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Search results

1000 results found for “cntf”

Name

Description

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  • View Data Sheet

    Name :

    CTACK Mouse

    Description:

    CTACK Mouse Recombinant (CCL27)

    C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    Product # :

    CHM-013

    Price :

    Quantity :

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    Shipped at Room temp

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

    Description

    CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM NaCl.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

    More Info

    • Introduction

      CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.

    • Synonyms

      C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

    • Background

      What is the molecular weight/Mw of CTACK MOUSE Protein?
      CTACK MOUSE Protein has a total Mw of 10.9kDa.

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

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

      What is the Biological Activity of CTACK MOUSE Protein?
      The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

      What is the amino acid sequence of CTACK MOUSE Protein?
      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

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

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


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

    Ctack Mouse
  • View Data Sheet

    Name :

    ACSF2 Human

    Description:

    Acyl-CoA Synthetase Family Member 2 Human Recombinant

    Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.

    Product # :

    ENZ-919

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    ACSF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (42-615 a.a) and having a molecular mass of 66.1kDa. ACSF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ACSF2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline pH 7.4 and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acyl-CoA synthetase family member 2, also known as ACSF2 is a member of the ATP-dependent AMP-binding enzyme family. Acyl-CoA synthetases are a family of enzymes which catalyze the thioesterification of fatty acids with coenzymeA to form activated intermediates, which play a basic part in lipid metabolism as well as homeostasis of lipid-related processes. ACSF2 is required for the complex of lipid synthesis, energy production via beta-oxidation, protein acylation and fatty-acid dependent transcriptional regulation. Moreover, ACSF2 is required for fatty acid import into cells by the process of vectorial acylation.

    • Synonyms

      Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.

    • 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 MGSLSSREVD RMVSTPIGGL SYVQGCTKKH LNSKTVGQCL ETTAQRVPER EALVVLHEDV RLTFAQLKEE VDKAASGLLS IGLCKGDRLG MWGPNSYAWV LMQLATAQAG IILVSVNPAY QAMELEYVLK KVGCKALVFP KQFKTQQYYN VLKQICPEVE NAQPGALKSQ RLPDLTTVIS VDAPLPGTLL LDEVVAAGST RQHLDQLQYN QQFLSCHDPI NIQFTSGTTG SPKGATLSHY NIVNNSNILG ERLKLHEKTP EQLRMILPNP LYHCLGSVAG TMMCLMYGAT LILASPIFNG KKALEAISRE RGTFLYGTPT MFVDILNQPD FSSYDISTMC GGVIAGSPAP PELIRAIINK INMKDLVVAY GTTENSPVTF AHFPEDTVEQ KAESVGRIMP HTEARIMNME AGTLAKLNTP GELCIRGYCV MLGYWGEPQK TEEAVDQDKW YWTGDVATMN EQGFCKIVGR SKDMIIRGGE NIYPAELEDF FHTHPKVQEV QVVGVKDDRM GEEICACIRL KDGEETTVEE IKAFCKGKIS HFKIPKYIVF VTNYPLTISG KIQKFKLREQ MERHLNL.

    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.

    Acsf2 Human
  • View Data Sheet

    Name :

    MLLT11 Human

    Description:

    Myeloid/Lymphoid Leukemia Translocated To 11 Human Recombinant

    AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    Product # :

    PRO-1991

    Price :

    Quantity :

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    • description
    • source
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    • More Info

    Description

    MLLT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids (1-90 a.a) and having a molecular mass of 12.4kDa. MLLT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MLLT11 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myeloid/Lymphoid Leukemia Translocated To 11 (MLLT11) is a part of the Mixed-Lineage Leukemia protein family. MLLT11 which takes part in leukemogenesis and in the progression of severe monocytic leukemia (AML) is located on chromosome 11q23. MLLT11 which is also expressed in embryonic brain cortex is upregulated during neuronal differentiation and is taking part in the evolution of the central nervous system.

    • Synonyms

      AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    • 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 MGSMRDPVSS QYSSFLFWRM PIPELDLSEL EGLGLSDTAT YKVKDSSVGK MIGQATAADQ EKNPEGDGLL EYSTFNFWRA PIASIHSFEL DLL.

    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.

    Mllt11 Human
  • View Data Sheet

    Name :

    CTSE Human

    Description:

    Cathepsin-E Human Recombinant

    Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.

    Product # :

    ENZ-776

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    CTSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (57-363 a.a) and having a molecular mass of 35.4kDa.CTSE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTSE protein solution (1mg/ml) containing 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

      Cathepsin-E also known as CTSE is a gastric aspartyl protease which functions as a disulfide-linked homodimer. CTSE belongs to the peptidase C1 family; furthermore it has specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase which does not seem to be involved in the digestion of dietary protein and is found in the uppermost concentration in the surface of epithelial mucus-producing cells of the stomach. CTSE is the first aspartic proteinaseexpressed in the fetal stomach and is discovered in more than half of gastric cancers. For that reason CTSE is anoncofetal antigen. In addition, transcript variants utilizing alternative polyadenylation signals and two transcript variantsencoding different isoforms exist for this gene.

    • Synonyms

      Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.

    • 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 MGSTESCSMD QSAKEPLINY LDMEYFGTIS IGSPPQNFTV IFDTGSSNLW VPSVYCTSPA CKTHSRFQPS QSSTYSQPGQ SFSIQYGTGS LSGIIGADQV SVEGLTVVGQ QFGESVTEPG QTFVDAEFDG ILGLGYPSLA VGGVTPVFDN MMAQNLVDLP MFSVYMSSNP EGGAGSELIF GGYDHSHFSG SLNWVPVTKQ AYWQIALDNM LWSVPTLTSC RMSPSPLTES PIPSAQLPTP YWTSWMECSS AAVAFKDLTS TLQLGPSGSW GMSSFDSFTQ SLTVGITVWD WPQQSPKEGP CVCACLSDRP

    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.

    Ctse Human
  • View Data Sheet

    Name :

    CUTC Human

    Description:

    cutC Copper Transporter Homolog Human Recombinant

    Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.

    Product # :

    PRO-911

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    Description

    CUTC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-273 a.a) and having a molecular mass of 31.5kDa.CUTC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CUTC protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUTC belongs to the Cut family and may be involved in efflux trafficking of cuprous ion. The Cut family is linked with the copper homeostasis and involved in several vital metabolisms, such as uptake, storage, delivery, and efflux of copper. Copper which is an essential heavy metal trace element has an imperative role in cell physiology.

    • Synonyms

      Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKRQGASSER KRARIPSGKA GAANGFLMEV CVDSVESAVN AERGGADRIE LCSGLSEGGT TPSMGVLQVV KQSVQIPVFV MIRPRGGDFL YSDREIEVMK ADIRLAKLYG ADGLVFGALT EDGHIDKELC MSLMAICRPL PVTFHRAFDM VHDPMAALET LLTLGFERVL TSGCDSSALE GLPLIKRLIE QAKGRIVVMP GGGITDRNLQ RILEGSGATE FHCSARSTRD SGMKFRNSSV AMGASLSCSE YSLKVTDVTK VRTLNAIAKN ILV.

    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.

    Cutc Human
  • View Data Sheet

    Name :

    SAT1 Human

    Description:

    Spermidine/Spermine N1-Acetyltransferase 1 Human Recombinant

    Diamine acetyltransferase 1, Spermidine/spermine N(1)-acetyltransferase 1, Putrescine acetyltransferase, Polyamine N-acetyltransferase 1, SSAT-1, SSAT, SAT1, SAT, DC21, KFSD, KFSDX.

    Product # :

    ENZ-433

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    Description

    SAT1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids (1-171 a.a.) and having a molecular mass of 22.1kDa.The SAT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAT1 solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SAT-1 is a member the acetyltransferase family, and is a rate-limiting enzyme in the catabolic pathway of polyamine metabolism. SAT1 catalyzes the acetylation of spermidine and spermine, and is involved in the regulation of the intracellular concentration of polyamines and their transport out of cells. Therefore, SAT-1’s role is essential in polyamine homoeostasis, given that acetylated products are either excreted from the cell or oxidized by acetylpolyamine oxidase. Increased SAT1 activity causes variety of other effects which include pancreatic cells death, obstruction of regenerative tissue growth, behavioral changes, keratosis follicularis spinulosa decalvans (KFSD), and hair loss.
      Defects in the SAT1 gene are linked to KFSD (keratosis follicularis spinulosa decalvans), which is a rare X-linked disorder affecting the skin and the eye. The KFSD affected men show thickening of the skin of the neck, ears, and extremities, particularly the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration. Even though the majority of the affected families are compatible with an X-linked inheritance, KFSD are found to be clinically and genetically heterogeneous.

    • Synonyms

      Diamine acetyltransferase 1, Spermidine/spermine N(1)-acetyltransferase 1, Putrescine acetyltransferase, Polyamine N-acetyltransferase 1, SSAT-1, SSAT, SAT1, SAT, DC21, KFSD, KFSDX.

    • 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 MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP FYHCLVAEVP KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMRC RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMATE E.

    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.

    Sat1 Human
  • View Data Sheet

    Name :

    NMNAT1 Human

    Description:

    Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant

    NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.

    Product # :

    ENZ-384

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    Description

    NMNAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-279 a.a.) and having a molecular mass of 36 kDa. The NMNAT1 is fused to a 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMNAT1 Human solution containing 20mM Tris pH-8, 0.1M NaCl, 1mM DTT, 1mM EDTA & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

    • Synonyms

      NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.

    • 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 KDRWGSMENS EKTEVVLLAC GSFNPITNMH LRLFELAKDY MNGTGRYTVV KGIISPVGDA YKKKGLIPAY HRVIMAELAT KNSKWVEVDT WESLQKEWKE TLKVLRHHQE KLEASDCDHQ QNSPTLERPG RKRKWTETQD SSQKKSLEPK TKAVPKVKLL CGADLLESFA VPNLWKSEDI TQIVANYGLI CVTRAGNDAQ KFIYESDVLW KHRSNIHVVN EWIANDISST KIRRALRRGQSIRYLVPDLV QEYIEKHNLY SSESEDRNAG VILAPLQRNT AEAKT.

    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.

    Nmnat1 Human
  • View Data Sheet

    Name :

    EGF Mouse

    Description:

    Epidermal Growth Factor Mouse

    Urogastrone, URG, EGF.

    Product # :

    CYT-554

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    Description

    Epidermal Growth Factor Mouse purified from submaxillary gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.1 kDa.The EGF is purified by proprietary chromatographic techniques.

    Source

    Mouse Submaxillary Gland.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

    Purity

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

    Biological Activity

    The biological activity is measured in a proliferation assay using BALB/MK cells.

    More Info

    • Introduction

      Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
      EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Illuminating Novel Avenues: Epidermal Growth Factor Mouse Variant in Cellular Dynamics and Therapeutic Prospects

      Abstract:

      This research paper delves into unexplored dimensions of the Epidermal Growth Factor Mouse Variant (EGF-M), unraveling its intricate molecular attributes, signaling cascades, and therapeutic implications. Employing advanced methodologies encompassing transgenic models, cellular assays, and bioinformatics, this study unveils the nuanced cellular responses elicited by EGF-M. The findings underscore its potential as a therapeutic target for regenerative medicine and cancer interventions.

      Introduction:

      Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper charts a new course, focusing on the Epidermal Growth Factor Mouse Variant (EGF-M), exploring its distinct molecular properties and therapeutic applications.

      Molecular Insights and Receptor Binding:

      EGF-M's interaction with the epidermal growth factor receptor (EGFR) initiates a cascade of intracellular events. Molecular dynamics simulations and binding studies decipher the nuances of this interaction, shedding light on structural motifs that drive receptor activation and downstream signaling.

      Cellular Signaling and Functional Responses:

      EGF-M engages canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) pathway and phosphoinositide 3-kinase (PI3K)/Akt pathway. High-resolution microscopy and phosphoproteomics unveil spatiotemporal dynamics, revealing how EGF-M orchestrates cell proliferation, migration, and survival.

      Transgenic Mouse Models and In Vivo Implications:

      In transgenic mouse models, EGF-M's impact on tissue regeneration becomes evident. Tailored wound healing assays demonstrate accelerated re-epithelialization and granulation tissue formation, affirming its potential in regenerative medicine. Furthermore, xenograft studies suggest its role in modulating tumor microenvironments, offering prospects for cancer therapy.

      Bioinformatics in EGF-M Interactions:

      Advanced bioinformatics analyses deepen our understanding of EGF-M's cellular interactions. Molecular docking simulations predict potential binding partners and off-target effects, enhancing our comprehension of its biological scope.

      Therapeutic Implications and Future Directions:

      EGF-M's distinctive attributes open doors for therapeutic innovation. Exploiting its regenerative potential, it holds promise for chronic wound management and tissue engineering. Moreover, targeted interventions exploiting its role in cancer microenvironments might revolutionize oncology treatments.

      Challenges and Prospects:

      Despite promising strides, challenges linger, including deciphering cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosage regimens to harness EGF-M's therapeutic potential.

      Conclusion:

      In a synthesis of intricate molecular insights and transformative therapeutic avenues, Epidermal Growth Factor Mouse Variant emerges as a captivating subject. Its distinctive binding mechanisms and multifaceted cellular orchestration spotlight its potential as a regenerative agent and a cancer therapeutic, propelling medical science into a new era.

      What is the molecular weight/Mw of EGF Protein?
      EGF Protein has a total Mw of 6.1Da.

      What is the source or expression system of EGF Protein?
      Mouse Submaxillary Gland.

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

      What is the Biological Activity of EGF Protein?
      The biological activity is measured in a proliferation assay using BALB/MK cells.

      What is the amino acid sequence of EGF Protein?
      EGF Protein is composed from 53 amino acids.

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

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

    Egf Mouse
  • View Data Sheet

    Name :

    CXCL13 Human

    Description:

    BCA-1/BLC Human Recombinant (CXCL13)

    C-X-C motif chemokine 13, Small-inducible cytokine B13, B lymphocyte chemoattractant, CXC chemokine BLC, CXCL13, BCA1, BCA-1, CXCL-13, B cell Attracting Chemokine-1, BLC, ANGIE, BLR1L, SCYB13, ANGIE2.

    Product # :

    CHM-348

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    Description

    CXCL13 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 10.3 kDa. The BCA-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCA-1 protein was lyophilized from a concentrated (0.5mg/ml) solution containing 20mM PBS & 150mM NaCl pH-7.4.

    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 human B cells using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.

    • Synonyms

      C-X-C motif chemokine 13, Small-inducible cytokine B13, B lymphocyte chemoattractant, CXC chemokine BLC, CXCL13, BCA1, BCA-1, CXCL-13, B cell Attracting Chemokine-1, BLC, ANGIE, BLR1L, SCYB13, ANGIE2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA1 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 CXCL13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VLEVYYTSLRCRCVQESSVFIPRRFIDRIQILPRGNG CPRKEIIVWKKNKSIVCVDPQAEWIQRMMEVLRKR SSSTLPVPVFKRKIP.

    • Background

      What is the molecular weight/Mw of CXCL13 HUMAN Protein?
      CXCL13 HUMAN Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CXCL13 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL13 HUMAN Protein?
      CXCL13 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL13 HUMAN Protein?
      Determined by its ability to chemoattract human B cells using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CXCL13 HUMAN Protein?
      VLEVYYTSLRCRCVQESSVFIPRRFIDRIQILPRGNG CPRKEIIVWKKNKSIVCVDPQAEWIQRMMEVLRKR SSSTLPVPVFKRKIP.

      What applications can CXCL13 HUMAN Protein be used in?
      CXCL13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL13 HUMAN Protein?
      The endotoxin level is minimal, CXCL13 HUMAN 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.

    Cxcl13 Human
  • View Data Sheet

    Name :

    FGF17 Human

    Description:

    Fibroblast Growth Factor 17 Human Recombinant

    Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    Product # :

    CYT-817

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    Description

    FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 22.6kDa.

    Source

    Escherichia Coli.

    Formulation

    FGF17 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

    More Info

    • Introduction

      Fibroblast Growth Factor 17 (FGF17) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.

    • Synonyms

      Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF17 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 FGF17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

    • Background

      What is the molecular weight/Mw of FGF17 Protein?
      FGF17 Protein has a total Mw of 22.6kDa.

      What is the source or expression system of FGF17 Protein?
      Escherichia Coli.

      What is the Purity of FGF17 Protein?
      FGF17 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF17 Protein?
      Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

      What is the amino acid sequence of FGF17 Protein?
      MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

      What applications can FGF17 Protein be used in?
      FGF17 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF17 Protein?
      The endotoxin level is minimal, FGF17 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.

    Fgf 17 Human
  • View Data Sheet

    Name :

    TGIF2LY Human

    Description:

    TGFB-Induced Factor Homeobox 2-Like Y-Linked Human Recombinant

    TGIFLY, Homeobox protein TGIF2LY, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, Y-linked, TGIF-like on the Y, TGIF2LY.

    Product # :

    PRO-1867

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    Description

    TGIF2LY Human Recombinant produced in E. coli is. a single polypeptide chain containing 208 amino acids (1-185) and having a molecular mass of 23.2kDa. TGIF2LY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TGIF2LY solution (1mg/ml) contains 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

      TGFB-Induced Factor Homeobox 2-Like Y-Linked (TGIF2LY) is a part of the TALE/TGIF homeobox family of transcription factors. TGIF2LY is located in the male specific region of chromosome Y, in a block of sequence which is the outcome of a large X-to-Y transposition. TGIF2LY act as a regulator of TGIF2LX due to the fact that the C-terminus of TGIF2LY is different from that of its chromosome X homolog (TGIF2LX). TGIF2LY has also a transcription role in testis.

    • Synonyms

      TGIFLY, Homeobox protein TGIF2LY, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, Y-linked, TGIF-like on the Y, TGIF2LY.

    • 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 MGSMEAAADG PAETQSPVEK DSPAKTQSPA QDTSIMSRNN ADTGRVLALP EHKKKRKGNL PAESVKILRD WMYKHRFKAY PSEEEKQMLS EKTNLSLLRI SNWFINARRR ILPDMLQQRR NDPIIGHKTG KDAHATHLQS TEASVPAKSG PVVQTMYKAC PCGPCQRARC QERSNQIRSR PLARSSPE.

    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.

    Tgif2Ly Human
  • View Data Sheet

    Name :

    CBX3 Human

    Description:

    Chromobox Homolog 3 Human Recombinant

    Chromobox homolog 3 (Drosophila HP1 gamma), Heterochromatin protein 1 homolog gamma, Modifier 2 protein, HP1 gamma homolog, HECH, HP1Hs-gamma.

    Product # :

    PRO-1057

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    • More Info

    Description

    CBX3 Human Recombinant produced in E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.4kDa.CBX3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CBX3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      CBX3 takes part in transcriptional silencing in heterochromatin-like complexes. CBX3 identifies and binds histone H3 tails methylated at 'Lys-9', thereby create an epigenetic repression. Additionally, CBX3 takes part in the formation of functional kinetochore by interacting with MIS12 complex proteins.

    • Synonyms

      Chromobox homolog 3 (Drosophila HP1 gamma), Heterochromatin protein 1 homolog gamma, Modifier 2 protein, HP1 gamma homolog, HECH, HP1Hs-gamma.

    • 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 MGSHMASNKT TLQKMGKKQN GKSKKVEEAE PEEFVVEKVL DRRVVNGKVE YFLKWKGFTD ADNTWEPEEN LDCPELIEAF LNSQKAGKEK DGTKRKSLSD SESDDSKSKK KRDAADKPRG FARGLDPERI IGATDSSGEL MFLMKWKDSD EADLVLAKEA NMKCPQIVIA FYEERLTWHS CPEDEAQ.

    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.

    Cbx3 Human
  • View Data Sheet

    Name :

    GDF5 Human, His

    Description:

    Growth differentiation factor 5 Human Recombinant, His Tag

    Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.

    Product # :

    CYT-653

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    Description

    GDF5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (382-501 a.a.) and having a total molecular mass of 15.8 kDa. GDF5 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDF5 solution contains 10mM sodium citrate pH-3.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.

    • Synonyms

      Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.

    • 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 MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.

    • Background

      What is the molecular weight/Mw of GDF5 HUMAN, HIS Protein?
      GDF5 HUMAN, HIS Protein has a total Mw of 15.8kDa.

      What is the source or expression system of GDF5 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of GDF5 HUMAN, HIS Protein?
      GDF5 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF5 HUMAN, HIS Protein?
      The biological functionality of GDF5 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of GDF5 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.

      What applications can GDF5 HUMAN, HIS Protein be used in?
      GDF5 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF5 HUMAN, HIS Protein?
      The endotoxin level is minimal, GDF5 HUMAN, HIS Protein was purified using conventional chromatography techniques.

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

    Gdf5 Human His
  • View Data Sheet

    Name :

    CFL2 Human

    Description:

    Cofilin-2 Human Recombinant

    Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    Product # :

    PRO-912

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    Description

    CFL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-166 a.a.) and having a molecular mass of 20.9kDa.CFL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CFL2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CFL2 protein is a member of the actin-binding proteins ADF family which contains 1 ADF-H domain. Cofilin is a broadly distributed intracellular actin-modulating protein which binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Defects in the CFL2 gene are the cause of nemaline myopathy type 7 (NEM7).

    • Synonyms

      Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    • 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 MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS 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.

    Cfl2 Human
  • View Data Sheet

    Name :

    GNGT1 Human

    Description:

    Guanine Nucleotide Binding Protein Gamma Transducing 1 Human Recombinant

    Guanine Nucleotide Binding Protein (G Protein), Gamma Transducing Activity Polypeptide 1, Transducin Gamma Chain, Guanine Nucleotide-Binding Protein G(T) Subunit Gamma-T1, GNG1, Guanine nucleotide-binding protein G(T) subunit gamma-T1.

    Product # :

    PRO-2084

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    Description

    GNGT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (1-71 a.a) and having a molecular mass of 10.6kDa. GNGT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GNGT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Guanine Nucleotide Binding Protein Gamma Transducing 1, also known as GNGT1 is amember of the G protein gamma family. GNGT1 is implicated in various transmembrane signaling systems as a modulator or transducer. In addition GNGT1 (beta & gamma chains) is required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.

    • Synonyms

      Guanine Nucleotide Binding Protein (G Protein), Gamma Transducing Activity Polypeptide 1, Transducin Gamma Chain, Guanine Nucleotide-Binding Protein G(T) Subunit Gamma-T1, GNG1, Guanine nucleotide-binding protein G(T) subunit gamma-T1.

    • 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 MGSMPVINIE DLTEKDKLKM EVDQLKKEVT LERMLVSKCC EEVRDYVEER SGEDPLVKGI PEDKNPFKEL KGGC.

    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.

    Gngt1 Human
  • View Data Sheet

    Name :

    FGF 21 Mouse, His

    Description:

    Fibroblast Growth Factor-21 Mouse Recombinant, His Tag

    Fibroblast growth factor 21, FGF-21.

    Product # :

    CYT-516

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    Description

    Fibroblast Growth Factor -21 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 21.2 kDa. The amino acid sequence of the recombinant human FGF21 is 100% homologous to the amino acid sequence of the Mouse FGF21 without signal sequence and contains 10 a.a. His tag at N-terminal.The FGF-21 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM TRIS, 20mM NaCl, pH 7.5.

    Purity

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

    More Info

    • Introduction

      The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
      FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
      FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
      FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

    • Synonyms

      Fibroblast growth factor 21, FGF-21.

    • Physical Appearance

      Filtered white lyophilized powder.

    • Stability

      Lyophilized FGF-21 Mouse Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 21 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 add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture. Add DTT (0.2mM) and NaCl (0.1-0.15M) before freezing to prevent potential aggregation.

    • Amino Acid Sequence

      MKHHHHHHAS AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALKPGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDATSWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY AS.

    • Background

      What is the molecular weight/Mw of FGF21 MOUSE,HIS Protein?
      FGF21 MOUSE,HIS Protein has a total Mw of 21.2kDa.

      What is the source or expression system of FGF21 MOUSE,HIS Protein?
      Escherichia Coli.

      What is the Purity of FGF21 MOUSE,HIS Protein?
      FGF21 MOUSE,HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF21 MOUSE,HIS Protein?
      The biological functionality of FGF21 MOUSE,HIS Protein will be determined in the future.

      What is the amino acid sequence of FGF21 MOUSE,HIS Protein?
      MKHHHHHHAS AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALKPGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDATSWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY AS.

      What applications can FGF21 MOUSE,HIS Protein be used in?
      FGF21 MOUSE,HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF21 MOUSE,HIS Protein?
      The endotoxin level is minimal, FGF21 MOUSE,HIS Protein was purified using conventional chromatography techniques.

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

    Fgf21 Mouse His
  • View Data Sheet

    Name :

    KGF Mouse

    Description:

    Keratinocye Growth Factor Mouse Recombinant

    HBGF-7, FGF7, FGF-7, KGF, Keratinocyte growth factor, Fibroblast growth factor 7, Heparin-binding growth factor 7.

    Product # :

    CYT-721

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    Description

    Keratinocyte Growth Factor-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 18.9 kDa. The FGF-7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM Phosphate buffer pH-8 and 0.1M NaCl.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant stimulation of KGF-responsive BaF3 indicator cells (measured by 3H-thymidine uptake) is < 10ng/ml corresponding to a specific activity of 100,000 Units/mg.

    More Info

    • Introduction

      KGF is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.

    • Synonyms

      HBGF-7, FGF7, FGF-7, KGF, Keratinocyte growth factor, Fibroblast growth factor 7, Heparin-binding growth factor 7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 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 KGF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MCNDMSPEQT ATSVNCSSPE RHTRSYDYME GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNSYNIMEI RTVAVGIVAI KGVESEYYLA MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHSG GEMFVALNQK GIPVKGKKTK KEQKTAHFLP MAIT.

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    Kgf Mouse
  • View Data Sheet

    Name :

    WIF1 Mouse

    Description:

    WNT Inhibitory Factor 1 Mouse Recombinant

    Wnt inhibitory factor 1, WIF-1, Wif1.

    Product # :

    PRO-2248

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    Description

    WIF1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 359 amino acids (29-379a.a.) and having a molecular mass of 39.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).WIF1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    WIF1 protein solution (1mg/ml) contains 20mM MES (pH5.5), 1mM DTT, 1mM PMSF and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.

    • Synonyms

      Wnt inhibitory factor 1, WIF-1, Wif1.

    • 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

      GQPPEESLYL WIDAHQARVL IGFEEDILIV SEGKMAPFTH DFRKAQQRMP AIPVNIHSMN FTWQAAGQAE YFYEFLSLRS LDKGIMADPT VNVPLLGTVP HKASVVQVGF PCLGKQDGVA AFEVNVIVMN SEGNTILRTP QNAIFFKTCQ QAECPGGCRN GGFCNERRVC ECPDGFYGPH
      CEKALCIPRC MNGGLCVTPG FCICPPGFYG VNCDKANCST TCFNGGTCFY PGKCICPPGL EGEQCELSKC PQPCRNGGKC IGKSKCKCPK GYQGDLCSKP VCEPGCGAHG TCHEPNKCQC REGWHGRHCN KRYGASLMHA PRPAGAGLER HTPSLKKAED RRDPPESNYI WVEHHHHHH.

    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.

    Wif1 Mouse
  • View Data Sheet

    Name :

    NELFE Human

    Description:

    Negative Elongation Factor Complex Member E Human Recombinant

    Negative elongation factor E, NELF-E, RNA-binding protein RD, NELFE, RD, RDBP, Negative Elongation Factor Complex Member E, D6S45, RDP.

    Product # :

    PRO-1968

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    Description

    NELFE Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-380) and having a molecular mass of 45.6 kDa.NELFE is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NELFE solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NELFE is a vital component of NELF complex which represses RNA polymerase II transcript elongation. NELFE is similar to nuclear RNA-binding proteins but does not bind RNA. NELFE contains a tract of alternating basic and acidic residues, mainly arginine and aspartic acid.

    • Synonyms

      Negative elongation factor E, NELF-E, RNA-binding protein RD, NELFE, RD, RDBP, Negative Elongation Factor Complex Member E, D6S45, RDP.

    • 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 MGSMLVIPPG LSEEEEALQK KFNKLKKKKK ALLALKKQSS SSTTSQGGVK RSLSEQPVMD TATATEQAKQ LVKSGAISAI KAETKNSGFK RSRTLEGKLK DPEKGPVPTF QPFQRSISAD DDLQESSRRP QRKSLYESFV SSSDRLRELG PDGEEAEGPG AGDGPPRSFD WGYEERSGAH SSASPPRSRS RDRSHERNRD RDRDRERDRD RDRDRDRERD RDRDRDRDRD RERDRDRERD RDRDREGPFR RSDSFPERRA PRKGNTLYVY GEDMTPTLLR GAFSPFGNII DLSMDPPRNC AFVTYEKMES ADQAVAELNG TQVESVQLKV NIARKQPMLD AATGKSVWGS LAVQNSPKGC HRDKRTQIVY SDDVYKENLV DGF.

    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.

    Nelfe Human
  • View Data Sheet

    Name :

    NMNAT2 Human

    Description:

    Nicotinamide Nucleotide Adenylyltransferase 2 Human Recombinant

    Nicotinamide Nucleotide Adenylyltransferase 2, C1orf15, Nicotinate-Nucleotide Adenylyltransferase 2, NaMN Adenylyltransferase 2, NMN Adenylyltransferase 2, PNAT2, KIAA0479, Chromosome 1 Open Reading Frame 15, Nicotinamide Mononucleotide Adenylyltransferase 2, Pyridine Nucleotide Adenylyltransferase 2, EC 2.7.7.1, EC 2.7.7.18.

    Product # :

    ENZ-509

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    Description

    NMNAT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-307 a.a) and having a molecular mass of 36.6kDa.NMNAT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMNAT2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 500 pmol/min/ug. One unit will convert 1.0 pmole of beta-NADH per minute to beta-NAD at PH 8.0 at 37°C.

    More Info

    • Introduction

      Nicotinamide Nucleotide Adenylyltransferase 2, also known as NMNAT2 is a member of the nicotinamide mononucleotide adenylyltransferase (NMNAT) enzyme family, members of which catalyze a vital step in NAD (NADP) biosynthetic pathway. Unlike the other human family member, which is localized to the nucleus, and is ubiquitously expressed; NMNAT2 is cytoplasmic, and is predominantly expressed in the brain. Two transcript variants encoding different isoforms have been found for NMNAT2. Among the diseases associated with NMNAT2 are tauopathy, and systemic lupus erythematosus.

    • Synonyms

      Nicotinamide Nucleotide Adenylyltransferase 2, C1orf15, Nicotinate-Nucleotide Adenylyltransferase 2, NaMN Adenylyltransferase 2, NMN Adenylyltransferase 2, PNAT2, KIAA0479, Chromosome 1 Open Reading Frame 15, Nicotinamide Mononucleotide Adenylyltransferase 2, Pyridine Nucleotide Adenylyltransferase 2, EC 2.7.7.1, EC 2.7.7.18.

    • 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 MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP SMTPVIGQPQ NETPQPIYQN SNVATKPTAA KILGKVGESL SRICCVRPPV ERFTFVDENA NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ LYINASG

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    Nmnat2 Human
  • View Data Sheet

    Name :

    TEF Human

    Description:

    Thyrotrophic Embryonic Factor Human Recombinant

    Thyrotroph embryonic factor, TEF, Thyrotroph embryonic factor isoform 1.FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.

    Product # :

    PRO-1523

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    • source
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    Description

    TEF Human Recombinant produced in E. coli is a single polypeptide chain containing 326 amino acids (1-303) and having a molecular mass of 35.6kDa.TEF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TEF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Thyrotroph embryonic factor (TEF) is a nuclear transcription factor which is a part of the bZIP (basic region/leucine zipper) family and PAR subfamily. TEF binds DNA as either a homodimer or heterodimer, and is known to transactivate the TSH beta promoter. TEF accumulates according to a robust circadian rhythm and is also inhibits cell growth by down-regulating beta chain expression of cytokine receptors.

    • Synonyms

      Thyrotroph embryonic factor, TEF, Thyrotroph embryonic factor isoform 1.FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.

    • 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 MGSMSDAGGG KKPPVDPQAG PGPGPGRAAG ERGLSGSFPL VLKKLMENPP REARLDKEKG KEKLEEDEAA AASTMAVSAS LMPPIWDKTI PYDGESFHLE YMDLDEFLLE NGIPASPTHL AHNLLLPVAE LEGKESASSS TASPPSSSTA IFQPSETVSS
      TESSLEKERE TPSPIDPNCV EVDVNFNPDP ADLVLSSVPG GELFNPRKHK FAEEDLKPQP MIKKAKKVFV PDEQKDEKYW TRRKKNNVAA KRSRDARRLK ENQITIRAAF LEKENTALRT EVAELRKEVG KCKTIVSKYE TKYGPL.

    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.

    Tef Human
  • View Data Sheet

    Name :

    TGFB3 Human, Plant

    Description:

    Transforming Growth Factor-Beta 3 Human Recombinant, Plant

    Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

    Product # :

    CYT-588

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    Description

    TGFB3 Human Recombinant produced in plant is a disulfide-linked homodimeric, glycosylated, polypeptide chain containing 118 amino acids and having a molecular mass of 27.2kDa. The TGFB3 is fused to 6xHis tag at N-terminus and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of TGFB3 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 ? 40ng/ml corresponding to a specific activity of 25,000 Units/mg.

    More Info

    • Introduction

      Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each 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.

    • Synonyms

      Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGFB3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 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 TGFB3 in sterile 5mM HCl & 50ug/ml BSA at a concentration of 0.05mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKG
      YYANFCSGPCPYLRSADTTHSTVLGLY
      NTLNPEASASP
      CCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS.

    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.

    Tgfb3 Human Plant
  • View Data Sheet

    Name :

    KCTD4 Human

    Description:

    Potassium Channel Tetramerisation Domain Containing 4 Human Recombinant

    Potassium Channel Tetramerization Domain Containing 4, Potassium Channel Tetramerisation Domain Containing 4, bA321C24.3, BTB/POZ Domain-Containing Protein KCTD4.

    Product # :

    PRO-1763

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    Description

    KCTD4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 282 amino acids (1-259 a.a) and having a molecular mass of 32.4kDa.KCTD4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KCTD4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      KCTD4 also known as Potassium Channel Tetramerisation Domain Containing 4 has an N-terminal homodimerization domain which contains multiple copies of kelch repeats and C2H2-type zinc fingers. Proteins which include BTB domains are consider being involved in transcriptional regulation through control of chromatin structure and function. In addition, KCTD4 is a 259 amino acid protein which contains one BTB domain, a possible role as a transcriptional regulator may be suggested.

    • Synonyms

      Potassium Channel Tetramerization Domain Containing 4, Potassium Channel Tetramerisation Domain Containing 4, bA321C24.3, BTB/POZ Domain-Containing Protein KCTD4.

    • 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 MGSMERKINR REKEKEYEGK HNSLEDTDQG KNCKSTLMTL NVGGYLYITQ KQTLTKYPDT FLEGIVNGKI LCPFDADGHY FIDRDGLLFR HVLNFLRNGE LLLPEGFREN QLLAQEAEFF QLKGLAEEVK SRWEKEQLTP RETTFLEITD NHDRSQGLRI FCNAPDFISK IKSRIVLVSK SRLDGFPEEF SISSNIIQFK YFIKSENGTR LVLKEDNTFV CTLETLKFEA IMMALKCGFR LLTSLDCSKG SIVHSDALHF IK

    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.

    Kctd4 Human
  • View Data Sheet

    Name :

    VTCN1 Human, Sf9

    Description:

    V-Set Domain Containing T Cell Activation Inhibitor 1 Human Recombinant, Sf9

    V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.

    Product # :

    PRO-2439

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    Description

    VTCN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 244 amino acids (25-259a.a.) and having a molecular mass of 26.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). VTCN1 is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    VTCN1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      V-Set Domain Containing T Cell Activation Inhibitor 1, also known as VCTN1, is part of the B7 costimulatory protein family. Proteins in this family are located on the surface of antigen-presenting cells and interact with ligand bound to receptors on the surface of T cells. High level of the encoded protein has been associated with tumor progression. VCTN1 also takes part in promoting epithelial cell transformation.

    • Synonyms

      V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.

    • 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

      ADPLIIGFGI SGRHSITVTT VASAGNIGED GILSCTFEPD IKLSDIVIQW LKEGVLGLVH EFKEGKDELS EQDEMFRGRT AVFADQVIVG NASLRLKNVQ LTDAGTYKCY IITSKGKGNA NLEYKTGAFS MPEVNVDYNA SSETLRCEAP RWFPQPTVVW ASQVDQGANF SEVSNTSFEL NSENVTMKVV SVLYNVTINN TYSCMIENDI AKATGDIKVT ESEIKRRSHL QLLNSKASHH HHHH.

    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.

    Vtcn1 Protein
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