SGDCKAYSPE DLEERKNSLK KWLEKNHIPI TEQGDAPRTL CVAGVLTIDP PYGPENCSSS NEIILSRVQD LIEGHLTASQ.

    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.

    Gemin6 Human
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