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Search results

667 results found for “Activating Transcription Factor”

Name

Description

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  • View Data Sheet

    Name :

    MED27 Human

    Description:

    Mediator Complex Subunit 27 Human Recombinant

    Mediator Complex Subunit 27, MED27, CRSP8, Cofactor Required For Sp1 Transcriptional Activation, Subunit 8 34kDa, P37 TRAP/SMCC/PC2 Subunit, Transcriptional Coactivator CRSP34, CRSP34, CRSP Complex Subunit 8, CRAP34, TRAP37, Mediator of RNA Polymerase II Transcription Subunit 27, Cofactor Required For Sp1 Transcriptional Activation Subunit 8.

    Product # :

    PRO-1946

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    Description

    MED27 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-311) and having a molecular mass of 37.8 kDa.MED27 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MED27 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Mediator Complex Subunit 27 (MED27) is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, together with TFIID, is necessary for efficient activation by SP1. MED27 is a component of the Mediator complex, a coactivator involved in the regulated transcription of virtually all RNA polymerase II-dependent genes. MED27 protein is also a component of other multisubunit complexes such as the thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. The activation of MED27 gene transcription is a multistep process, which is triggered by factors that identify transcriptional enhancer sites in DNA.

    • Synonyms

      Mediator Complex Subunit 27, MED27, CRSP8, Cofactor Required For Sp1 Transcriptional Activation, Subunit 8 34kDa, P37 TRAP/SMCC/PC2 Subunit, Transcriptional Coactivator CRSP34, CRSP34, CRSP Complex Subunit 8, CRAP34, TRAP37, Mediator of RNA Polymerase II Transcription Subunit 27, Cofactor Required For Sp1 Transcriptional Activation Subunit 8.

    • 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 MGSMADVINV SVNLEAFSQA ISAIQALRSS VSRVFDCLKD GMRNKETLEG REKAFIAHFQ DNLHSVNRDL NELERLSNLV GKPSENHPLH NSGLLSLDPV QDKTPLYSQL LQAYKWSNKL QYHAGLASGL LNQQSLKRSA NQMGVSAKRR PKAQPTTLVL PPQYVDDVIS RIDRMFPEMS IHLSRPNGTS AMLLVTLGKV LKVIVVMRSL FIDRTIVKGY NENVYTEDGK LDIWSKSNYQ VFQKVTDHAT TALLHYQLPQ MPDVVVRSFM TWLRSYIKLF QAPCQRCGKF LQDGLPPTWR DFRTLEAFHD TCRQ.

    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.

    Med27 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.

    Citations

    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 :

    TFF2 Human, His

    Description:

    Trefoil Factor-2 Human Recombinant, His Tag

    TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    Product # :

    CYT-611

    Price :

    Quantity :

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    Shipped at Room temp

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    • Citations

    Description

    TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids (24-129) which includes a 10 amino acid His Tag fused at N-terminus and having a total molecular mass of 13.2 kDa. TFF2 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5, and 20mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.

    • Synonyms

      TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.

    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.

    Tff2 Human His
  • View Data Sheet

    Name :

    TSFM Human

    Description:

    Ts Translation Elongation Factor Mitochondrial Human Recombinant

    Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.

    Product # :

    PRO-1971

    Price :

    Quantity :

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    • description
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    Description

    TSFM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (46-346 a.a) and having a molecular mass of 32.9kDa.TSFM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TSFM is a mitochondrial translation elongation factor which is linked with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. TSFM stays bound to the aminoacyl-tRNA.EF-Tu.GTP complex until the GTP hydrolysis stage on the ribosome. Mutations in TSFM are related with combined oxidative phosphorylation deficiency-3 syndrome.

    • Synonyms

      Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.

    • 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

      MSKELLMKLR RKTGYSFVNC KKALETCGGD LKQAEIWLHK EAQKEGWSKA AKLQGRKTKE GLIGLLQEGN TTVLVEVNCE TDFVSRNLKF QLLVQQVALG TMMHCQTLKD QPSAYSKVQW LTPVNLALWE AEAGGSLEGF LNSSELSGLP AGPDREGSLK DQLALAIGKL GENMILKRAA WVKVPSGFYV GSYVHGAMQS PSLHKLVLGK YGALVICETS EQKTNLEDVG RRLGQHVVGM APLSVGSLDD EPGGEAETKM LSQPYLLDPS ITLGQYVQPQ GVSVVDFVRF ECGEGEEAAE TE.

    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.

    Tsfm Human
  • View Data Sheet

    Name :

    TFF2 Human

    Description:

    Trefoil Factor-2 Human Recombinant

    TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    Product # :

    CYT-612

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • biological activity
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    • Citations

    Description

    TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 106 amino acids (24-129) and having a total molecular mass of 12 kDa. TFF2 Human Recombinant includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds and was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 1mg/mL containing 1x PBS 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 MCF-7 cells using a concentration 1.0-10.0 ng/ml.

    Citations

    More Info

    • Introduction

      Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.

    • Synonyms

      TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 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 TFF2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.

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    Tff2 Human
  • View Data Sheet

    Name :

    ARF1 Human

    Description:

    ADP-Ribosylation Factor 1 Human Recombinant

    ARF-1, ADP-ribosylation factor 1.

    Product # :

    PRO-867

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    Description

    ARF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8 kDa. The ARF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARF1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARF1 is a small guanine nucleotide-binding protein that increases the enzymatic activities of cholera toxin. ARF1 is necessary and ubiquitous in eukaryotes. ARF1 takes part in vesicular transport and functioning via phospholipase D activation. ARF1 is involved in membrane traffic and organelle integrity which are closely tied to their reversible association with membranes and distinct interactions with membrane phospholipids.

    • Synonyms

      ARF-1, ADP-ribosylation 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

      MGSSHHHHHH SSGLVPRGSH MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K.

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    Arf1 Human
  • View Data Sheet

    Name :

    TNFRSF4 Mouse

    Description:

    TNF Receptor Superfamily Member 4 Mouse Recombinant

    Tumor necrosis factor receptor superfamily member 4, OX40 antigen, OX40L receptor, Txgp1, Tnfrsf4, tax-transcriptionally activated glycoprotein 1 receptor, TXGP1L, ACT35, Txgp, Ly-70, ACT3, OX4, CD134.

    Product # :

    CYT-1179

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    Description

    TNFRSF4 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-211) containing 435 amino acids and having a molecular mass of 48.6kDa.TNFRSF4 is fused to a 243 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    TNFRSF4 protein (0.25mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤ 0.4 ug/ml which measured by its binding ability in a functional ELISA with Mouse OX40 Ligand/TNFSF4.

    Citations

    More Info

    • Introduction

      TNFRSF4, also known as TNF Receptor Superfamily Member 4, is a T cell co-stimulatory molecule which belongs to the TNF receptor superfamily. TNFRSF4 coordinates with other co-stimulatory substances such as CD28, CD40, CD30, CD27 and 4-1BB to control the activation of the immune response. TNFRSF4 takes a vital part in antigen-specific T cell expansion as well as survival. TNFRSF4 is up-regulated on CD4+ and CD8+ T cells upon engagement of the TCR by antigen presenting cells along with co-stimulation by CD40-CD40 Ligand and CD28-B7. In addition, TNFRSF4 regulates cytokine production from T cells, antigen presenting cells, natural killer cells and natural killer cells. TNFRSF4 regulates cytokine receptor signaling.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 4, OX40 antigen, OX40L receptor, Txgp1, Tnfrsf4, tax-transcriptionally activated glycoprotein 1 receptor, TXGP1L, ACT35, Txgp, Ly-70, ACT3, OX4, CD134.

    • 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

      DGSMVTARRL NCVKHTYPSG HKCCRECQPG HGMVSRCDHT RDTLCHPCET GFYNEAVNYD TCKQCTQCNH RSGSELKQNC TPTQDTVCRC RPGTQPRQDS GYKLGVDCVP CPPGHFSPGN NQACKPWTNC TLSGKQTRHP ASDSLDAVCE DRSLLATLLW ETQRPTFRPT TVQSTTVWPR TSELPSPPTL VTPEGPLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH

    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.

    Tnfrsf4 Mouse
  • View Data Sheet

    Name :

    PURB Human

    Description:

    Purine-Rich Element Binding Protein B Human Recombinant

    Transcriptional activator protein Pur-beta, Purine-rich element-binding protein B, PURB, PURBETA.

    Product # :

    PRO-1969

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    Description

    PURB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312) and having a molecular mass of 35.6 kDa.PURB is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Purine-Rich Element Binding Protein B (PURB) is a single-stranded DNA-binding protein which takes part in the dendritic transport of a subset of mRNAs. PURB operates as repressor in myoblasts and fibroblasts in the control of vascular smooth muscle alpha-actin gene transcription. PURB binds preferentially to the single strand of the purine-rich element termed PUR, which is present at origins of replication and in gene flanking regions in various eukaryotes from yeasts through humans.

    • Synonyms

      Transcriptional activator protein Pur-beta, Purine-rich element-binding protein B, PURB, PURBETA.

    • 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 MGSMADGDSG SERGGGGGPC GFQPASRGGG EQETQELASK RLDIQNKRFY LDVKQNAKGR FLKIAEVGAG GSKSRLTLSM AVAAEFRDSL GDFIEHYAQL GPSSPEQLAA GAEEGGGPRR ALKSEFLVRE NRKYYLDLKE NQRGRFLRIR QTVNRGGGGF GAGPGPGGLQ SGQTIALPAQ GLIEFRDALA KLIDDYGGED DELAGGPGGG AGGPGGGLYG ELPEGTSITV DSKRFFFDVG CNKYGVFLRV SEVKPSYRNA ITVPFKAWGK FGGAFCRYAD EMKEIQERQR DKLYERRGGG SGGGEESEGE EVDED.

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    Purb Human
  • View Data Sheet

    Name :

    TNF a Rat

    Description:

    Tumor Necrosis Factor-Alpha Rat Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-393

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    Description

    Tumor Necrosis Factor-a Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17339.44 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The concentrated protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer and 0.1M NaCl.

    Purity

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

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 IU/mg.

    Citations

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MLRSSSQNSS DKPVVHVVAN HQAEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLIY SQVLFKGQGC PDYVLLTHTV SRFATSYQEK VSLLSAIKSP CPKDTPEGAE LKPWYEPMYL GGVSQLEKGD LLSAEVNLPK YLDITESGQV YFGVIAL.

    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.

    Tnf Alpha Rat
  • View Data Sheet

    Name :

    TNFR Human, Sf9

    Description:

    Tumor Necrosis Factor Receptor, sf9 Human Recombinant

    Tumor Necrosis Factor Receptor Superfamily Member 9, Tumor Necrosis Factor Receptor Superfamily, Member 9, T-Cell Antigen 4-1BB Homolog, 4-1BB Ligand Receptor, T-Cell Antigen ILA, CD137 Antigen, CDw137, CD137, ILA, Interleukin-Activated Receptor, Homolog Of Mouse Ly63,Induced By Lymphocyte Activation (ILA), Homolog Of Mouse 4-1BB, Receptor Protein 4-1BB, T Cell Antigen ILA, 4-1BB.

    Product # :

    CYT-951

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    Description

    TNFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 411 amino acids (18-186 a.a.) and having a molecular mass of 45.3kDa. (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TNFR is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
      There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
      TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
      Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 9, Tumor Necrosis Factor Receptor Superfamily, Member 9, T-Cell Antigen 4-1BB Homolog, 4-1BB Ligand Receptor, T-Cell Antigen ILA, CD137 Antigen, CDw137, CD137, ILA, Interleukin-Activated Receptor, Homolog Of Mouse Ly63,Induced By Lymphocyte Activation (ILA), Homolog Of Mouse 4-1BB, Receptor Protein 4-1BB, T Cell Antigen ILA, 4-1BB.

    • 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

      ADLFERTRSL QDPCSNCPAG TFCDNNRNQI CSPCPPNSFS SAGGQRTCDI CRQCKGVFRT RKECSSTSNA ECDCTPGFHC LGAGCSMCEQ DCKQGQELTK KGCKDCCFGT FNDQKRGICR PWTNCSLDGK SVLVNGTKER DVVCGPSPAD LSPGASSVTP PAPAREPGHS PQLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

    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.

    Tnfr Human Sf9
  • View Data Sheet

    Name :

    TNF a Mouse

    Description:

    Tumor Necrosis Factor-Alpha Mouse Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-252

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    Description

    Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

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

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.

    Citations

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL

    • Background

      Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.

      TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.

      In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.

      However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.

      In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.

      In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-a 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.

    Tnf Alpha Mouse
  • View Data Sheet

    Name :

    Activin-A Human Plant-Active

    Description:

    Activin-A Human Recombinant, Plant-Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-414

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    Description

    Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4

    Purity

    Greater than 98% as obsereved by SDS-PAGE.

    Biological Activity

    The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.

    • Solubility

      INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.

    • Amino Acid Sequence

      HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
      YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
      NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    • Background

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

      What is the source or expression system of Activin A Protein?
      Nicotiana benthamiana.

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

      What is the Biological Activity of Activin A Protein?
      The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

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

      What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS

      What applications can ACTIVIN-A Protein be used in?

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

       

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    Activin A Active
  • View Data Sheet

    Name :

    TGFB3 Human

    Description:

    Transforming Growth Factor-Beta 3 Human Recombinant

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

    Product # :

    CYT-368

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    Description

    TGF-β 3 Human Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.8kDa. The TGF-β 3 is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20% Ethanol and 10mM Acetic acid (AcOH).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the ability to induce chondrogenic differentiation.

    Citations

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    • 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 clear solution.

    • Stability

      TGF-beta 3 although stable at room temperature for 1 week, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

    • Amino Acid Sequence

      MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

    • Background

      TGFB3 (207 a.a.) Human



      About TGFB3 (207 a.a.) Human:

      Transforming growth factor beta-3 (also known as TGF-β3) is a cytokine encoded by the TGFB3 gene that belongs to the transforming growth factor beta superfamily. It plays a significant role in cell differentiation, embryogenesis, and development by regulating molecules involved in cell adhesion and extracellular matrix formation. TGF-β3 is necessary for palate development, as its absence causes clefting. In addition, it controls lung development and wound healing processes by regulating cell adhesion and movement in the respective tissues. Together, TGF-β3 coordinates a variety of cellular processes that are critical for mammalian embryonic development and tissue homeostasis. In this article we will explore the features and applications of TGFB3 Human Recombinant Protein, expanding on its significance in in advanced research pursuits.

      Description:

      TGFB3 Human Recombinant protein encodes amino acids 644-850 and total molecular mass of 50 kDa (Including GST Tag). As TGFB3 Human derives from Escherichia Coli, it appears as a sterile filtered clear solution and is formulated as 100µl of purified human TGF Beta 3 protein at 100µg/ml. In addition, its protein is formulated in a solution comprising 50mM Tris-Acetate (pH 7.5), 1mM EDTA, and 20% Glycerol. In terms of stability, TGF-beta 3 Human Recombinant is stable at 4°C for up to a week. However, it is preferable to store at -20°C. However, if you are looking to store it for a long term it is preferable to add a carrier protein (0.1% HSA or BSA).

      Activation:

      While TGF-β plays a crucial role regulating essential cell functions, its activation pathways is still being explored and understood. Some pathways are specific to certain cells or tissues, while others are more widespread. Factors like proteases, integrins, pH, and reactive oxygen species can activate TGF-β. Disruptions in these factors can lead to uncontrolled TGF-β signaling, causing issues like inflammation, autoimmune diseases, and cancer.

      Applications and Usage:

      TGFB3 (207 a.a.) Human is intended for laboratory research, serving as an important tool in stem cell differentiation as well as T-cell regulation and differentiation. Accordingly, its versatility extends to applications such as ELISA, Western Blotting, and Inhibition Assays, offering different avenues for discovery and research.

      Safety Information:

      TGFB3 (207 a.a.) Human is intended for use only in laboratory research, in accordance with safety guidelines. It emphasizes adherence to ethical and regulatory norms and is not intended for use as household chemicals, pharmaceuticals, agricultural products, or food additives.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.718 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TGF-b 3 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.

    Tgf Beta 3 Human
  • View Data Sheet

    Name :

    MAFG Human

    Description:

    V-maf Musculoaponeurotic Fibrosarcoma Oncogene G Human Recombinant

    Transcription factor MafG, V-maf musculoaponeurotic fibrosarcoma oncogene homolog G, hMAF, MAFG, hMAF.

    Product # :

    PRO-968

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    Description

    MAFG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-162) and having a molecular mass of 20kDa.MAFG is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Transcription factor MafG (MAFG) is a member of the Maf family. Given that they lack a putative transactivation domain, the small Mafs act as transcriptional repressors when they dimerize amongst themselves. Nevertheless, they seem to function as transcriptional activators by dimerizing with other (generally larger) basic-zipper proteins and engaging them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may function as competitive repressors of the NF-E2 transcription factor.

    • Synonyms

      Transcription factor MafG, V-maf musculoaponeurotic fibrosarcoma oncogene homolog G, hMAF, MAFG, hMAF.

    • 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 MTTPNKGNKA LKVKREPGEN GTSLTDEELV TMSVRELNQH LRGLSKEEIV QLKQRRRTLK NRGYAASCRV KRVTQKEELE KQKAELQQEV EKLASENASM KLELDALRSK YEALQTFART VARSPVAPAR GPLAAGLGPL VPGKVAATSV ITIVKSKTDA RS.

    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.

    Mafg Human
  • View Data Sheet

    Name :

    TNF a Rabbit

    Description:

    Tumor Necrosis Factor-Alpha Rabbit Recombinant

    Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2. 

    Product # :

    CYT-008

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    Description

    Tumor Necrosis Factor-a Rabbit Recombinant consists of three identical polypeptide chains of 158 amino acids combined to form a compact, bell-shaped homotrimer. TNF-alpha was produced in E.Coli is a non-glycosylated, polypeptide chain having a molecular mass of 17.4 kDa for the individual subunit. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF-alpha Rabbit was lyophilized after extensive dialysis against 20mM PB, pH7.4, 300mM NaCl.

    Purity

    Greater than 95% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is less than 0.03ng/ml, corresponding to a Specific Activity of 30,000,000 IU/mg.

    Citations

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    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ser-Ala-Ser-Arg.

    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.

    Tnf A Rabbit
  • View Data Sheet

    Name :

    M CSF Rat HEK

    Description:

    Macrophage Colony Stimulating Factor Rat Recombinant HEK

    CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-046

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    Description

    MCSF Rat Recombinant produced in HEK-293 cells is a secreted protein (amino acids Glu33-Arg254). M-CSF is disulfide-linked homodimer containing 2 x 222 a.a chains.

    Source

    HEK293

    Formulation

    The recombinant MCSF was lyophilized after extensive dialysis against PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of mouse M-NFS-60 cells.

    Citations

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    • Introduction

      Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    M Csf Rat
  • View Data Sheet

    Name :

    TGFB3 Rat

    Description:

    Transforming Growth Factor-Beta 3 Rat Recombinant

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

    Product # :

    CYT-1269

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    Description

    TGFB3 Rat Recombinant produced in CHO cells is a glycosylated, polypeptide homodimer chain containing 2x112 amino acids and having a total molecular mass of 25.0kDa. The TGFB3 is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    TGFB3 was lyophilized from a concentrated solution containing 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

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    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Transforming Growth Factor-Beta 3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 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 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSSDTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

    • Background

      Recombinant TGF-β3 Rat is commonly used in cell culture and biomedical research to investigate TGF-β signalling, stem cell differentiation, tissue engineering, chondrogenesis, wound healing, fibrosis, and cancer biology. TGFB3 is added to mesenchymal stem cell and chondrocyte cultures to promote cartilage formation and maintain specific cellular phenotypes under defined experimental conditions.

      What is the molecular weight / Mw of TGFB3 Rat Protein?
      TGFB3 Rat Protein has a total Mw of 25kDa.

      What is the source or expression system of TGFB3 Rat Protein?
      CHO Cells

      What is the Purity of TGFB3 Rat Protein?
      TGFB3 rat Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of TGFB3 rat Protein?
      Determined by the ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0×107 units/mg.

      What is the amino acid sequence of TGFB3 Protein?
      ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS

      What applications can TGFB3 rat Protein be used in?
      TGFB3 rat Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for TGFB3 rat Protein?
      The endotoxin level is minimal, TGFB3 rat Protein was purified using conventional chromatography techniques.

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

    TGFB3 Rat
  • View Data Sheet

    Name :

    TGFB3 Human, HEK

    Description:

    Transforming Growth Factor-Beta 3 Human Recombinant, HEK

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

    Product # :

    CYT-113

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    Description

    TGF-beta 3 Human Recombinant produced in HEK cells is a homodimer containing 2 x 112 amino acids linked by a disulfide bond having a total molecular weight of 25kDa. The TGF-b 3 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The TGF-b 3 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2) and is typically 0.05 ng/ml corresponding to a specific activity of ≥ 20,000,000 units/mg.

    Citations

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    • 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 TGF-b 3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 3 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 TGF-b 3 in sterile 4mM HCl containing 0.1% endotoxin-free recombinant HSA.

    • Amino Acid Sequence

      MALDTNYCFR NLEENCCVRP LYIDFRQDLG WKWVHEPKGY YANFCSGPCP YLRSADTTHS TVLGLYNTLN PEASASPCCV PQDLEPLTIL YYVGRTPKVE QLSNMVVKSC KCS




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

    Tgf B 3 Human Hek
  • View Data Sheet

    Name :

    TNFRSF8 igG-His Human

    Description:

    CD30 Ligand Receptor, IgG-His Tag Human Recombinant

    Tumor Necrosis Factor Receptor Superfamily Member 8, Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1.

    Product # :

    CYT-983

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    Description

    TNFRSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 613 amino acids (19-379 a.a.) and having a molecular mass of 66.7kDa (Molecular size on SDS-PAGE will appear at approximately 25-100kDa). TNFRSF8 is expressed with a 252 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 8, Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-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

      ADPFPQDRPF EDTCHGNPSH YYDKAVRRCC YRCPMGLFPT QQCPQRPTDC RKQCEPDYYL DEADRCTACV TCSRDDLVEK TPCAWNSSRV CECRPGMFCS TSAVNSCARC FFHSVCPAGM IVKFPGTAQK NTVCEPASPG VSPACASPEN CKEPSSGTIP QAKPTPVSPA TSSASTMPVR GGTRLAQEAA SKLTRAPDSP SSVGRPSSDP GLSPTQPCPE GSGDCRKQCE PDYYLDEAGR CTACVSCSRD DLVEKTPCAW NSSRTCECRP GMICATSATN SCARCVPYPI CAAETVTKPQ DMAEKDTTFE APPLGTQPDC NPTPENGEAP ASTSPTQSLL VDSQASKTLP IPTSAPVALS STGKAAAFES RACSLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

    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.

    Tnfrsf8 Igg His Human
  • View Data Sheet

    Name :

    TGFB1 (113 a.a.) Human

    Description:

    Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant

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

    Product # :

    CYT-679

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    Description

    TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 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 beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 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

      MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.

    • Background

      Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential

      Abstract:


      Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.

      Introduction:


      TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.

      Production Process and Characteristics:


      TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.

      Therapeutic Applications:


      TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.

      Advantages and Challenges:


      The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.

      Conclusion:


      TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

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    Tgf Beta 1 Human 113 Aa
  • View Data Sheet

    Name :

    CREB3L2 Human

    Description:

    CAMP Responsive Element Binding Protein 3-Like 2 Human Recombinant

    CAMP Responsive Element Binding Protein 3-Like 2, BBF2H7, CAMP-Responsive Element-Binding Protein 3-Like Protein 2, BBF2 Human Homolog On Chromosome 7, Cyclic AMP-Responsive Element-Binding Protein 3-Like Protein 2, Basic Transcription Factor 2, B-ZIB Transcription Factor, FUS/BBF2H7 Protein, TCAG_1951439, Cyclic AMP-responsive element-binding protein 3-like protein 2, cAMP-responsive element-binding protein 3-like protein 2.

    Product # :

    PRO-2153

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    Description

    CREB3L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-378 a.a) and having a molecular mass of 44kDa. CREB3L2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CREB3L2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CAMP Responsive Element Binding Protein 3-Like 2, also known as CREB3L2 belongs to the oasis bZIP transcription factor family. Members of this family are able to dimerize however from homodimers only. CREB3L2 is a transcriptional activator. Translocations between CREB3L2 on chromosome 7 and the gene fused in sarcoma on chromosome 16 can be found in some tumors. One disease which is associated with CREB3L2 is myxofibrosarcoma.

    • Synonyms

      CAMP Responsive Element Binding Protein 3-Like 2, BBF2H7, CAMP-Responsive Element-Binding Protein 3-Like Protein 2, BBF2 Human Homolog On Chromosome 7, Cyclic AMP-Responsive Element-Binding Protein 3-Like Protein 2, Basic Transcription Factor 2, B-ZIB Transcription Factor, FUS/BBF2H7 Protein, TCAG_1951439, Cyclic AMP-responsive element-binding protein 3-like protein 2, cAMP-responsive element-binding protein 3-like protein 2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEVLESG EQGVLQWDRK LSELSEPGDG EALMYHTHFS ELLDEFSQNV LGQLLNDPFL SEKSVSMEVE PSPTSPAPLI QAEHSYSLCE EPRAQSPFTH ITSDSFNDDE VESEKWYLST DFPSTSIKTE PITDEPPPGL VPSVTLTITA ISTPLEKEEP PLEMNTGVDS SCQTIIPKIK LEPHEVDQFL NFSPKEAPVD HLHLPPTPPS SHGSDSEGSL SPNPRLHPFS LPQTHSPSRA APRAPSALSS SPLLTAPHKL QGSGPLVLTE EEKRTLIAEG YPIPTKLPLS KSEEKALKKI RRKIKNKISA QESRRKKKEY MDSLEKKVES CSTENLELRK KVEVLENTNR TLLQQLQKLQ TLVMGKVSRT CKLAGTQTGT 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.

    Creb3L2 Human
  • View Data Sheet

    Name :

    Tissue Factor Human, Active

    Description:

    Coagulation Factor III Active Human Recombinant

    Tissue factor, TF, Coagulation factor III, CD142.

    Product # :

    PRO-2845

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    Description

    Recombinant Human Tissue Factor Active is a glycosylated, polypeptide chain containing 225 amino acids and having a total molecular mass of 45.0kDa. Coagulation Factor III is fused at C-terminus & is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    Lyophilized from a 0.2μm filtered solution in 20mM Tris and 150mM NaCl, pH 8.0.

    Purity

    Greater than 98.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The ED50 was determined by its ability to activate fluorogenic peptide substrate Boc-VPR-AMC cleavage, when bound in 1:1 complex with Coagulation Factor VII.

    Citations

    More Info

    • Synonyms

      Tissue factor, TF, Coagulation factor III, CD142.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SGTTNTVAAY NLTWKSTNFK TILEWEPKPV NQVYTVQIST KSGDWKSKCF YTTDTECDLT DEIVKDVKQT YLARVFSYPA GNVESTGSAG EPLYENSPEF TPYLETNLGQ PTIQSFEQVG TKVNVTVEDE RTLVRRNNTF LSLRDVFGKD LIYTLYYWKS SSSGKKTAKT NTNEFLIDVD KGENYCFSVQ AVIPSRTVNR KSTDSPVECM GQEKGEFREH HHHHH.

    • Background

      Tissue Factor is the main initiator of the extrinsic blood coagulation pathway. after vascular injury, Tissue Factor binds circulating Factor VII/VIIa, forming the TF–FVIIa complex, which activates Factors IX and X, leading to thrombin generation and fibrin clot formation. Tissue Factor also participates in cell signalling influencing inflammation, angiogenesis, wound healing, and tumor progression.

      What is the molecular weight / Mw of Tissue Factor Protein?
      Tissue Factor Protein has a total Mw of 45kDa.

      What is the source or expression system of Tissue Factor Protein?
      CHO Cells

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

      What is the Biological Activity of Tissue Factor Protein?
      The enzymatic activity was determined by its ability to activate fluorogenic peptide substrate Boc-VPR-AMC cleavage, when bound in 1:1 complex with Coagulation Factor VII.

      What is the amino acid sequence of Tissue Factor Protein?
      SGTTNTVAAY NLTWKSTNFK TILEWEPKPV NQVYTVQIST KSGDWKSKCF YTTDTECDLT DEIVKDVKQT YLARVFSYPA GNVESTGSAG EPLYENSPEF TPYLETNLGQ PTIQSFEQVG TKVNVTVEDE RTLVRRNNTF LSLRDVFGKD LIYTLYYWKS SSSGKKTAKT NTNEFLIDVD KGENYCFSVQ AVIPSRTVNR KSTDSPVECM GQEKGEFREH HHHHH

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

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

    Tissue Factor Human, Active
  • View Data Sheet

    Name :

    TNF a Human, Sf9

    Description:

    Tumor Necrosis Factor-alpha Human Recombinant, Sf9

    Tumor Necrosis Factor, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis factor.

    Product # :

    CYT-903

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    Description

    TNF a produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 163 amino acids (77-233a.a.) and having a molecular mass of 18.1kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). TNF a is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNF a protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined bySDS-PAGE.

    Biological Activity

    Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D. 
    The ED50 for this effect is ≤ 0.2 ng/ml.

    Citations

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      Tumor Necrosis Factor, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis factor.

    • 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

      VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELRDNQLVV PSEGLYLIYS QVLFKGQGCP STHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINRPD YLDFAESGQV YFGIIALHHH HHH.

    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.

    Tnf A Human Sf9
  • View Data Sheet

    Name :

    TRAIL Mouse

    Description:

    TNF-Related Apoptosis Inducing Ligand/Apo2L Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10. 

    Product # :

    CYT-806

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    Description

    TRAIL Recombinant Mouse produced in E.coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20.2kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized containing PBS, pH 7.4, and 3mM DTT.

    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 cytotoxicity assay using murine L929 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2,000,000 IU/mg in the presence of actinomycin D.

    Citations

    More Info

    • Introduction

      TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPRGGRPQKV AAHITGITRR SNSALIPISK DGKTLGQKIE SWESSRKGHS FLNHVLFRNG ELVIEQEGLY YIYSQTYFRF QEAEDASKMV SKDKVRTKQL VQYIYKYTSY PDPIVLMKSA RNSCWSRDAE YGLYSIYQGG LFELKKNDRI FVSVTNEHLM DLDQEASFFG AFLIN

    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.

    Trail Mouse
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