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  • MEC (CCL28)

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Search results

1000 results found for “cntf”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CFB-a Human

    Description:

    Complement Factor B Fragment a Human

    Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    Product # :

    PRO-2735

    Price :

    Quantity :

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    Description

    CFB-a Human produced in Human Plasma having a molecular mass of 33 kDa.

    Source

    Human Plasma.

    Formulation

    CFB-a solution (1mg/ml) contains Phosphate-buffered saline, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

    • Synonyms

      Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFB-a Human is stable at 4°C if entire vial will be used within 2-4 weeks. Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

    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.

    Cfb Protein
  • View Data Sheet

    Name :

    EIF4E Human

    Description:

    Eukaryotic Translation Initiation Factor 4E Human Recombinant

    CBP, EIF4E1, EIF4EL1, EIF4F.

    Product # :

    PRO-530

    Price :

    Quantity :

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    Description

    EIF4E Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular weight of 27.2kDa. The EIF4E is fused to a 20 aa His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF4E 0.5mg/ml protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.

    • Synonyms

      CBP, EIF4E1, EIF4EL1, EIF4F.

    • 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 MATVEPETTP TPNPPTTEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL RLISKFDTVE
      DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG
      DKIAIWTTEC ENREAVTHIG RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV.

    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.

    Eif4E Human
  • 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

    Price :

    Quantity :

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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.

    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.

    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.

    Flt4 Human
  • View Data Sheet

    Name :

    VEGF Rat

    Description:

    Vascular Endothelial Growth Factor Rat Recombinant

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-392

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    • purity
    • biological activity
    • More Info

    Description

    Vascular Endothelial Growth Factor Rat Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38,750 Dalton. The VEGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 10mM NaP, pH 7.5.

    Purity

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

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 4.0-8.0 ng/ml.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAPTTEGEQK AHEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNVTMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

    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.

    Vegf Rat
  • View Data Sheet

    Name :

    PNMT Human

    Description:

    Phenylethanolamine-N-Methyltransferase Human Recombinant

    PENT, PNMTase, Noradrenaline-N-methyltransferase, Phenylethanolamine N-methyltransferase, PNMT, MGC34570.

    Product # :

    ENZ-457

    Price :

    Quantity :

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    • description
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    Description

    Recombinant Human PNMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 282 amino acids (1-282 a.a.) and having a molecular mass of 30.8 kDa.PNMT is purified by conventional chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PNMT protein solution contains 20mM Tris-HCl, pH-8 & 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PNMT is an enzyme located in the adrenal medulla and it catalyzes the final step of the catecholamine biosynthesis pathway. PNMT has beta-carboline 2N-methyltransferase activity. PNMT takes part in regulating epinephrine production. Glucocorticoid receptors form multimers of PNMT independent of the DNA binding domain. PNMT expression is regulated late in mouse gestation by AP2-alpha and glucocorticoids.

    • Synonyms

      PENT, PNMTase, Noradrenaline-N-methyltransferase, Phenylethanolamine N-methyltransferase, PNMT, MGC34570.

    • 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

      MSGADRSPNA GAAPDSAPGQ AAVASAYQRF EPRAYLRNNY APPRGDLCNP NGVGPWKLRC LAQTFATGEV SGRTLIDIGS GPTVYQLLSA CSHFEDITMT DFLEVNRQEL GRWLQEEPGA FNWSMYSQHA CLIEGKGECW QDKERQLRAR VKRVLPIDVH QPQPLGAGSP APLPADALVS AFCLEAVSPD LASFQRALDH ITTLLRPGGH LLLIGALEES WYLAGEARLT VVPVSEEEVR EALVRSGYKV RDLRTYIMPA HLQTGVDDVK GVFFAWAQKV GL.

    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.

    Pnmt Human
  • View Data Sheet

    Name :

    RNF34 Human

    Description:

    Ring Finger Protein 34 Human Recombinant

    Ring Finger Protein 34, E3 Ubiquitin Protein Ligase, RING Finger Protein 34, Caspase Regulator CARP1, Caspases-8 And -10-Associated RING Finger Protein 1, FYVE-RING Finger Protein Momo, Human RING Finger Homologous To Inhibitor Of Apoptosis Protein, CARP-1, hRFI, RING Finger Protein RIFF, RFI, CARP1, RIF, RIFF, E3 Ubiquitin-Protein Ligase RNF34, EC 6.3.2.

    Product # :

    PRO-1761

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    Description

    RNF34 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.2kDa.RNF34 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNF34 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ring Finger Protein 34 (RNF34) has E3 ubiquitin-protein ligase activity. RNF34 has a RINF finger, a motif recognized to be involved in protein-protein and protein-DNA interactions. RNF34 regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. In addition, RNF34 protects cells against apoptosis induced by TNF. RNF34 also binds phosphatidylinositol 5-phosphateand phosphatidylinositol 3-phosphate. Alternatively splicing results in multiple transcript variants encoding distinct isoforms.

    • Synonyms

      Ring Finger Protein 34, E3 Ubiquitin Protein Ligase, RING Finger Protein 34, Caspase Regulator CARP1, Caspases-8 And -10-Associated RING Finger Protein 1, FYVE-RING Finger Protein Momo, Human RING Finger Homologous To Inhibitor Of Apoptosis Protein, CARP-1, hRFI, RING Finger Protein RIFF, RFI, CARP1, RIF, RIFF, E3 Ubiquitin-Protein Ligase RNF34, EC 6.3.2.

    • 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 MGS MRKAGAT SMWASCCGLL NEVMGTGAVR GQQSAFAGAT GPFRFTPNPE FSTYPPAATE GPNIVCKACG LSFSVFRKKH VCCDCKKDFC SVCSVLQENL RRCSTCHLLQ ETAFQRPQLM RLKVKDLRQY LILRNIPIDT CREKEDLVDL VLCHHGLGSE DDMDTSSLNS SRSQTSSFFT RSFFSNYTAP SATMSSFQGE LMDGDQTSRS GVPAQVQSEI TSANTEDDDD DDDEDDDDEE ENAEDRNPGL SKERVRASLS DLSSLDDVEG MSVRQLKEIL ARNFVNYSGC CEKWELVEKV NRLYKENEEN QKSYGERLQL QDEEDDSLCR ICMDAVIDCV LLECGHMVTC TKCGKRMSEC PICRQYVVRA VHVFKS

    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.

    Rnf34 Human
  • View Data Sheet

    Name :

    RNF4 Human

    Description:

    Ring Finger Protein 4 Human Recombinant

    E3 ubiquitin-protein ligase RNF4, RING finger protein 4, Small nuclear ring finger protein, Protein SNURF, RNF4, SNURF, RES4-26, SLX5.

    Product # :

    PRO-1255

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    Description

    RNF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a) and having a molecular mass of 23.7kDa.RNF4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNF4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      E3 ubiquitin ligase RNF4 (RNF4) contains a RING finger motif and functions as a transcription regulator. RNF4 interacts with, and inhibits the activity of, TRPS1, a transcription suppressor of GATA-mediated transcription. Transcription repressor ZNF278/PATZ also interacts with the RNF4 protein thus reducing the enhancement of androgen receptor-dependent transcription mediated by RNF4. RNF4 is broadly expressed at low levels in many tissues and highly expressed in the testis.

    • Synonyms

      E3 ubiquitin-protein ligase RNF4, RING finger protein 4, Small nuclear ring finger protein, Protein SNURF, RNF4, SNURF, RES4-26, SLX5.

    • 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 MGSMSTRKRR GGAINSRQAQ KRTREATSTP EISLEAEPIE LVETAGDEIV DLTCESLEPV VVDLTHNDSV VIVDERRRPR RNARRLPQDH ADSCVVSSDD EELSRDRDVY VTTHTPRNAR DEGATGLRPS GTVSCPICMD GYSEIVQNGR LIVSTECGHV FCSQCLRDSL KNANTCPTCR KKINHKRYHP IYI.

    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.

    Rnf4 Human
  • View Data Sheet

    Name :

    TGFB1 Human, HEK

    Description:

    Transforming Growth Factor-Beta 1 Human Recombinant, HEK

    Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

    Product # :

    CYT-1260

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    Description

    TGFB1 Human Recombinant produced in 293 cells is a glycosylated homodimer polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.0kDa. The TGFB1 is purified by proprietary chromatographic techniques.

    Source

    HEK 293 cells.

    Formulation

    Lyophilized from a sterile filtered solution containing TFA (0.1%).

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 107 units/mg.

    More Info

    • Synonyms

      Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human 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 TGFB1 in sterile in 18MΩ-cm H2O at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.

    • Background

      Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

    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.

    Tgf Beta 1 Hek
  • View Data Sheet

    Name :

    TGFB2 Rat

    Description:

    Transforming Growth Factor-Beta 2 Rat Recombinant

    Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.

    Product # :

    CYT-1267

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    Description

    Transforming Growth Factor-Beta 2 Rat Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
    TGFB2 Rat Recombinant is purified by proprietary chromatographic techniques.

    Source

    CHO Cells.

    Formulation

    The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

    Purity

    Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

    Biological Activity

    The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

    More Info

    • Synonyms

      Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 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 Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.

    • Background

      Rat TGFB22 signals through TGFBR2, TGFBR1 using an accessory co-receptor TGFBR3 (betaglycan) that enhances presentation of TGFβ2
      Rat TGFB2 is a potent inducer of epithelial–mesenchymal transition (EMT) therefore is used in Cancer metastasis, Fibrosis, Retinal disorders, Developmental biology and Wound healing

      What is the source or expression system of Rat TGFB2 Protein?
      CHO Cells

      What is the Purity of Rat TGFB2 Protein?
      Rat TGFB2 Protein is >97% pure as determined by SDS-PAGE.

      What is the molecular weight / Mw of Rat TGFB2 Protein?
      Rat TGFB2 Protein having a total Mw of 25.6kDa.

      What is the Biological Activity of Rat TGFB2 Protein?
      The biological functionality of Rat TGFB2 Protein is determined by mouse HT-2 cells.

      What is the endotoxin level for Rat TGFB2 Protein?
      The endotoxin level is minimal, Rat TGFB2 Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of Rat TGF beta 2 Protein?
      If there is sequence put it instead of the sentence

      Is TGFB2 a homodimer / homodimeric protein?
      Yes, TGFB1 is homo dimer consisting of 2 identical chains.

    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.

    tgfb2 rat
  • View Data Sheet

    Name :

    HB-EGF Human

    Description:

    HB-EGF Human Recombinant

    HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    Product # :

    CYT-119

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    Description

    HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

    More Info

    • Introduction

      HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

    • Synonyms

      HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC

      KYVKELRAPS CICHPGYHGE RCHGLSL.

    • Background

      What is the molecular weight/Mw of HB-EGF Protein?
      HB-EGF Protein has a total Mw of 9.9kDa.

      What is the source or expression system of HB-EGF Protein?
      Escherichia Coli.

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

      What is the Biological Activity of HB-EGF Protein?
      The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

      What is the amino acid sequence of HB-EGF Protein?
      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
      KYVKELRAPS CICHPGYHGE RCHGLSL.

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

      What is the endotoxin level for HB-EGF Protein?
      The endotoxin level is minimal, HB-EGF 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.

    Hb Egf Human
  • View Data Sheet

    Name :

    TWF1 Human

    Description:

    Twinfilin-1 Human Recombinant

    Twinfilin-1, Protein A6, Protein tyrosine kinase 9, TWF1, PTK9.

    Product # :

    PRO-1003

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    Description

    TWF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-252 a.a.) and having a molecular mass of 31.5kDa. TWF1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TWF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Twinfilin (TWF1) is a ubiquitous actin-monomer-binding protein which is composed of two ADF-homology domains. Twinfilin forms a 1:1 complex with ADP-actin-monomers, prevents nucleotide exchange on actin monomers and blocks assembly of the monomer into filaments. TWF1 is composed of 2 ADF/cofilin-like (ADF-H) domains joined by a short linker region and followed by a C-terminal tail of approximately 20 residues. The 2 ADF-H domains are approximately 20% homologous to ADF/cofilin and to each other. TWF1 protein may be an actin monomer-binding protein, and its localization to cortical G-actin-rich structures might be regulated by the small GTPase RAC1.

    • Synonyms

      Twinfilin-1, Protein A6, Protein tyrosine kinase 9, TWF1, PTK9.

    • 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 MGSHMMLYAA TRATLKKEFG GGHIKDEVFG TVKEDVSLHG YKKYLLSQSS PAPLTAAEEE LRQIKINEVQ TDVGVDTKHQ TLQGVAFPIS REAFQALEKL NNRQLNYVQL EIDIKNEIII LANTTNTELK DLPKRIPKDS ARYHFFLYKH SHEGDYLESI VFIYSMPGYT CSIRERMLYS SCKSRLLEIV ERQLQMDVIR KIEIDNGDEL TADFLYEEVH PKQHAHKQSF AKPKGPAGKR GIRRLIRGPA ETEATTD.

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    Twf1 Human
  • View Data Sheet

    Name :

    HIV-1 CRF

    Description:

    HIV-1 Circulating Recombinant Form

    Product # :

    HIV-008

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    Description

    HIV-1 CRF Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids and having a molecular mass of 20.1kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized with 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HIV-1 circulating recombinant forms (CRFs) are part of viral recombinant lineages that play a major role in the global epidemic. HIV-1 CRF is 1 of 2 genes which dominate the epidemic in Burkina Faso. Multiple HIV-1 subtypes and circulating recombinant forms are known to cocirculate in Africa. In West Africa, the high prevalence of HIV-1 CRFand cocirculation of subtype Aand other complex intersubtype recombinants has been highly documented. Cocirculation of HIV-1 CRFstrain with other genetic subtypes may lead to novel and complex HIV-1 recombinants.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized HIV-1 CRF although stable at room temperature for 1 week, should be stored desiccated below -18°C. Upon reconstitution HIV-1 CRF 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 HIV-1 CRF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Applications

      Western Blotting, SDS Page

    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.

    Hiv 1 Crf
  • View Data Sheet

    Name :

    CANX Human

    Description:

    Calnexin Human Recombinant

    Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.

    Product # :

    PRO-725

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    Description

    CANX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 462 amino acids (21-481 a.a.) and having a molecular mass of 52.5kDa.The CANX is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CANX protein solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calnexin (CANX) belongs to the calnexin family of molecular chaperones. Calnexin is a calcium-binding, ER-associated protein that interacts briefly with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Calnexin grants long-term protection of wild-type Shaker protein from ER-associated degradation. Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.

    • Synonyms

      Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.

    • 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

      MHDGHDDDVI DIEDDLDDVI EEVEDSKPDT TAPPSSPKVT YKAPVPTGEV YFADSFDRGT LSGWILSKAK KDDTDDEIAK YDGKWEVEEM KESKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTPELNLDQF HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGIYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIPDPEAV KPDDWDEDAP AKIPDEEATK PEGWLDDEPE YVPDPDAEKP EDWDEDMDGE WEAPQIANPR CESAPGCGVW QRPVIDNPNY KGKWKPPMID NPSYQGIWKP RKIPNPDFFE DLEPFRMTPF SAIGLELWSM TSDIFFDNFI ICADRRIVDD WANDGWGLKK AADGAAEPGV VGQMIEAAEE RP.

    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.

    Canx Human
  • View Data Sheet

    Name :

    CFL1 Human

    Description:

    Cofilin-1 Human Recombinant

    CFL-1, CFL1, Cofilin1, Cofilin-1, Cofilin, non-muscle isoform, 18 kDa phosphoprotein, p18.

    Product # :

    PRO-591

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    Description

    Cofilin1 Human Recombinant (aa 1-166) fused to a 20 aa N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 186 amino acids and having a molecular mass of 20kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Cofilin is a family of actin-binding proteins which disassembles actin filaments. It is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.

    • Synonyms

      CFL-1, CFL1, Cofilin1, Cofilin-1, Cofilin, non-muscle isoform, 18 kDa phosphoprotein, p18.

    • 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 prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCLSEDKKNIILE EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLVFIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL.

    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.

    Cfl1 Human
  • View Data Sheet

    Name :

    CNDP2 Human

    Description:

    CNDP Dipeptidase 2 Human Recombinant

    Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.

    Product # :

    ENZ-681

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    Description

    CNDP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 498 amino acids (1-475) and having a molecular mass of 55.3 kDa. CNDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CNDP2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CNDP Dipeptidase 2 (CNDP2), is a cytosolic, non-specific dipeptidase which is a part of the peptidase M20A protein family. CNDP2 is a secreted peptidase homologous to M20 peptidases. CNDP2 expresses through all adult and fetal tissue, though, an isoform missing exons 3 and 4 expresses in all fetal tissue in adult liver. Over expression of CPGL-B in hepatocellular carcinoma cells results in significant inhibition of HC cell viability, colony formation, cell invasiveness and tumor configuration.

    • Synonyms

      Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.

    • 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 MGSMAALTTL FKYIDENQDR YIKKLAKWVA IQSVSAWPEK RGEIRRMMEV AAADVKQLGG SVELVDIGKQ KLPDGSEIPL PPILLGRLGS DPQKKTVCIY GHLDVQPAAL EDGWDSEPFT LVERDGKLYG RGSTDDKGPV AGWINALEAY QKTGQEIPVN VRFCLEGMEE SGSEGLDELI FARKDTFFKD VDYVCISDNY WLGKKKPCIT YGLRGICYFF IEVECSNKDL HSGVYGGSVH EAMTDLILLM GSLVDKRGNI LIPGINEAVA AVTEEEHKLY DDIDFDIEEF AKDVGAQILL HSHKKDILMH RWRYPSLSLH GIEGAFSGSG AKTVIPRKVV GKFSIRLVPN MTPEVVGEQV TSYLTKKFAE LRSPNEFKVY MGHGGKPWVS DFSHPHYLAG RRAMKTVFGV EPDLTREGGS IPVTLTFQEA TGKNVMLLPV GSADDGAHSQ NEKLNRYNYI EGTKMLAAYL YEVSQLKD.

    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.

    Cndp2 Human
  • View Data Sheet

    Name :

    VEGF (121 a.a.) Human

    Description:

    Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-343

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    Description

    Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

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

    Biological Activity

    VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 Vascular Endothelial Growth Factor -121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR R

    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.

    Vegf121 Human
  • View Data Sheet

    Name :

    TFB2M Human

    Description:

    Transcription Factor B2, Mitochondrial Human Recombinant

    Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.

    Product # :

    PRO-1259

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    Description

    TFB2M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (20-396 a.a) and having a molecular mass of 45.8kDa.TFB2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TFB2M protein solution (0.5mg/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

      Transcription Factor B2, Mitochondrial (TFB2M) is an S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. In addition, TFB2M is essential for basal transcription of mitochondrial DNA, most likely via its interaction with POLRMT and TFAM. TFB2M promotes transcription independently of the methyltransferase activity. TFB2M like TFB1M, activates transcription of mitochondrial DNA more effectively, whilst having less methyltransferase activity.

    • Synonyms

      Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.

    • 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 MGSMAGRFCI LGSEAATRKH LPARNHCGLS DSSPQLWPEP DFRNPPRKAS KASLDFKRYV TDRRLAETLA QIYLGKPSRP PHLLLECNPG PGILTQALLE AGAKVVALES DKTFIPHLES LGKNLDGKLR VIHCDFFKLD PRSGGVIKPP AMSSRGLFKN LGIEAVPWTA DIPLKVVGMF PSRGEKRALW KLAYDLYSCT SIYKFGRIEV NMFIGEKEFQ KLMADPGNPD LYHVLSVIWQ LACEIKVLHM EPWSSFDIYT RKGPLENPKR RELLDQLQQK LYLIQMIPRQ NLFTKNLTPM NYNIFFHLLK HCFGRRSATV IDHLRSLTPL DARDILMQIG KQEDEKVVNM HPQDFKTLFE TIERSKDCAY KWLYDETLED R.

    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.

    Tfb2M Human
  • View Data Sheet

    Name :

    CTHRC1 Human, HEK

    Description:

    Collagen Triple Helix Repeat Containing 1 Human Recombinant, HEK

    Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.

    Product # :

    PRO-2028

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    Description

    CTHRC1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser31-Lys243) containing a total of 219 amino acids, having a calculated molecular mass of 23.9kDa and fused to a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    CTHRC1 was filtered (0.4µm) and lyophilized in phosphate buffered saline pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Collagen triple helix repeat-containing protein 1 (CTHRC1) functions as a negative regulator of collagen matrix deposition. CTHRC1 is a secreted 28kDa protein which is glycosylated and highly conserved from lower chordates to mammals. CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells. CTHRC1 is detected qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers. The hormonal functions of CTHRC1 include regulation of lipid storage and cellular glycogen levels with potentially far-reaching implications for cell metabolism and physiology. CTHRC1 gene deletion leads to fatty liver (steatosis) formation in mice while others exhibited inactivation of the CTHRC1 gene also results in low bone mass.

    • Synonyms

      Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. CTHRC1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      SEIPKGKQKA QLRQREVVDL YNGMCLQGPA GVPGRDGSPG ANGIPGTPGI PGRDGFKGEK GECLRESFEE SWTPNYKQCS WSSLNYGIDL GKIAECTFTK MRSNSALRVL FSGSLRLKCR NACCQRWYFT FNGAECSGPL PIEAIIYLDQ GSPEMNSTIN IHRTSSVEGL CEGIGAGLVD VAIWVGTCSD YPKGDASTGW NSVSRIIIEE LPK HHHHHH.

    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.

    Cthrc1 Human Hek
  • View Data Sheet

    Name :

    AITRL Human, T7

    Description:

    AITRL Human Recombinant, T7 Tag

    Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

    Product # :

    CYT-807

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    Description

    AITRL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (81-199 a.a) and having a molecular mass of 15kDa.AITRL is fused to a 15 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Osteostat is the cytokine that binds to TNFRSF18/AITR/GITR and is important for interactions between activated T-lymphocytes and endothelial cells and may modulate T-lymphocyte survival in peripheral tissues. Osteostat is expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells after stimulation by lipopolysaccharides.
      Osteostat protein is detectable in human microvascular EC and is highly up-regulated by IFN-alpha and IFN-beta. Osteostat inhibit differentiation of osteoclasts from monocytic precursor cells. Osteostat suppresses the early stage of osteoclastogenesis via inhibition of macrophage colony-stimulating factorinduced receptor activator of NF-kappaB (RANK) expression in the osteoclast precursor cells. Osteostat does not inhibit lipopolysaccharide-induced RANK expression in monocytes and dendritic cells, or activation-induced RANK expression in T cells. Osteostat is a novel regulator of osteoclast generation and substantiate the major role played by the endothelium in bone physiology.

    • Synonyms

      Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

    • 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 GRGSHMAKFG PLPSKWQMAS SEPPCVNKVS DWKLEILQNG LYLIYGQVAP NANYNDVAPF EVRLYKNKDM IQTLTNKSKI QNVGGTYELH VGDTIDLIFN SEHQVLKNNT YWGIILLANP QFIS.

    • Background

      What is the molecular weight/Mw of AITRL Protein?
      AITRL Protein has a total Mw of 15kDa.

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

      What is the Purity of AITRL Protein?
      AITRL Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of AITRL Protein?
      MASMTGGQQM GRGSHMAKFG PLPSKWQMAS SEPPCVNKVS DWKLEILQNG LYLIYGQVAP NANYNDVAPF EVRLYKNKDM IQTLTNKSKI QNVGGTYELH VGDTIDLIFN SEHQVLKNNT YWGIILLANP QFIS.

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

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

    Aitrl Human T7
  • View Data Sheet

    Name :

    EOGT Mouse

    Description:

    EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase Mouse Recombinant

    EGF domain-specific O-linked N-acetylglucosamine transferase, Extracellular O-linked N-acetylglucosamine transferase.

    Product # :

    ENZ-946

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    Description

    EOGT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 516 amino acids (20-527 a.a.) and having a molecular mass of 60.4kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). EOGT is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EOGT protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase (EOGT) takes part in the regulation of Notch receptor. EOGT catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine/ threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). EOGT mainly glycosylates the Thr residue positioned between the fifth and sixth conserved cysteines of folded EGF-like domains.

    • Synonyms

      EGF domain-specific O-linked N-acetylglucosamine transferase, Extracellular O-linked N-acetylglucosamine transferase.

    • 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

      DKAHSEADDA PGKALYDYSS LRLPAEHIPF FLHNNRHVAS VCREDSHCPY KKHLENLNYC WGYEKSCAPE FRFGSPVCSY VDLGWTDTLE SAQDMFWRQA DFGYARERLG EIRTICQPER ASDSSLVCSR YLQYCRATGL YLDLRNIKRN HDRFKEDFLQ GGEIGGYCKL DSHALVSEGQ RKSPLQSWFA ELQGYTQLNF RPIEDAKCDI VVEKPTYFMK LDAGINMYHH FCDFLNLYLT QHVNNSFSTD VYIVMWDTST YGYGDLFSDT WKAFTDYDVI HLKTYDSKKV CFKEAVFSLL PRMRYGLFYN TPLISGCQNT GLFRAFSQHV LHRLNITQEG PKDGKVRVTI LARSTEYRKI LNQDELVNAL KTVSTFEVRV VDYKYRELGF LDQLRITHNT DIFIGMHGAG LTHLLFLPDW AAVFELYNCE DERCYLDLAR LRGIHYITWR KPSKVFPQDK GHHPTLGEHP KFTNYSFDVE EFMYLVLQAA EHVLQHPQWP FKKKHDELLE HHHHHH.

    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.

    Eogt Mouse
  • View Data Sheet

    Name :

    AITRL Human, His

    Description:

    AITRL Human Recombinant, His Tag

    Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

    Product # :

    CYT-317

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    Description

    AITRL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 50-177) containing a total of 137 amino acids and having a molecular mass of 15.6kDa. The AITRL protein is fused to a 9 aa His Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AITRL protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) & 10% glycerol.

    Purity

    Greater than 85.0% as determined bySDS-PAGE.

    More Info

    • Introduction

      Osteostat is the cytokine that binds to TNFRSF18/AITR/GITR and is important for interactions between activated T-lymphocytes and endothelial cells and may modulate T-lymphocyte survival in peripheral tissues. Osteostat is expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells after stimulation by lipopolysaccharides.
      Osteostat protein is detectable in human microvascular EC and is highly up-regulated by IFN-alpha and IFN-beta. Osteostat inhibit differentiation of osteoclasts from monocytic precursor cells. Osteostat suppresses the early stage of osteoclastogenesis via inhibition of macrophage colony-stimulating factorinduced receptor activator of NF-kappaB (RANK) expression in the osteoclast precursor cells. Osteostat does not inhibit lipopolysaccharide-induced RANK expression in monocytes and dendritic cells, or activation-induced RANK expression in T cells. Osteostat is a novel regulator of osteoclast generation and substantiate the major role played by the endothelium in bone physiology.

    • Synonyms

      Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

    • 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

      MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH.

    • Background

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

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

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH

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

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

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

    Gitrl Human
  • View Data Sheet

    Name :

    KCTD15 Human

    Description:

    Potassium Channel Tetramerisation Domain Containing 15 Human Recombinant

    BTB/POZ domain-containing protein KCTD15, Potassium channel tetramerisation domain containing 15, KCTD15, MGC2628, MGC25497.

    Product # :

    PRO-1002

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    Description

    KCTD15 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 254 amino acids (1-234 a.a) and having a molecular mass of 28.6kDa.KCTD15 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    KCTD15 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      KCTD15 protein is encoded in humans by the KCTD15 gene. KCTD15 is expressed at a high level in the brain and the hypothalamus. The potassium channel KCTD15 was identified as a genetic loci linked to higher than normal BMI in humans along with genes such as GNPDA2, MTCH2, FTO, and TMEM18. SNPs (Single nucleotide polymorphisms) in non-diabetic and diabetic patients showed that FTO was most strongly associated with obesity while MTCH2 and GNPDA2 were still notably associated with higher than normal BMI levels.

    • Synonyms

      BTB/POZ domain-containing protein KCTD15, Potassium channel tetramerisation domain containing 15, KCTD15, MGC2628, MGC25497.

    • 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 MPHRKERPSG SSLHTHGSTG TAEGGNMSRL SLTRSPVSPL AAQGIPLPAQ LTKSNAPVHI DVGSHMYTSS LATLTKYPDS RISRLFNGTE PIVLDSLKQH YFIDRDGEIF RYVLSFLRTS KLLLPDDFKD FSLLYEEARY YQLQPMVREL ERWQQEQEQR RRSRACDCLV VRVTPDLGER IALSGEKALI EEVFPETGDV MCNSVNAGWN QDPTHVIRFP LNGYCRLNSV QDVL.

    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.

    Kctd15 Human
  • View Data Sheet

    Name :

    GNMT Human

    Description:

    Glycine N-methyltransferase Human Recombinant

    Glycine N-methyltransferase, GNMT.

    Product # :

    ENZ-386

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    Description

    GNMT Human Recombinant fused with 20 amino acid His-Tag tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 315 amino acids (1-295 a.a.) and having a molecular mass of 34.9 kDa.The GNMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GNMT solution contains 20mM Tris pH 8.0 & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

    • Synonyms

      Glycine N-methyltransferase, GNMT.

    • 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 MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD.

    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.

    Gnmt Human
  • View Data Sheet

    Name :

    CTDSPL Human

    Description:

    CTD Small Phosphatase-Like Human Recombinant

    CTD small phosphatase-like protein, CTDSP-like, Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3, NIF-like protein, Nuclear LIM interactor-interacting factor 1, NLI-interacting factor 1, Protein YA22, hYA22, RBSP3, Small C-terminal domain phosphatase 3, SCP3, Small CTD phosphatase 3, CTDSPL, C3orf8, NIF1, NIFL, SCP3, YA22, PSR1.

    Product # :

    ENZ-569

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CTDSPL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (82-265) and having a molecular mass of 23.9kDa.CTDSPL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTDSPL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTD small phosphatase-like protein (CTDSPL) specially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the biggest RNA polymerase II subunit POLR2A. CTDSPL negatively regulates RNA polymerase II transcription, probably by directing the transition from initiation/capping to processive transcript elongation. CTDSPL is employed by REST to neuronal genes which contain RE-1 elements, directing to neuronal gene silencing in non-neuronal cells.

    • Synonyms

      CTD small phosphatase-like protein, CTDSP-like, Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3, NIF-like protein, Nuclear LIM interactor-interacting factor 1, NLI-interacting factor 1, Protein YA22, hYA22, RBSP3, Small C-terminal domain phosphatase 3, SCP3, Small CTD phosphatase 3, CTDSPL, C3orf8, NIF1, NIFL, SCP3, YA22, PSR1.

    • 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 MGSHMKYLLP EVTVLDYGKK CVVIDLDETL VHSSFKPISN ADFIVPVEID GTIHQVYVLK RPHVDEFLQR MGQLFECVLF TASLAKYADP VADLLDRWGV FRARLFRESC VFHRGNYVKD LSRLGRELSK VIIVDNSPAS YIFHPENAVP VQSWFDDMTD TELLDLIPFF EGLSREDDVY SMLHRLCNR.

    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.

    Ctdspl Human
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