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Search results

1000 results found for “tachykinin”

Name

Description

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  • View Data Sheet

    Name :

    IL17E Mouse

    Description:

    Interleukin-17E Mouse Recombinant

    IL-25, IL-17E, IL17E, IL25, Interleukin-25.

    Product # :

    CYT-641

    Price :

    Quantity :

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    • source
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    Description

    Recombinant mouse IL-17E is a non-glycosylated, disulfide-linked homodimer, containing 2x145 amino acid chains, with a total molecular weight of 35.5 kDa. The Mouse IL-17E is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL17E was lyophilized from a concentrated (1mg/ml) solution containing no additives.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent production of IL-8 by human PBMCs and is 322-488ng/ml.

    More Info

    • Introduction

      IL-25 also called IL-17E cytokine has a sequence similarity with IL17.
      IL-17E indluces NF-kappaB activation, and stimulates the production of IL-8. IL17E and IL17B are ligands for the cytokine receptor IL17BR. IL-25 is a proinflammatory cytokine favoring Th2-type immune response. The upregulation of costimulation-induced IL-17E receptors and release of cytokines and chemokines from IL-17E treated costimulated Th cells are differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Blocking Iinterleukin-25 prevents airway hyperresponsiveness, a critical feature of clinical asthma. IL25 produced by innate effector eosinophils and basophils increase the allergic inflammation by enhancing the maintenance and functions of TSLP-DC activated adaptive Th2 memory cells. Over expression of IL-25 up-regulates gene expression of Th2 cytokines and induces growth retardation, jaundice, and multiorgan inflammation in a transgenic mouse model. IL-25 contributes to the induction and maintenance of eosinophilic inflammation by acting on lung fibroblasts which supports the fact that IL-17E is an important factor in asthma pathophysiology. IL-17E operates by amplifying TH2 cell-mediated allergic airway inflammation but doesn’t induce allergic inflammation in vivo.

    • Synonyms

      IL-25, IL-17E, IL17E, IL25, Interleukin-25.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Murine IL17E although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17E 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 Mouse IL17E in sterile 10mM HCl at a concentration not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VSLRIQEGCSHLPSCCPSKEQEPPEEWLKWSSASVS
      PPEPLSHTHHAESCRASKDGPLNSRAISPWSYELDRD
      LNRVPQDLYHARCLCPHCVSLQTGSHMDPLGNSVPL
      YHNQTVFYRRPCHGEEGTHRRYCLERRLYRVSLACV
      CVRPRVMA.

    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.

    Il17E Mouse
  • View Data Sheet

    Name :

    MINA Human

    Description:

    MYC Induced Nuclear Antigen Human Recombinant

    MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.

    Product # :

    PRO-2078

    Price :

    Quantity :

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    Description

    MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MINA protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.

    • Synonyms

      MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.

    • 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 MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.

    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.

    Mina Human
  • View Data Sheet

    Name :

    NKIRAS1 Human

    Description:

    NFKB Inhibitor Interacting Ras-Like 1 Human Recombinant

    NF-kappa-B inhibitor-interacting Ras-like protein 1, I-kappa-B-interacting Ras-like protein 1, Kappa B-Ras protein 1, KappaB-Ras1, NKIRAS1, KBRAS1.

    Product # :

    PRO-1039

    Price :

    Quantity :

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    • description
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    Description

    NKIRAS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a) and having a molecular mass of 23.8kDa (Molecular weight on SDS-PAGE will appear higher).NKIRAS1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NKIRAS1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NF-kappa-B inhibitor-interacting Ras-like protein 1 (NKIRAS1) is a member of the small GTPase superfamily. NKIRAS1 is an unusual Ras-like protein which acts as a potent regulator of NF-kappa-B activity by thwarting the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, describing why NFKBIB is more resistant to degradation. NKIRAS1 functions by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB.

    • Synonyms

      NF-kappa-B inhibitor-interacting Ras-like protein 1, I-kappa-B-interacting Ras-like protein 1, Kappa B-Ras protein 1, KappaB-Ras1, NKIRAS1, KBRAS1.

    • 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 MGKGCKVVVC GLLSVGKTAI LEQLLYGNHT IGMEDCETME DVYMASVETD RGVKEQLHLY DTRGLQEGVE LPKHYFSFAD GFVLVYSVNN LESFQRVELL KKEIDKFKDK KEVAIVVLGN KIDLSEQRQV DAEVAQQWAK SEKVRLWEVT VTDRKTLIEP FTLLASKLSQ PQSKSSFPLP GRKNKGNSNS EN.

    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.

    Nkiras1 Human
  • View Data Sheet

    Name :

    GCK Human, Active

    Description:

    Hexokinase-4 Human Recombinant, Active

    Glucokinase, Glucokinase (Hexokinase 4), Hexokinase Type IV, HK IV, HK4, Maturity Onset Diabetes of The Young 2, ATP:D-Hexose 6-Phosphotransferase, Hexokinase D, Pancreatic Isozyme, Hexokinase-4, Hexokinase-D, Hexokinase 4.

    Product # :

    PKA-116

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    Description

    GCK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.3kDa. GCK is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GCK protein solution (1mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,000 pmol/min/ug. One unit will convert 1 pmoles of D-Glucose to D-Glucose-6-phosphate per minute at pH8.0 at 37C.

    More Info

    • Introduction

      GCK is an enzyme that expedite the formation of glucose-6-phosphate for glucose by phosphorylation. Humans and other vertebrates have GCK in the cells of the pancreas and liver. In both organs, the enzyme has an important role in carbohydrate metabolism regulation by sensing sugar levels and acting according to the change in glucose levels, that can rise after a meal or fall during fasting. Mutations in the gene that codes for this enzyme can cause hypoglycemia or diabetes.

      .

    • Synonyms

      Glucokinase, Glucokinase (Hexokinase 4), Hexokinase Type IV, HK IV, HK4, Maturity Onset Diabetes of The Young 2, ATP:D-Hexose 6-Phosphotransferase, Hexokinase D, Pancreatic Isozyme, Hexokinase-4, Hexokinase-D, Hexokinase 4.

    • 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 MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH EEASVKMLPT YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS VKTKHQMYSI PEDAMTGTAE MLFDYISECI SDFLDKHQMK HKKLPLGFTF SFPVRHEDID KGILLNWTKG FKASGAEGNN VVGLLRDAIK RRGDFEMDVV AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN VELVEGDEGR MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGQQLYE KLIGGKYMGE LVRLVLLRLV DENLLFHGEA SEQLRTRGAF ETRFVSQVES DTGDRKQIYN ILSTLGLRPS TTDCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED VMRITVGVDG SVYKLHPSFK ERFHASVRRL TPSCEITFIE SEEGSGRGAA LVSAVACKKA CMLGQ.

    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.

    Hexokinase 4
  • View Data Sheet

    Name :

    p59-Fyn Human

    Description:

    p59-Fyn Human Recombinant

    Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.

    Product # :

    PRO-506

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    Description

    p59-Fyn Human Recombinant (a.a. 23-216) expressed in E.coli, shows a 50 kDa SDS-PAGE (Including GST tag).The p59-Fyn is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    p59-Fyn in 50mM Tris-Acetate, pH7.5, 1mM EDTA and 20% Glycerol.

    More Info

    • Introduction

      p59-Fyn is a member of the protein-tyrosine kinase oncogene family. p59fyn is a membrane-associated non-receptor protein tyrosine kinase that belongs to the Src-family of kinases. p59-Fyn encodes a membrane-associated tyrosine kinase which is implicated in the control of cell growth. p59-Fyn associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. The unique N-terminal domain of p59fyn interacts with the CD3 and eta chains of the TcR. p59fyn can bind other proteins (p82 and p116) through its SH2 and SH3 domains, which may act as substrates or regulators of fyn activity. p59fyn is highly expressed in brain suggesting that it may have a role in the sensory nervous network and in myelination at early stages of CNS formation. Distinct isoforms exist due to alternative splicing.

    • Synonyms

      Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

    • Applications

      • ELISA
      • Inhibition Assays
      • Western Blotting.

    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.

    P59 Fyn Human
  • View Data Sheet

    Name :

    SERPINI1 Human, His

    Description:

    Serpin Peptidase Inhibitor, Clade I Member 1 Human Recombinant, His Tag

    Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    Product # :

    PRO-1595

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    Description

    SERPINI1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 17-410) containing 404 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 45.9kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.025M phosphate buffer and 0.035M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).

    • Synonyms

      Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    • 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. SERPINI1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASTGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL.

    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.

    Serpini1 Human His
  • View Data Sheet

    Name :

    IL 12 Mouse

    Description:

    Interleukin-12 Mouse Recombinant

    NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    Product # :

    CYT-144

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    Description

    Interleukin-12 Mouse Recombinant produced in HEK 293 cells is a glycosylated disulfide linked heterodimeric polypeptide containing 506 amino acids and having a molecular weight of 75 kDa comprised of disulfide-bonded 35 kDa (p35) and 40 kDa (p40) subunits.The IL-12 is purified by proprietary chromatographic techniques.

    Source

    HEK-293 Cells.

    Formulation

    The protein was lyophilized from 0.5xPBS, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    IL-12 Mouse has full biological activity when compared to standards. The ED50 is determined by the dose-dependent induces secretion of SEAP in HEK-Blue IL-12 cells is 2.302 ng/ml corresponding to a specific activity of 4.3x105 units/mg.

    More Info

    • Introduction

      IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.

    • Synonyms

      NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized mouse IL-12 although stable at room temperature for 3 weeks, should be stored below -18°C. Upon reconstitution IL12 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 murine IL12 in sterile distilled pyrogen free water at 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.

      p40 Subunit: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS
      WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS.

    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.

    Il12 Mouse
  • View Data Sheet

    Name :

    Eotaxin Rat

    Description:

    Eotaxin Rat Recombinant (CCL11)

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.

    Product # :

    CHM-260

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    Description

    Eotaxin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8.4kDa. The CCL11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in in 1×PBS, pH7.4.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution CCL11 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Eotaxin in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.

    • Background

      What is the molecular weight/Mw of EOTAXIN RAT Protein?
      EOTAXIN RAT Protein has a total Mw of 8.4kDa.

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

      What is the Purity of EOTAXIN RAT Protein?
      EOTAXIN RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of EOTAXIN RAT Protein?
      Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.

      What is the amino acid sequence of EOTAXIN RAT Protein?
      HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.

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

      What is the endotoxin level for EOTAXIN RAT Protein?
      The endotoxin level is minimal, EOTAXIN 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.

    Eotaxin Rat
  • View Data Sheet

    Name :

    CDKN1A Human (20-149)

    Description:

    Cyclin-Dependent Kinase Inhibitor 1A (20-149 a.a.) Human Recombinant

    Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

    Product # :

    PKA-137

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    Description

    The CDKN1A Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CDKN1A His-Tagged Fusion Protein, produced in E. coli, is a 20kDa protein containing 130 amino acid residues of the CDKN1A Human, 20-149 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized CDKN1A 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Amino Acid Sequence

      LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLEGDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLVPRSGEQAEGS PGGPGDSQGR KRRQTSMTDF

    • Background

      CDKN1A gene in humans plays an important role in maintaining genomic stability which is critical to cancer prevention and proper function of regular cellular processes. CDKN1A plays a main role in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. CDKN1A, along with CDK2 complexes aids to prevent kinase activity and inhibits progression through G1/S. CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D.

    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.

    Cdkn1A Protein
  • View Data Sheet

    Name :

    CSNK2A2 Human

    Description:

    Casein Kinase 2, Alpha 2 Prime Human Recombinant

    Casein Kinase 2, Alpha Prime Polypeptide, CK II Alpha, EC 2.7.11.1, CK2A2, EC 2.7.11, CSNK2A1, Casein kinase II subunit alpha'.

    Product # :

    PKA-042

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    Description

    CSNK2A2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 374 amino acids (1-350 a.a) and having a molecular mass of 43.7kDa. CSNK2A2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CSNK2A2 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.

    More Info

    • Introduction

      Casein kinase 2 subunit alpha (CSNK2A2) controls numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. CSNK2A2 protein functions as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response.

    • Synonyms

      Casein Kinase 2, Alpha Prime Polypeptide, CK II Alpha, EC 2.7.11.1, CK2A2, EC 2.7.11, CSNK2A1, Casein kinase II subunit alpha'.

    • 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 MGSHMPGPAA GSRARVYAEV NSLRSREYWD YEAHVPSWGN QDDYQLVRKL GRGKYSEVFE AINITNNERV VVKILKPVKK KKIKREVKIL ENLRGGTNII KLIDTVKDPV SKTPALVFEY INNTDFKQLY QILTDFDIRF YMYELLKALD YCHSKGIMHR DVKPHNVMID HQQKKLRLID WGLAEFYHPA QEYNVRVASR YFKGPELLVD YQMYDYSLDM WSLGCMLASM IFRREPFFHG QDNYDQLVRI AKVLGTEELY GYLKKYHIDL DPHFNDILGQ HSRKRWENFI HSENRHLVSP EALDLLDKLL RYDHQQRLTA KEAMEHPYFY PVVKEQSQPC ADNAVLSSGL TAAR.

    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.

    Csnk2A2 Human
  • View Data Sheet

    Name :

    Activin A Human Plant

    Description:

    Activin A Human Recombinant, Plant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-052

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    Description

    Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 27.4 kDa.
      What is the source or expression system of Activin A Protein?
      Nicotinia

      What is the Purity of Activin A Protein?
      Activin A Protein is >97% pure as determined by SDS-PAGE.

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

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

      What is the amino acid sequence of ACTIVIN A Protein?
      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

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

    • Serological Identification

      The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin A.

    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.

    Activin A Human Plant
  • View Data Sheet

    Name :

    HK3 Human

    Description:

    Hexokinase-3 Human Recombinant

    Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.

    Product # :

    PKA-229

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    Description

    HK-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain fused to His tag at the N-terminal encoding the sequence of 943 amino acids and having a molecular mass of 101.1 kDa.HXK3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris pH 8.0 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. HK3 encodes hexokinase 3. Similar to hexokinases 1 and 2, this allosteric enzyme is inhibited by its product glucose-6-phosphate. Hexokinase3 lacks the hydrophobic N-terminal sequence critical for targeting to mitochondria. Hexpkinase3 may have anabolic functions, providing H6P for glycogen or lipid synthesis.

    • Synonyms

      Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.

    • 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). Please avoid freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MDSIGSSGLR QGEETLSCSE EGLPGPSDSSE LVQECLQQFKVTRAQLQQI QASLLGSMEQ ALRGQASPAP AVRMLPTYVG STPHGTEQGD FVVLELGATG ASLRVLWVTL TGIEGHRVEP RSQEFVIPQE VMLGAGQQLF DFAAHCLSEF LDAQPVNKQGLQLGFSFSFP CHQTGLDRST LISWTKGFRC SGVEGQDVVQ LLRDAIRRQG AYNIDVVAVV NDTVGTMMGC EPGVRPCEVG LVVDTGTNAC YMEEARHVAV LDEDRGRVCV SVEWGSFSDD GALGPVLTTF DHTLDHESLN PGAQRFEKMI GGLYLGELVR LVLAHLARCG VLFGGCTSPA LLSQGSILLE HVAEMEDPST GAARVHAILQ DLGLSPGASD VELVQHVCAA VCTRAAQLCA AALAAVLSCL QHSREQQTLQ VAVATGGRVC ERHPRFCSVL QGTVMLLAPE CDVSLIPSVDGGGRGVAMVT AVAARLAAHR RLLEETLAPF RLNHDQLAAV QAQMRKAMAK GLRGEASSLR MLPTFVRATP DGSERGDFLA LDLGGTNFRV LLVRVTTGVQ ITSEIYSIPE TVAQGSGQQL FDHIVDCIVD FQQKQGLSGQ SLPLGFTFSF PCRQLGLDQG ILLNWTKGFK ASDCEGQDVV SLLREAITRR QAVELNVVAI VNDTVGTMMS CGYEDPRCEI GLIVGTGTNA CYMEELRNVAGVPGDSGRMC INMEWGAFGD DGSLAMLSTR FDASVDQASI NPGKQRFEKM ISGMYLGEIV RHILLHLTSL GVLFRGQQIQ RLQTRDIFKT KFLSEIESDS LALRQVRAIL EDLGLPLTSDDALMVLEVCQ AVSQRAAQLC GAGVAAVVEK IRENRGLEEL AVSVGVDGTL YKLHPRFSSL VAATVRELAP RCVVTFLQSE DGSGKGAALV TAVACRLAQL TRV.

    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.

    Hk3 Human
  • View Data Sheet

    Name :

    IDNK E.Coli

    Description:

    Thermosensitive Gluconokinase E.Coli Recombinant

    Thermosensitive gluconokinase, Gluconate kinase 1, idnK.

    Product # :

    PKA-060

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    Description

    IDNK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187 a.a) and having a molecular mass of 23.4kDa. IDNK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IDNK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thermosensitive Gluconokinase, also known as IDNK is a 187 a.a protein which is a member of the gluconokinase gntK/gntV family. IDNK catalyzes theconversion of ATP and D-gluconate to ADP and 6-phospho-D-gluconate. In addition, IDNK is considered to take part in gender determination, deletion of the distal portion of 9p is able to lead to a development of male to female sex reversal, the phenotype of a female with a male X, Y genotype.

    • Synonyms

      Thermosensitive gluconokinase, Gluconate kinase 1, idnK.

    • 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 MGSMAGESFI LMGVSGSGKT LIGSKVAALL SAKFIDGDDL HPAKNIDKMS QGIPLSDEDR LPWLERLNDA SYSLYKKNET GFIVCSSLKK QYRDILRKGS PHVHFLWLDG DYETILARMQ RRAGHFMPVA LLKSQFEALE RPQADEQDIV RIDINHDIAN VTEQCRQAVL AIRQNRICAK EGSASDQRCE.

    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.

    Idnk Ecoli
  • View Data Sheet

    Name :

    Stratifin Human

    Description:

    Tyr-3/Trp- 5 Monooxygenase Activation Protein Sigma Human Recombinant

    14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.

    Product # :

    PKA-357

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    Description

    Stratifin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids (1-248) and having a molecular mass of 27.7 kDa. Stratifin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Stratifin solution containing 20mM Tris-HCl pH-8, 50mM NaCl and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stratifin is part of the 14-3-3 family. The 14-3-3 family of proteins plays an important regulatory function in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are 7 isoforms, beta, gamma, epsilon, sigma, zeta, tau and eta that have been identified in mammals. Stratifin is an epithelial cell marker that functions as a tumor suppressor whose expression can be down regulated via methylation. Failure of Stratifin expression results in a defective G2/M phase checkpoint and results in epithelial and non-epithelial tumorigenesis.

    • Synonyms

      14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.

    • 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

      MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS.

    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.

    Stratifin Human
  • View Data Sheet

    Name :

    STXBP6 Human

    Description:

    Syntaxin Binding Protein 6 Human Recombinant

    Syntaxin-binding protein 6, Amisyn, STXBP6, HSPC156, Syntaxin Binding Protein 6.

    Product # :

    PRO-2056

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    Description

    STXBP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a.) and having a molecular mass of 25.9kDa.STXBP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STXBP6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Syntaxin-binding protein 6 (STXBP6) binds components of the SNARE complex and takes part in regulating SNARE complex configuration. STXBP6 forms non-fusogenic complexes with SNAP25 and STX1A and modulates the formation of SNARE complexes and exocytosis.

    • Synonyms

      Syntaxin-binding protein 6, Amisyn, STXBP6, HSPC156, Syntaxin Binding Protein 6.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSAKSAI SKEIFAPLDE RMLGAVQVKR RTKKKIPFLA TGGQGEYLTY ICLSVTNKKP TQASITKVKQ FEGSTSFVRR SQWMLEQLRQ VNGIDPNGDS AEFDLLFENA FDQWVASTAS EKCTFFQILH HTCQRYLTDR KPEFINCQSK IMGGNSILHS AADSVTSAVQ KASQALNERG ERLGRAEEKT EDLKNSAQQF AETAHKLAMK HKC.

    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.

    Stxbp6 Human
  • View Data Sheet

    Name :

    KLK10 Human

    Description:

    Kallikrein-10 Human Recombinant

    Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    Product # :

    ENZ-795

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    Description

    KLK10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (34-276) and having a molecular mass of 29.1kDa.KLK10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KLK10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.

    • Synonyms

      Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    • 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 MGSALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSN.

    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.

    Klk10 Human
  • View Data Sheet

    Name :

    CINP Human

    Description:

    Cyclin-Dependent Kinase 2 Interacting Protein Human Recombinant

    Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    Product # :

    PKA-269

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    Description

    CINP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.4 kDa.The CINP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CINP protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.

    • Synonyms

      Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    • Physical Appearance

      CINP is supplied as a 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 MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLLN KDKIELDSSS PASKENEEKV CLEYNEELEK LCEELQATLD GLTKIQVKME KLSSTTKGIC ELENYHYGEE SKRPPLFHTW PTTHFYEVSH KLLEMYRKEL LLKRTVAKEL AHTGDPDLTL SYLSMWLHQP YVESDSRLHL ESMLLETGHR AL

    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.

    Cinp Human
  • View Data Sheet

    Name :

    CKS2 Human

    Description:

    CDC28 Protein Kinase 2 Human Recombinant

    CDC28, CKSHS2, CKS2, CDC28 Protein Kinase 2.

    Product # :

    PKA-258

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    Description

    CKS2 Human Recombinant fused to T7-Tag produced in E.Coli is a single, non- glycosylated polypeptide chain containing 94 amino acids and having a molecular mass of 11 kDa.

    Source

    Escherichia Coli.

    Formulation

    The CKS2 protein solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CKS2 protein binds to the catalytic subunit of the cyclin dependent kinases and is necessary for their biological function. The CKS2 mRNA is expressed in various patterns through the cell cycle in HeLa cells, which shows spcific role for the encoded protein. CKS2 (CDC28) Protein kinase 2 binds to the catalytic subunit of cyclin-dependent kinases and has thus in involved in cell cycle regulation. CKS2 is required for the first metaphase/anaphase transition during the meiosis. An increase in expression of CKS2 protects the cells from apoptosis. CKS2 is essential during early embryogenesis and cell cycle progression in somatic cells.

    • Synonyms

      CDC28, CKSHS2, CKS2, CDC28 Protein Kinase 2.

    • 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

      MASMTGGQQM GRGSHMAHKQ IYYSDKYFDE HYEYRHVMLP RELSKQVPKT HLMSEEEWRRLGVQQSLGWV HYMIHEPEPH ILLFRRPLPK DQQ.

    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.

    Cks2 Human
  • View Data Sheet

    Name :

    UPK2 Human

    Description:

    Uroplakin 2 Human Recombinant

    Uroplakin-2, UP2, Uroplakin II, UPII, UPK2.

    Product # :

    PRO-479

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    Description

    UPK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (26-155 a.a) and having a molecular mass of 16.2kDa.UPK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UPK2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M UREA and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Uroplakin 2 (UPK2) is one of the proteins of the highly urothelium-specific integral membrane proteins of the asymmetric unit membrane which forms urothelium apical plaques in mammals. The asymmetric unit membrane is thought to strengthen the urothelium by preventing cell rupture during bladder distention. The UPK2 protein is expressed in the peripheral blood of bladder cancer patients with transitional cell carcinomas.

    • Synonyms

      Uroplakin-2, UP2, Uroplakin II, UPII, UPK2.

    • 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 MGSDFNISSL SGLLSPALTE SLLVALPPCH LTGGNATLMV RRANDSKVVT SSFVVPPCRG RRELVSVVDS GAGFTVTRLS AYQVTNLVPG TKFYISYLVK KGTATESSRE IPMSTLPRRN MESIGLGMAR TGG.

    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.

    Upk2 Human
  • View Data Sheet

    Name :

    Clusterin Human, His

    Description:

    Apolipoprotein-J Human Recombinant, His Tag

    CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.

    Product # :

    CYT-814

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    • sds-page

    Description

    Clusterin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 463 amino acids (23-449 a.a.) and having a molecular mass of 54.1kDa. Clusterin is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Clusterin protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    Clusterin-sds-page - Product image 1

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 54.1kDa.

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

      What is the Purity of CLUSTERIN Protein?
      CLUSTERIN Protein is >85% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of CLUSTERIN Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.

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

      What is the endotoxin level for CLUSTERIN Protein?
      The endotoxin level is minimal, CLUSTERIN 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.

    Clusterin Human His
  • View Data Sheet

    Name :

    IL 7 Human, HEK

    Description:

    Interleukin-7 Human Recombinant, HEK

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-197

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    Description

    IL-7 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 19-30kDa due to glycosylation.The IL-7 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The IL7 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.

    More Info

    • Introduction

      IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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-7 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    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 7 Human Hek
  • View Data Sheet

    Name :

    Thymosin β4

    Description:

    Thymosin-b4 Human Recombinant

    Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.

    Product # :

    HOR-003

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    Shipped at Room temp

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    • description
    • source
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    Description

    Thymosin b4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 43 amino acids and having a molecular mass of 4.9kDa.The Thymosin b4 Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2um filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    More Info

    • Introduction

      CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.

    • Synonyms

      Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin B4 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymosin B4 Human should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Thymosin B4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES

    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.

    Thymosin B4
  • View Data Sheet

    Name :

    NEUROG3 Human

    Description:

    Neurogenin 3 Human Recombinant

    Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.

    Product # :

    CYT-811

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    Shipped with Ice Packs

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    Description

    NEUROG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-214) and having a molecular mass of 25.1 kDa. NEUROG3 is fused to a 20 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The NEUROG3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      NEUROG3 is a common helix-loop-helix (bHLH) transcription factor which takes part in neurogenesis. NEUROG3 functions as a heterodimer with another bHLH protein. Mutations in this gene can result in congenital malabsorptive diarrhea 4 (DIAR4).

    • Synonyms

      Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.

    • 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 MTPQPSGAPT VQVTRETERS FPRASEDEVT CPTSAPPSPT RTRGNCAEAE EGGCRGAPRK LRARRGGRSR PKSELALSKQ RRSRRKKAND RERNRMHNLN SALDALRGVL PTFPDDAKLT KIETLRFAHN YIWALTQTLR IADHSLYALE PPAPHCGELG SPGGSPGDWG SLYSPVSQAG SLSPAASLEE RPGLLGATSS ACLSPGSLAF SDFL

    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.

    Neurog3 Human
  • View Data Sheet

    Name :

    STX12 Human

    Description:

    Syntaxin-12 Human Recombinant

    Syntaxin 12, STX13, STX14.

    Product # :

    PRO-1099

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    Description

    STX12 Human Recombinant produced in E. coli is a single polypeptide chain containing 272 amino acids (1-248) and having a molecular mass of 31.0kDa.STX12 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The STX12 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      STX12 is a member of the syntaxin family which are cellular receptors for transport of vesicles that take part in exocytosis in neutrophils. STX12 regulates protein transport from late endosomes and the trans-Golgi network and back. Additionally, STX12 cooperates with ABC1 (ATP-binding cassette transporter A1), which enables cellular release of cholesterol and choline-phospholipids to apoA-I (apolipoprotein A-I).

    • Synonyms

      Syntaxin 12, STX13, STX14.

    • 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 MGSHMSYGPL DMYRNPGPSG PQLRDFSSII QTCSGNIQRI SQATAQIKNL MSQLGTKQDS SKLQENLQQL QHSTNQLAKE TNELLKELGS LPLPLSTSEQ RQQRLQKERL MNDFSAALNN FQAVQRRVSE KEKESIARAR AGSRLSAEER QREEQLVSFD SHEEWNQMQS QEDEVAITEQ DLELIKERET AIRQLEADIL DVNQIFKDLA MMIHDQGDLI DSIEANVESS EVHVERATEQ LQRAAYYQKK SR

    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.

    Stx12 Human
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