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Search results

1000 results found for “mortality factor”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    TCEAL7 Human

    Description:

    Transcription Elongation Factor A (SII)-Like 7 Human Recombinant

    Transcription elongation factor A (SII)-like 7, TCEA-like protein 7, transcription elongation factor A protein-like 7, MGC23947, MPMGp800C04260Q003.

    Product # :

    PRO-1147

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TCEAL7 Human Recombinant produced in E. coli is a single polypeptide chain containing 124 amino acids (1-100) and having a molecular mass of 14.8 kDa.TCEAL7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TCEAL7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription Elongation Factor A (SII)-Like 7 (TCEAL7) has a role in the negative regulation of NF-kappa-B signaling at the basal level by controlling transcriptional activity of NF-kappa-B on its target gene promoters. TCEAL7 links with cyclin D1 promoter containing Myc E-box sequence and transcriptionally inhibits cyclin D1 expression. TCEAL7 regulates telomerase reverse transcriptase expression and telomerase activity in both alternative lengthening of telomeres (ALT) and telomerase-positive cell lines. TCEAL7 is highly expressed in normal and fetal brain tissues, and weakly expressed in the uterus and ovary. TCEAL7 is down-regulated in epithelial ovarian, cervical, prostate, breast, brain and lung cancer cell lines and in the brain and ovarian tumors.

    • Synonyms

      Transcription elongation factor A (SII)-like 7, TCEA-like protein 7, transcription elongation factor A protein-like 7, MGC23947, MPMGp800C04260Q003.

    • 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 MGSHMQKPCK ENEGKPKCSV PKREEKRPYG EFERQQTEGN FRQRLLQSLE EFKEDIDYRH FKDEEMTREG DEMERCLEEI RGLRKKFRAL HSNHRHSRDR PYPI

    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.

    Tceal7 Human
  • View Data Sheet

    Name :

    OSM Human, His

    Description:

    Oncostatin-M Human Recombinant, His Tag

    OSM, MGC20461.

    Product # :

    CYT-060

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      OSM, MGC20461.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Osm Human His
  • View Data Sheet

    Name :

    LTF Holo Human

    Description:

    Lactoferrin Holo Human Recombinant

    Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    Product # :

    PRO-592

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Recombinant Human Holo Lactoferrin produced in Plant is a glycosylated mature polypeptide sequence having an approximate molecular mass of 80 kDa.The Human Holo Lactoferrin is purified by proprietary chromatographic techniques.

    Source

    Rice Flour.

    Formulation

    The Human Holo lactoferrin was lyophilized with no additives.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

    • Synonyms

      Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    • Physical Appearance

      Pink lyophilized powder.

    • Stability

      Recombinant Holo Lactoferrin although stable at room temperature for 5 days, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized LTF Holo Human in sterile water at 10mg/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.

    Lactoferrin Holo Human
  • View Data Sheet

    Name :

    Leptin Pufferfish

    Description:

    Leptin Pufferfish Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-530

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.

    More Info

    • Introduction

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

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pufferfish Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE

      GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE

      QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Pufferfish
  • View Data Sheet

    Name :

    Leptin-B Tilapia

    Description:

    Leptin-B Tilapia Recombinant

    Product # :

    CYT-1110

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.

    Purity

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

    Biological Activity

    Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.

    More Info

    • Introduction

      Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin-B Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-B Tilapia should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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

    Leptin B
  • View Data Sheet

    Name :

    CTF1 Mouse

    Description:

    Cardiotrophin-1 Mouse Recombinant

    CTF1, CT1, CT-1, Cardiophin 1.

    Product # :

    CYT-151

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    Description

    CTF1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 202 amino acids and having a molecular mass of 21.3kDa.The CTF1 Mouse is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 1.0ng/ml, corresponding to a specific activity of > 1,000,000units/mg.

    More Info

    • Introduction

      Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
      CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
      Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
      Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.

    • Synonyms

      CTF1, CT1, CT-1, Cardiophin 1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CTF1 in sterile 4mM HCl to a concentration of 0.1-0.5 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-200C. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      SQREGSLEDH QTDSSISFLP HLEAKIRQTH NLARLLTKYA EQLLEEYVQQ QGEPFGLPGF SPPRLPLAGL SGPAPSHAGL PVSERLRQDA AALSVLPALL DAVRRRQAEL NPRAPRLLRS LEDAARQVRA LGAAVETVLA ALGAAARGPG PEPVTVATLF TANSTAGIFS AKVLGFHVCG LYGEWVSRTE GDLGQLVPGG VA

    • Background

      What is the molecular weight/Mw of CTF1 Protein?
      CTF1 Protein has a total Mw of 21.3kDa.

      What is the source or expression system of CTF1 Protein?
      Escherichia Coli.

      What is the Purity of CTF1 Protein?
      CTF1 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF1 Protein?
      The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 1.0ng/ml, corresponding to a specific activity of > 1,000,000units/mg.

      What is the amino acid sequence of CTF1 Protein?
      SQREGSLEDH QTDSSISFLP HLEAKIRQTH NLARLLTKYA EQLLEEYVQQ QGEPFGLPGF SPPRLPLAGL SGPAPSHAGL PVSERLRQDA AALSVLPALL DAVRRRQAEL NPRAPRLLRS LEDAARQVRA LGAAVETVLA ALGAAARGPG PEPVTVATLF TANSTAGIFS AKVLGFHVCG LYGEWVSRTE GDLGQLVPGG VA

      What applications can CTF1 Protein be used in?
      CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF1 Protein?
      The endotoxin level is minimal, CTF1 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.

    Ct 1 Mouse
  • View Data Sheet

    Name :

    CBFB HUman

    Description:

    Core Binding Factor Beta Human Recombinant

    PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.

    Product # :

    PRO-534

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    Description

    CBFB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-202 a.a.) and having a molecular mass of 23.6 kDa. The CBFB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing 20mM MES pH-6, 0.1mM PMSF & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CBFB beta subunit is a heterodimeric core-binding transcription factor that is part of the PEBP2/CBF transcription factor family which controls a host of genes particulary to hematopoiesis and osteogenesis. CBFB is a non-DNA binding regulatory subunit which increases DNA binding by alpha subunit.

    • Synonyms

      PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CBFB Human although stable at 4C for 1 week, should be stored below -18C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT GTNLSLQFFP
      ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH
      REEMEVRVSQ LLAVTGKKTT 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.

    Cbfb Human
  • View Data Sheet

    Name :

    PDCD5 Human

    Description:

    Programmed Cell Death-5 Human Recombinant

    Programmed cell death protein 5, TF-1 cell apoptosis-related protein 19, Protein TFAR19, PDCD5, TFAR19, MGC9294.

    Product # :

    PRO-624

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    Description

    PDCD5 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids and having a molecular mass of 14 kDa.

    Source

    Escherichia Coli.

    Formulation

    PDCD5 protein solution contains 1x PBS pH-7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PDCD5 is expressed in tumor cells during apoptosis independent of the apoptosis-inducing stimuli. Prior to apoptosis induction, PDCD5 is distributed in both the nucleus and cytoplasm. Once apoptosis is induced, the amount of PDCD5 increases and by relocation from the cytoplasm, it accumulates in the nucleus.PDCD5 protein has a stable helical core conformation consisting of a triple-helix bundle and two dissociated terminal regions. PDCD5 is an important novel protein that regulates both apoptotic and non-apoptotic programmed cell death. PDCD5 functions in the process of apoptosis.
      PDCD5 plays an important role in regulation of apoptotic processes in gastric cancer cells and gastric tumors.
      PDCD5 plays a role in the pathogenesis of rheumatoid arthritis.
      -27G/-11A SNP is associated with reduced PDCD5 promoter activity and increased susceptibility to chronic myelogenous leukemia.
      PDCD5 gene may be a target gene under the control of some important apoptosis-related transcriptional factors during the cell apoptosis.

    • Synonyms

      Programmed cell death protein 5, TF-1 cell apoptosis-related protein 19, Protein TFAR19, PDCD5, TFAR19, MGC9294.

    • 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

      MADEELEALR RQRLAELQAK HGDPGDAAQQ EAKHRGAEMR NSILAQVLDQ SARARLSNLA LVKPEKTKAV ENYLIQMARY GQLSEKVSEQ GLIEILKKVS QQTEKTTTVK LNRRKVMDSD EDDDY.

    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.

    Pdcd5 Human
  • View Data Sheet

    Name :

    FGF6 Human

    Description:

    Fibroblast Growth Factor-6 Human Recombinant

    Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.

    Product # :

    CYT-979

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    Description

    FGF6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 169 amino acids and having a molecular mass of 18.9kDa.The FGF-6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-6 protein was lyophilized from a 0.2µm filtered solution in 10mM sodium phosphate and 50mM sodium chloride pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fibroblast Growth Factor-6 (FGF6) belongs to the fibroblast growth factor (FGF) family. FGF family members possess extensive mitogenic and cell survival functions, and are involved in various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF6 gene displayes oncogenic transforming activity when transfected into mammalian cells. The mouse homolog of the FGF6 gene displays a restricted expression profile predominantly in the myogenic lineage, suggesting a role in muscle regeneration or differentiation.

    • Synonyms

      Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-6 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 FGF6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.

    • Background

      What is the molecular weight/Mw of FGF6 Protein?
      FGF6 Protein has a total Mw of 18.9kDa.

      What is the source or expression system of FGF6 Protein?
      Escherichia Coli.

      What is the Purity of FGF6 Protein?
      FGF6 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF6 Protein?
      The biological functionality of FGF6 Protein will be determined in the future.

      What is the amino acid sequence of FGF6 Protein?
      MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.

      What applications can FGF6 Protein be used in?
      FGF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF6 Protein?
      The endotoxin level is minimal, FGF6 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.

    Fgf6 Human
  • View Data Sheet

    Name :

    FGF 9 Mouse

    Description:

    Fibroblast Growth Factor-9 Mouse Recombinant

    GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    Product # :

    CYT-349

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    Description

    Fibroblast Growth Factor-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids and having a molecular mass of 23308 Dalton.The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 10mM Tris, pH 8.0, 0.15M Amonium Sulfate.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

    More Info

    • Introduction

      Rat and mouse FGF-9 show a very high homology to human FGF-9. The transcripts for FGF-9 have been found in brain and in kidney tissue. Fibroblast Growth Factor-9 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. FGF9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog (Shh) signaling. Mice lacking the homolog gene displayed a male-to-female sex reversal phenotype, which suggested a role in testicular embryogenesis Fibroblast Growth Factor 9 may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.

    • Synonyms

      GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fibroblast Growth Factor-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF9 Mouse Recombinant 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 Fibroblast Growth Factor 9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Pro-Leu-Gly-Glu-Val.

    • Background

      What is the molecular weight/Mw of FGF9 Protein?
      FGF9 Protein has a total Mw of 23.3kDa.

      What is the source or expression system of FGF9 Protein?
      Escherichia Coli.

      What is the Purity of FGF9 Protein?
      FGF9 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF9 Protein?
      The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

      What is the amino acid sequence of FGF9 Protein?
      FGF9 Protein is composed from 205 amino acids.

      What applications can FGF9 Protein be used in?
      FGF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF9 Protein?
      The endotoxin level is minimal, FGF9 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.

    Fgf9 Mouse
  • View Data Sheet

    Name :

    GDF5 Human

    Description:

    Growth Differentiation Factor-5 Human Recombinant

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

    Product # :

    CYT-442

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    Description

    Growth Differentiation Factor 5 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 120 amino acids and having a total molecular mass of 27.4kDa. To enable bacterial expression the N-terminal sequence of Ala-Pro-Leu-Thr was replaced with a Lys.GDF5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized without any additives.

    Purity

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

    Biological Activity

    GDF-5 activity as determined by the induction of alkaline phosphatase activity in ATDC5 cells is typically 10-20ng/ml.

    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 White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth Differentiation Factor 5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Growth Differentiation Factor-5 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 Growth Differentiation Factor-5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APSATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.

    • Background

      What is the molecular weight/Mw of GDF5 HUMAN Protein?
      GDF5 HUMAN Protein has a total Mw of 27.4kDa.

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

      What is the Purity of GDF5 HUMAN Protein?
      GDF5 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF5 HUMAN Protein?
      GDF-5 activity as determined by the induction of alkaline phosphatase activity in ATDC5 cells is typically 10-20ng/ml.

      What is the amino acid sequence of GDF5 HUMAN Protein?
      APSATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.

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

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


    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.15 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of GDF5 as a Reference Standard.

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

    Gdf5 Human
  • View Data Sheet

    Name :

    MANF Rat

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Rat Recombinant

    Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    Product # :

    CYT-828

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    • More Info

    Description

    MANF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18.2kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using rat C6 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

    More Info

    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIEEELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDKQ IDLSTVDLKK LRVKELKKIL DDWGEMCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.

    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.

    Manf Rat
  • View Data Sheet

    Name :

    WIF1 Human

    Description:

    WNT Inhibitory Factor 1 Human Recombinant

    WIF1, WIF-1, Wnt inhibitory factor 1.

    Product # :

    PRO-684

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    Description

    WIF1 Human is a single, glycosylated polypeptide chain containing 360 amino acids (29-379 a.a.) and having a molecular mass of 39.5 kDaWIF1 is fused to 6 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The WIF1 protein solution contains 1X PBS pH 7.4, 20% glycerol, 1mM DTT and 0.1mM PMSF.

    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

      WIF1, WIF-1, Wnt inhibitory factor 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADLGPPQEES LYLWIDAHQA RVLIGFEEDI LIVSEGKMAP FTHDFRKAQQ RMPAIPVNIH SMNFTWQAAG QAEYFYEFLS LRSLDKGIMA DPTVNVPLLG TVPHKASVVQ VGFPCLGKQD GVAAFEVDVI VMNSEGNTIL QTPQNAIFFK TCQQAECPGG CRNGGFCNER RICECPDGFH GPHCEKALCT PRCMNGGLCV TPGFCICPPG FYGVNCDKAN CSTTCFNGGT CFYPGKCICP PGLEGEQCEI SKCPQPCRNG GKCIGKSKCK CSKGYQGDLC SKPVCEPGCG AHGTCHEPNK CQCQEGWHGR HCNKRYEASL IHALRPAGAQ LRQHTPSLKK AEERRDPPES NYIWHHHHHH

    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 Human
  • View Data Sheet

    Name :

    IRF3 Human

    Description:

    IFN Regulatory Factor-3 Human Recombinant

    IRF-3, IRF3, IFN Regulatory Factor 3.

    Product # :

    CYT-292

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    Description

    IRF-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (1-112) and having a molecular mass of 13 kDa.The IRF3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml in phosphate-buffered saline (PBS), pH 7.4.

    Purity

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

    More Info

    • Introduction

      Members of the IFN regulatory factor (IRF) family regulate gene expression critical to immune response, hemopoiesis, and proliferation. IRF-3 is a member of the IRF family, and is distinct from other family members. Its transcriptional activity is regulated solely by posttranslational modifications. It plays a crucial role in activation of innate immunity and inflammation in response to viral infection. IRF-3 mediates IFN-stimulated response element (isre) promoter activation. Functions as a molecular switch for antiviral activity. Dsrna generated during the course of an viral infection leads to IRF3 phosphorylation on the c-terminal serine/threonine cluster. This induces a conformational change, leading to its dimerization, nuclear localization and association with creb binding protein (crebbp) to form dsrna-activated factor 1 (draf1), a complex which activates the transcription of genes under the control of isre. The complex binds to the ie and prdiii regions on the ifn-alpha and ifn-beta promoters respectively. IRF-3 does not have any transcription activation domains.

    • Synonyms

      IRF-3, IRF3, IFN Regulatory Factor 3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Liquid IRF3 although stable at 10°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP HDPHKIYEFV NS.

    • Background

      What is the molecular weight/Mw of IRF3 HUMAN Protein?
      IRF3 HUMAN Protein has a total Mw of 13kDa.

      What is the source or expression system of IRF3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IRF3 HUMAN Protein?
      IRF3 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IRF3 HUMAN Protein?
      The biological functionality of IRF3 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IRF3 HUMAN Protein?
      MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP HDPHKIYEFV NS.

      What applications can IRF3 HUMAN Protein be used in?
      IRF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IRF3 HUMAN Protein?
      The endotoxin level is minimal, IRF3 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.

    Irf 3 Human
  • View Data Sheet

    Name :

    EIF4H Human

    Description:

    Eukaryotic Translation Initiation Factor 4H Human Recombinant

    Eukaryotic translation initiation factor 4H, eIF-4H, Williams-Beuren syndrome chromosomal region 1 protein, EIF4H, KIAA0038, WBSCR1, WSCR1.

    Product # :

    PRO-1114

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    Description

    EIF4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a) and having a molecular mass of 29.9kDa.EIF4H is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EIF4H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic translation initiation factor 4H (EIF4H) is a 248 amino acid protein which localizes to the perinuclear region of the cytoplasm and is expressed as 2 isoforms, termed short and long. EIF4H functions to stimulate the initiation of protein synthesis at the level of mRNA employment. EIF4H stimulates the RNA-dependent ATP hydrolysis catalyzed by EIF4A and EIF4B. EIF4H gene defects linked to Williams- Beuren syndrome (WBS), a rare developmental disorder characterized by cardiovascular and musculo-skeletal abnormalities and caused by the deletion of contiguous genes at 7q11.23.

    • Synonyms

      Eukaryotic translation initiation factor 4H, eIF-4H, Williams-Beuren syndrome chromosomal region 1 protein, EIF4H, KIAA0038, WBSCR1, WSCR1.

    • 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 MGSHMADFDT YDDRAYSSFG GGRGSRGSAG GHGSRSQKEL PTEPPYTAYV GNLPFNTVQG DIDAIFKDLS IRSVRLVRDK DTDKFKGFCY VEFDEVDSLK EALTYDGALL GDRSLRVDIA EGRKQDKGGF GFRKGGPDDR GMGSSRESRG GWDSRDDFNS
      GFRDDFLGGR GGSRPGDRRT GPPMGSRFRD GPPLRGSNMD FREPTEEERA QRPRLQLKPR TVATPLNQVA NPNSAIFGGA RPREEVVQKE QE.

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    Eif4H Human
  • View Data Sheet

    Name :

    IRF3 Antibody

    Description:

    Interferon Regulatory Factor-3, Mouse Anti Human

    IRF-3, IRF3, Interferon Regulatory Factor 3.

    Product # :

    ANT-365

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    More Info

    • Introduction

      Members of the Interferon regulatory factor (IRF) family regulate gene expression critical to immune response, hemopoiesis, and proliferation. IRF-3 is a member of the IRF family, and is distinct from other family members. Its transcriptional activity is regulated solely by posttranslational modifications. It plays a crucial role in activation of innate immunity and inflammation in response to viral infection. IRF-3 mediates interferon-stimulated response element (isre) promoter activation. Functions as a molecular switch for antiviral activity. Dsrna generated during the course of an viral infection leads to IRF3 phosphorylation on the c-terminal serine/threonine cluster. This induces a conformational change, leading to its dimerization, nuclear localization and association with creb binding protein (crebbp) to form dsrna-activated factor 1 (draf1), a complex which activates the transcription of genes under the control of isre. The complex binds to the ie and prdiii regions on the ifn

    • Synonyms

      IRF-3, IRF3, Interferon Regulatory Factor 3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human IRF3 mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human IRF3 amino acids 108-166 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P3F10AT.

    • Applications

      IRF3 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      IRF3 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Irf3 Antibody
  • View Data Sheet

    Name :

    IGFBP4 Human

    Description:

    Insulin-Like Growth Factor Binding Protein-4 Human

    Insulin-like growth factor-binding protein 4, IBP-4, IGF-binding protein 4, IGFBP-4, IGFBP4, IBP4, BP-4, HT29-IGFBP.

    Product # :

    CYT-030

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    Description

    IGFBP-4 Human Recombinant amino acids Asp22- Glu258, produced in HEK293 cells and fused with a polyhistidine tag at the C-terminus. IGFBP4 predicted Mw is 27kDa and on SDS-PAGE appears as a 32kDa band under denaturing conditions.IGFBP4 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    IGFBP 4 was lyophilized after extensive dialysis against PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is 0.01-0.09µg/ml as measured by its ability to inhibit the biological activity of IGFII (20ng/ml) on MCF7 human breast adenocarcinoma cells.

    More Info

    • Introduction

      Insulin-like growth factor-binding protein 4 (IGFBP-4) belongs to the insulin-like growth factor binding protein (IGFBP) family. IGFBP4 includes an IGFBP domain and a thyroglobulin type-I domain. IGFBP4 binds both insulin-like growth factors (IGFs) I and II. IGFBP-4 circulates in the plasma in both glycosylated and non-glycosylated forms. IGFBPs can either inhibit or enhance the biological activities of IGF, or act in an IGF independent manner. IGFBP-4 is exceptional since it consistently inhibits several cancer cells in vivo and in vitro, suggesting that it may function as an apoptotic factor. IGFBP4 is produced by all colon cancer cells. Binding of IGFBP-4 prolongs the half-life of the IGFs and changes their interaction with cell surface receptors.

    • Synonyms

      Insulin-like growth factor-binding protein 4, IBP-4, IGF-binding protein 4, IGFBP-4, IGFBP4, IBP4, BP-4, HT29-IGFBP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGFBP4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP-4 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 IGFBP4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GLGMPCGVYT PRCGSGLRCY PPRGVEKPLH TLMHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRRCLQK HFAKIRDRST SGGKMKVNGA PREDARPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE + His Tag.

    • Background

      What is the molecular weight/Mw of IGFBP4 HUMAN Protein?
      IGFBP4 HUMAN Protein has a total Mw of 27kDa.

      What is the source or expression system of IGFBP4 HUMAN Protein?
      HEK293 cells.

      What is the Purity of IGFBP4 HUMAN Protein?
      IGFBP4 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGFBP4 HUMAN Protein?
      The ED50 range is 0.01-0.09µg/ml as measured by its ability to inhibit the biological activity of IGFII (20ng/ml) on MCF7 human breast adenocarcinoma cells.
      What is the amino acid sequence of IGFBP4 HUMAN Protein?
      DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GLGMPCGVYT PRCGSGLRCY PPRGVEKPLH TLMHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRRCLQK HFAKIRDRST SGGKMKVNGA PREDARPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE + His Tag.

      What applications can IGFBP4 HUMAN Protein be used in?
      IGFBP4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGFBP4 HUMAN Protein?
      The endotoxin level is minimal, IGFBP4 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.

    Igfbp 4 Human
  • View Data Sheet

    Name :

    PEDF Human, His

    Description:

    Pigment Epithelium-Derived Factor Human Recombinant, His Tag

    Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    Product # :

    CYT-552

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    Description

    PEDF Human Recombinant produced in E.Coli containing a natural variant M72T is a single, non-glycosylated, polypeptide chain containing 420 amino acids (20-418 a.a.) and having a total molecular mass of 46.7 kDa. PEDF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PEDF solution contains 20mM Tris-HCl buffer(pH 8.0), 0.1M NaCl , and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
      Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
      Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
      PEDF & VEGF genes contribute to the development of diabetic retinopathy.
      PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
      PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
      SerpinF1 is a new promising approach for the treatment of osteosarcoma.
      Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
      VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
      Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
      PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.

    • Synonyms

      Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    • 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 MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.

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    Serpinf1 Human His
  • View Data Sheet

    Name :

    MANF Human, His

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant, His Tag

    Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    Product # :

    CYT-133

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    Description

    MANF Human Recombinant produced in E. coli is a single polypeptide chain containing 183 amino acids (25-182) and having a molecular mass of 20.8kDa.MANF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MANF solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    • 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 MGSHMLRPGD CEVCISYLGR FYQDLKDRDV TFSPATIENE LIKFCREARG KENRLCYYIG ATDDAATKII NEVSKPLAHH IPVEKICEKL KKKDSQICEL KYDKQIDLST VDLKKLRVKE LKKILDDWGE TCKGCAEKSD YIRKINELMP KYAPKAASAR TDL

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    Manf Human
  • View Data Sheet

    Name :

    TPO Human, CHO

    Description:

    Thrombopoietin Human Recombinant, CHO

    MPL Ligand, THCYT1, MPLLG, TPO, ML, Thrombopoietin Nirs Variant 1, MKCSF, Thrombopoietin, Myeloproliferative Leukemia Virus Oncogene Ligand, Megakaryocyte Growth and Development Factor, Megakaryocyte Colony-Stimulating Factor, C-Mpl Ligand, MGDF, Megakaryocyte Stimulating Factor, Prepro-Thrombopoietin.

    Product # :

    CYT-1070

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    Description

    Thrombopoietin Human Recombinant produced in CHO cells has a molecular weight range of 80-90kDa due to glycosylation. The TPO is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells.

    Formulation

    TPO protein solution contains phosphate buffered saline (pH7.4) and 2% albumin.

    Purity

    Greater than 98% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of MO7e cells corresponding to a specific activity of 3x105 units/mg.

    More Info

    • Introduction

      Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets.

    • Synonyms

      MPL Ligand, THCYT1, MPLLG, TPO, ML, Thrombopoietin Nirs Variant 1, MKCSF, Thrombopoietin, Myeloproliferative Leukemia Virus Oncogene Ligand, Megakaryocyte Growth and Development Factor, Megakaryocyte Colony-Stimulating Factor, C-Mpl Ligand, MGDF, Megakaryocyte Stimulating Factor, Prepro-Thrombopoietin.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Thrombopoietin although stable at room temperature for 1 week, should be stored between 2-8°C.

    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.

    Thrombopoietin
  • View Data Sheet

    Name :

    FLT1 D7 Human

    Description:

    Vascular Endothelial Growth Factor Receptor-1 D1-7 Human Recombinant

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

    Product # :

    PKA-241

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    Description

    Soluble FLT1 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric, glycosylated, polypeptide containing 751 amino acids and having a molecular mass of 130 kDa. The soluble receptor protein contains only the first 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. The FLT1 fc/Chimera is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT1 D1-7 was lyophilized from a concentrated (1 mg/ml) sterile solution containing PBS Buffer, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity of FLT1/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells. The ED50 for this effect is typically 10-30 ng/ml, corresponding to a specific activity of 33,333.33-100,000 units/mg.

    More Info

    • Introduction

      Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution FLT1 should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FLT1 Fc/Chimera in PBS not less than 50µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG TAASDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI S.

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

    Flt1 D7 Human
  • View Data Sheet

    Name :

    LZTFL1 Human

    Description:

    Leucine Zipper Transcription Factor-Like 1 Human Recombinant

    Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.

    Product # :

    PRO-2157

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    Description

    LZTFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a) and having a molecular mass of 37.0kDa. LZTFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LZTFL1 protein solution (1mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leucine Zipper Transcription Factor-Like 1, also known as LZTFL1 is a ubiquitously expressed protein which localizes to the cytoplasm. LZTFL1 interacts with Bardet-Biedl Syndrome proteins (BBS) and during its interaction with BBS protein complexes, regulates protein trafficking to the ciliary membrane. Nonsense mutations in LZTFL1 cause a form of Bardet-Biedl Syndrome; a ciliopathy characterized partly by polydactyly, obesity, cognitive impairment, hypogonadism, and kidney failure. LZTFL1 also acts as a tumor suppressor; possibly by interacting with E-cadherin as well as the actin cytoskeleton and in this manner regulating the transition of epithelial cells to mesenchymal cells.

    • Synonyms

      Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAELGLN EHHQNEVINY MRFARSKRGL RLKTVDSCFQ DLKESRLVED TFTIDEVSEV LNGLQAVVHS EVESELINTA YTNVLLLRQL FAQAEKWYLK LQTDISELEN RELLEQVAEF EKAEITSSNK KPILDVTKPK LAPLNEGGTA ELLNKEILRL QEENEKLKSR LKTIEIQATN ALDEKSKLEK ALQDLQLDQG NQKDFIKAQD LSNLENTVAA LKSEFQKTLN DKTENQKSLE ENLATAKHDL LRVQEQLHMA EKELEKKFQQ TAAYRNMKEI LTKKNDQIKD LRKRLAQYEP ED.

    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.

    Lztfl1 Human
  • View Data Sheet

    Name :

    STK16 Human

    Description:

    Serine/Threonine Kinase 16 Human Recombinant

    Serine/threonine-protein kinase 16, Myristoylated and palmitoylated serine/threonine-protein kinase, MPSK, Protein kinase PKL12, TGF-beta-stimulated factor 1, TSF-1, Tyrosine-protein kinase STK16, hPSK, STK16, MPSK1, PKL12, TSF1, KRCT.

    Product # :

    PKA-032

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    Description

    STK16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-305 a.a) and having a molecular mass of 37.2kDa.STK16 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STK16 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serine/threonine-protein kinase 16 (STK16) is a membrane-associated protein kinase which phosphorylates on serine and threonine residues. STK16 is involved in secretory vesicle trafficking or intracellular signaling. Furthermore, the STK16 protein may have a role in regulating stromal-epithelial interactions which occur during ductal morphogenesis in the mammary gland. STK16 can autophosphorylate on Tyr residue; it is however unclear whether STK16 has tyrosine-protein kinase toward other proteins. STK16 may also be involved in TGF-beta signaling.

    • Synonyms

      Serine/threonine-protein kinase 16, Myristoylated and palmitoylated serine/threonine-protein kinase, MPSK, Protein kinase PKL12, TGF-beta-stimulated factor 1, TSF-1, Tyrosine-protein kinase STK16, hPSK, STK16, MPSK1, PKL12, TSF1, KRCT.

    • 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 MGSHMGHALC VCSRGTVIID NKRYLFIQKL GEGGFSYVDL VEGLHDGHFY ALKRILCHEQ QDREEAQREA DMHRLFNHPN ILRLVAYCLR ERGAKHEAWL LLPFFKRGTL WNEIERLKDK GNFLTEDQIL WLLLGICRGL EAIHAKGYAH RDLKPTNILL GDEGQPVLMD LGSMNQACIH VEGSRQALTL QDWAAQRCTI SYRAPELFSV QSHCVIDERT DVWSLGCVLY AMMFGEGPYD MVFQKGDSVA LAVQNQLSIP QSPRHSSALR QLLNSMMTVD PHQRPHIPLL LSQLEALQPP APGQHTTQI.

    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.

    Stk16 Human
  • View Data Sheet

    Name :

    TIAF1 Human

    Description:

    TGFB1-Induced Anti-Apoptotic Factor 1 Human Recombinant

    TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.

    Product # :

    PRO-1211

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    Description

    TIAF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 152 amino acids (1-115) and having a molecular mass of 16.6 kDa.TIAF1 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TIAF1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TGFB1-induced anti-apoptotic factor 1 (TIAF1) hinders the cytotoxic effects of TNF-alpha and overexpressed TNF receptor adapters TRADD, FADD, and RIPK1. The TIAF1 protein is involved in TGF-beta1 inhibition of IkappaB-alpha expression and suppression of TNF-mediated IkappaB-alpha degradation. TIAF1 is not detected in normal kidney and liver. TIAF1 is up-regulated in chronic and acute allograft rejection: expressed in the inflammatory infiltrate and in tubular epithelial cells.

    • Synonyms

      TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.

    • 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 KDRWGSHMSS PSSPFREQSF LCAAGDAGEE SRVQVLKNEV RRGSPVLLGW VEQAYADKCV CGPSAPPAPT PPSLSQRVMC NDLFKVNPFQ LQQFRADPST ASLLLCPGGL DHKLNLRGKA WG

    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.

    Tiaf1 Human
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