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Search results

1000 results found for “Transferrin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Follistatin Human, His

    Description:

    Follistatin Human Recombinant, His Tag

    FST, FS, Activin-binding protein.

    Product # :

    CYT-029

    Price :

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    • source
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    Description

    FST His Protein is 36.0 kDa protein containing 325 amino acid residues of the FST His and the 10 aa N-Terminal His-tag.

    Source

    E. coli.

    Formulation

    FST His Tag was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.

    More Info

    • Introduction

      Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

    • Synonyms

      FST, FS, Activin-binding protein.

    • Stability

      Store lyophilized FST His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted FST His can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.

    • Background

      What is the molecular weight/Mw of FOLLISTATIN HUMAN, HIS Protein?
      FOLLISTATIN HUMAN, HIS Protein has a total Mw of 36kDa.

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

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

      What is the amino acid sequence of FOLLISTATIN HUMAN, HIS Protein?
      MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.

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

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

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

    Fst His Human
  • View Data Sheet

    Name :

    L Selectin Human

    Description:

    L-selectin Human Recombinant

    L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.

    Product # :

    PRO-381

    Price :

    Quantity :

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    • More Info

    Description

    L-Selectin Human Recombinant is expressed in E. coli containing 294 amino acids 39-332 fused to an amino terminal hexahistidine tag, having a total molecular weight of 37.55kDa.

    Source

    Escherichia Coli.

    Formulation

    L-Sel is supplied in 1x PBS and 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    More Info

    • Introduction

      L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
      L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
      L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.

    • Synonyms

      L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Applications

      L-Selectin can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    L Selectin Human
  • View Data Sheet

    Name :

    TRIM33 Human

    Description:

    Tripartite Motif Containing 33 Human Recombinant

    E3 ubiquitin-protein ligase TRIM33, Ectodermin homolog, RET-fused gene 7 protein, Protein Rfg7, Transcription intermediary factor 1-gamma, TIF1-gamma, Tripartite motif-containing protein 33, TRIM33, KIAA1113, RFG7, TIF1G, ECTO, PTC7, TF1G, TIFGAMMA, TIF1GAMMA.

    Product # :

    PRO-1506

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
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    Description

    TRIM33 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 124,041 Dalton. TRIM33 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    TRIM33 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tripartite Motif Containing 33 (TRIM33) belongs to the tripartite motif family. This motif includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM33 is assumed to be a transcriptional corepressor. TRIM33 functions as an E3 ubiquitin-protein ligase. TRIM33 also promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. In addition, TRIM33 inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Furthermore, TRIM33 has a role in the control of cell proliferation.

    • Synonyms

      E3 ubiquitin-protein ligase TRIM33, Ectodermin homolog, RET-fused gene 7 protein, Protein Rfg7, Transcription intermediary factor 1-gamma, TIF1-gamma, Tripartite motif-containing protein 33, TRIM33, KIAA1113, RFG7, TIF1G, ECTO, PTC7, TF1G, TIFGAMMA, TIF1GAMMA.

    • 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. Avoid multiple freeze-thaw cycles.

    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.

    Trim33 Human
  • View Data Sheet

    Name :

    TWF1 Human

    Description:

    Twinfilin-1 Human Recombinant

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

    Product # :

    PRO-1003

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    • More Info

    Description

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

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Twf1 Human
  • View Data Sheet

    Name :

    TXNRD1 Human 161-649 a.a.

    Description:

    Thioredoxin Reductase 1 161-649 a.a. Human Recombinant

    Thioredoxin reductase 1 cytoplasmic, TR, Gene associated with retinoic and interferon-induced mortality 12 protein, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.

    Product # :

    ENZ-042

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    Description

    TXNRD1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 510 amino acids (161-649 a.a.) and having a molecular mass of 55.9kDa. The TXNRD1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TXNRD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TXNRD1 belongs to the selenium-containing pyridine nucleotide-disulphide oxidoreductase family, which has a conserved catalytic site of Cys-Val-Asn-Val-Gly-Cys. TXNRD1 decreases thioredoxins as well as other substrates, and participates in selenium metabolism and protection against oxidative stress. Inhibition of TXNRD1 activity serves as a potential treatment for cancer, AIDS and other autoimmune diseases as well as bacterial infections and parasitic diseases.

    • Synonyms

      Thioredoxin reductase 1 cytoplasmic, TR, Gene associated with retinoic and interferon-induced mortality 12 protein, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.

    • 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 MYDYDLIIIG GGSGGLAAAK EAAQYGKKVM VLDFVTPTPL GTRWGLGGTC VNVGCIPKKL MHQAALLGQA LQDSRNYGWK VEETVKHDWD RMIEAVQNHI GSLNWGYRVA LREKKVVYEN AYGQFIGPHR IKATNNKGKE KIYSAERFLI ATGERPRYLG IPGDKEYCIS SDDLFSLPYC PGKTLVVGAS YVALECAGFL AGIGLDVTVM VRSILLRGFD QDMANKIGEH MEEHGIKFIR QFVPIKVEQI EAGTPGRLRV VAQSTNSEEI IEGEYNTVML AIGRDACTRK IGLETVGVKI NEKTGKIPVT DEEQTNVPYI YAIGDILEDK VELTPVAIQA GRLLAQRLYA GSTVKCDYEN VPTTVFTPLE YGACGLSEEK AVEKFGEENI EVYHSYFWPL EWTIPSRDNN KCYAKIICNT KDNERVVGFH VLGPNAGEVT QGFAAALKCG LTKKQLDSTI GIHPVCAEVF TTLSVTKRSG ASILQAGCCG.

    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.

    Txnrd1 Human 161 649 Aa
  • View Data Sheet

    Name :

    PTMA Human

    Description:

    Prothymosin Alpha Human Recombinant

    Prothymosin alpha, TMSA, PTMA, Prothymosin alpha, N-terminally processed, Thymosin alpha-1.

    Product # :

    PRO-1694

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    Description

    PTMA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-110) and having a molecular mass of 14.5 kDa.PTMA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTMA solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Prothymosin alpha (PTMA) is a part of the pro/parathymosin family. PTMA mediates immune function by conferring resistance to some opportunistic infections.

    • Synonyms

      Prothymosin alpha, TMSA, PTMA, Prothymosin alpha, N-terminally processed,
      Thymosin alpha-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 MGSMSDAAVD TSSEITTKDL KEKKEVVEEA ENGRDAPANG NANEENGEQE ADNEVDEEEE EGGEEEEEEE EGDGEEEDGD EDEEAESATG KRAAEDDEDD DVDTKKQKTD EDD.

    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.

    Ptma Human
  • View Data Sheet

    Name :

    AAGAB Human

    Description:

    Alpha & Gamma-Adaptin Binding Protein Human Recombinant

    P34, Alpha- and gamma-adaptin-binding protein p34.

    Product # :

    PRO-1479

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    Description

    AAGAB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-315 a.a.) and having a molecular mass of 36.7kDa.AAGAB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.

    • Synonyms

      P34, Alpha- and gamma-adaptin-binding protein p34.

    • 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 MAAGVPCALV TSCSSVFSGD QLVQHILGTE DLIVEVTSND AVRFYPWTID NKYYSADINL CVVPNKFLVT AEIAESVQAF VVYFDSTQKS GLDSVSSWLP LAKAWLPEVM ILVCDRVSED GINRQKAQEW CIKHGFELVE LSPEELPEED DDFPESTGVK RIVQALNANV WSNVVMKNDR NQGFSLLNSL TGTNHSIGSA DPCHPEQPHL PAADSTESLS DHRGGASNTT DAQVDSIVDP MLDLDIQELA SLTTGGGDVE NFERLFSKLK EMKDKAATLP HEQRKVHAEK VAKAFWMAIG GDRDEIEGLS SDEEH.

    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.

    Aagab Human
  • View Data Sheet

    Name :

    MGAT2 Human

    Description:

    Mannoside Acetylglucosaminyltransferase 2 Human Recombinant

    Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.

    Product # :

    ENZ-781

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    Description

    MGAT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (30-447a.a) and having a molecular mass of 50kDa. MGAT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MGAT2 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.

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    • Introduction

      Mannoside Acetylglucosaminyltransferase 2 (MGAT2) is a golgi enzyme catalyzing an vital step in the conversion of oligomannose to complex N-glycans. MGAT2 enzyme has the characteristic glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. MGAT2 gene mutations may lead to carbohydrate-deficient glycoprotein syndrome, type II.

    • Synonyms

      Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MRQRKNEALA PPLLDAEPAR GAGGRGGDHP SVAVGIRRVS NVSAASLVPA VPQPEADNLT LRYRSLVYQL NFDQTLRNVD KAGTWAPREL VLVVQVHNRP EYLRLLLDSL RKAQGIDNVL VIFSHDFWST EINQLIAGVN FCPVLQVFFP FSIQLYPNEF PGSDPRDCPR DLPKNAALKL GCINAEYPDS FGHYREAKFS QTKHHWWWKL HFVWERVKIL RDYAGLILFL EEDHYLAPDF YHVFKKMWKL KQQECPECDV LSLGTYSASR SFYGMADKVD VKTWKSTEHN MGLALTRNAY QKLIECTDTF CTYDDYNWDW TLQYLTVSCL PKFWKVLVPQ IPRIFHAGDC GMHHKKTCRP STQSAQIESL LNNNKQYMFP ETLTISEKFT VVAISPPRKN GGWGDIRDHE LCKSYRRLQ.

    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.

    Mgat2 Human
  • View Data Sheet

    Name :

    SERPINA3

    Description:

    Alpha-1 AntiChymotrypsin Human Recombinant

    Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    Product # :

    PRO-750

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    Description

    SERPINA3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.The SERPINA3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINA3 solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1-ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
      Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT.

    • Synonyms

      Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    • 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 MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ A.

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

    Serpina3 Human Recombinant
  • View Data Sheet

    Name :

    ANXA13 Human

    Description:

    Annexin A13 Human Recombinant

    Annexin A13, Annexin XIII, Annexin-13, Intestine-specific annexin, ISA, ANXA13, ANX13, MGC150460.

    Product # :

    PRO-197

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    Description

    ANXA13 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 336 amino acids (1-316 a.a.) and having a molecular mass of 37.5kDa. The ANXA13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA13 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Annexin A13 (ANXA13) belongs to the annexin protein family, whose members play a role in cytoskeletal interactions, phospholipase inhibition, regulation of cellular growth, and intracellular signal transduction pathways. ANXA13 is believed to be the original originator of the 12 members of vertebrate annexins. ANXA13 expression is decidedly tissue-specific, being expressed only in intestinal and kidney epithelial cells. This expression is linked with a highly differentiated intracellular transport function.

    • Synonyms

      Annexin A13, Annexin XIII, Annexin-13, Intestine-specific annexin, ISA, ANXA13, ANX13, MGC150460.

    • 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 MGNRHAKASS PQGFDVDRDA KKLNKACKGM GTNEAAIIEI LSGRTSDERQ QIKQKYKATY GKELEEVLKS ELSGNFEKTA LALLDRPSEY AARQLQKAMK GLGTDESVLI EVLCTRTNKE IIAIKEAYQR LFDRSLESDV KGDTSGNLKK ILVSLLQANR NEGDDVDKDL AGQDAKDLYD AGEGRWGTDE LAFNEVLAKR SYKQLRATFQ AYQILIGKDI EEAIEEETSG DLQKAYLTLV RCAQDCEDYF AERLYKSMKG AGTDEETLIR IVVTRAEVDL QGIKAKFQEK YQKSLSDMVR SDTSGDFRKL LVALLH.

    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.

    Anxa13 Human
  • View Data Sheet

    Name :

    PFN4 Human

    Description:

    Profilin-4 Human Recombinant

    PFN-4, Profilin-IV, Profilin4.

    Product # :

    PRO-818

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    Description

    PFN4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 149 amino acids (1-129 a.a.) and having a molecular mass of 16.4 kDa. PFN4 protein is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN4 Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      PFN4 is a small actin-binding protein that participates in the dynamic turnover and restructuring of the actin cytoskeleton. PFN4 is localized in all eukaryotic organisms in the majority of cells. PFN4 is crucial for spatially and temporally controlled growth of actin microfilaments, which is a necessary process in cellular locomotion and cell shape changes.

    • Synonyms

      PFN-4, Profilin-IV, Profilin4.

    • 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 MSHLQSLLLD TLLGTKHVDS AALIKIQERS LCVASPGFNV TPSDVRTLVN GFAKNPLQAR REGLYFKGKD YRCVRADEYS LYAKNENTGV VVVKTHLYLL VATYTEGMYP SICVEATESL GDYLRKKGS.

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    Pfn4 Human
  • View Data Sheet

    Name :

    THAP7 Human

    Description:

    THAP Domain Containing, Apoptosis Associated Protein 7 Human Recombinant

    THAP domain containing 7, THAP7.

    Product # :

    PRO-1989

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    Description

    THAP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 332 amino acids (1-309 a.a) and having a molecular mass of 36.8kDa. THAP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    THAP7 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.

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    • Introduction

      THAP Domain Containing, Apoptosis Associated Protein 7 (THAP7) holds one THAP-type zinc finger. THAP7 is a chromatin-associated, histone tail-binding protein which represses transcription by recruiting HDAC3 and nuclear hormone receptor corepressors.

    • Synonyms

      THAP domain containing 7, THAP7.

    • 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 MGSMPRHCSA AGCCTRDTRE TRNRGISFHR LPKKDNPRRG LWLANCQRLD PSGQGLWDPA SEYIYFCSKH FEEDCFELVG ISGYHRLKEG AVPTIFESFS KLRRTTKTKG HSYPPGPAEV SRLRRCRKRC SEGRGPTTPF SPPPPADVTC FPVEEASAPA TLPASPAGRL EPGLSSPFSD LLGPLGAQAD EAGCSAQPSP ERQPSPLEPR PVSPSAYMLR LPPPAGAYIQ NEHSYQVGSA LLWKRRAEAA LDALDKAQRQ LQACKRREQR LRLRLTKLQQ ERAREKRAQA DARQTLKEHV QDFAMQLSSS MA.

    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.

    Thap7 Human
  • View Data Sheet

    Name :

    Thrombin Human

    Description:

    Thrombin Human Recombinant

    Coagulation Factor II (Thrombin), Prepro-Coagulation Factor II, EC 3.4.21.5, RPRGL2, THPH1, Coagulation Factor II, Prothrombin B-Chain, Serine Protease, Prothrombin, EC 3.4.21, PT, F2.

    Product # :

    PRO-1954

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    Description

    Thrombin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (328-622) and having a molecular mass of 33.9 kDa.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

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    • Introduction

      Coagulation factor II (F2) is proteolytically cleaved to form thrombin in the 1st step of the coagulation cascade which ultimately results in the stemming of blood loss. F2 also has a role in preserving vascular integrity during development and postnatal life. F2 gene mutations lead to various forms of thrombosis and dysprothrombinemia.

    • Synonyms

      Coagulation Factor II (Thrombin), Prepro-Coagulation Factor II, EC 3.4.21.5, RPRGL2, THPH1, Coagulation Factor II, Prothrombin B-Chain, Serine Protease, Prothrombin, EC 3.4.21, PT, F2.

    • 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

      MTFGSGEADC GLRPLFEKKS LEDKTERELL ESYIDGRIVE GSDAEIGMSP WQVMLFRKSP QELLCGASLI SDRWVLTAAH CLLYPPWDKN FTENDLLVRI GKHSRTRYER NIEKISMLEK IYIHPRYNWR ENLDRDIALM KLKKPVAFSD YIHPVCLPDR ETAASLLQAG YKGRVTGWGN LKETWTANVG KGQPSVLQVV NLPIVERPVC KDSTRIRITD NMFCAGYKPD EGKRGDACEG DSGGPFVMKS PFNNRWYQMG IVSWGEGCDR DGKYGFYTHV FRLKKWIQKV IDQFGE.

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    Human Thrombin
  • View Data Sheet

    Name :

    Troponin-C2 Human

    Description:

    Troponin-C2 Human Recombinant

    Troponin C, skeletal muscle, TNNC2.

    Product # :

    PRO-2572

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    Description

    Troponin-C2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 160 amino acids having a molecular mass of 18.1kDa. The Recombinant Human Troponin-C2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20 mM Tris-HCl buffer (pH 7.5), 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Troponin-C2 (Troponin C, skeletal muscle) is the central regulatory antigen of striated muscle contraction, and modulates the Ca2+-activation characteristics of muscle fibers. Troponin-C2 has three subunits, Troponin I(Tn-1), Troponin T(Tn-T) and Troponin C(Tn-C). Tn-I subunit inhibits actomyosin ATPase and Tn-T subunit binds tropomyosin and Tn-C, while Tn-C subunit binds calcium and overcomes the inhibitory action of the troponin complex on actin filaments. Mutations in all components of this complex have been linked with skeletal muscle disease.

    • Synonyms

      Troponin C, skeletal muscle, TNNC2.

    • 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

      MTDQQAEARS YLSEEMIAEF KAAFDMFDAD GGGDISVKEL GTVMRMLGQT PTKEELDAII EEVDEDGSGT IDFEEFLVMM VRQMKEDAKG KSEEELAECF RIFDRNADGY IDPEELAEIF RASGEHVTDE EIESLMKDGD KNNDGRIDFD EFLKMMEGVQ.

    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.

    Troponin C2
  • View Data Sheet

    Name :

    TTC32 Human

    Description:

    Tetratricopeptide Repeat Domain 32 Human Recombinant

    Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.

    Product # :

    PRO-1246

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    Description

    TTC32 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-151) and having a molecular mass of 19.7 kDa. TTC32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TTC32 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TTC32 contains 3 TPR repeats. The tetratricopeptide repeat (TPR) is a structural motif. TPR is observed in organized 3–16 motifs, which form scaffolds to mediate protein–protein interactions and frequently the assembly of multiprotein complexes. TPR-containing proteins include the anaphase-promoting complex subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, the major receptor for peroxisomal matrix protein import PEX5, the PKR protein kinase inhibitor and mitochondrial import proteins.

    • Synonyms

      Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.

    • 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 MGSMEGQRQE SHATLTLAQA HFNNGEYAEA EALYSAYIRR CACAASSDES PGSKCSPEDL ATAYNNRGQI KYFRVDFYEA MDDYTSAIEV QPNFEVPYYN RGLILYRLGY FDDALEDFKK VLDLNPGFQD ATLSLKQTIL DKEEKQRRNV AKNY.

    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.

    Ttc32 Human
  • View Data Sheet

    Name :

    Agrin Rat

    Description:

    Agrin Rat Recombinant

    Agrin, Agrn, C90, C22, Agrin N-terminal 110 kDa subunit, Agrin C-terminal 110 kDa subunit, Agrin C-terminal 90 kDa fragment, Agrin C-terminal 22 kDa fragment, AGR

    Product # :

    PRO-2627

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    Description

    Agrin Rat produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 766 amino acids (997-1753 a.a.) and having a molecular mass of 82.5kDa.Agrin is fused to a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Agrin solution (0.5mg/ml) contains 10% Glycerol in Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Agrin or AGRN is a large protein (proteoglycan) that has a crucial part in the development of neuromuscular junction amid embryogenesis. The protein has an involvement in the collection and aggregation of acetylcholine receptors through synaptogenesis. The agrin gene can be found and expressed in rat embryonic nervous system andmuscle tissue. This Agrin protein is aggregated in the synapses, there it can take part in regeneration & development. The protein binds to receptors on the surface of skeletal muscle.

    • Synonyms

      Agrin, Agrn, C90, C22, Agrin N-terminal 110 kDa subunit, Agrin C-terminal 110 kDa subunit, Agrin C-terminal 90 kDa fragment, Agrin C-terminal 22 kDa fragment, AGR

    • 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

      ADPSCYNSPL GCCSDGKTPS LDSEGSNCPA TKAFQGVLEL EGVEGQELFY TPEMADPKSE LFGETARSIE STLDDLFRNS DVKKDFWSVR LRELGPGKLV RAIVDVHFDP TTAFQASDVG QALLRQIQVS RPWALAVRRP LQEHVRFLDF DWFPTFFTGA ATGTTAAMAT ARATTVSRLP ASSVTPRVYP SHTSRPVGRT TAPPTTRRPP TTATNMDRPR TPGHQQPSKS CDSQPCLHGG
      TCQDQDSGKG FTCSCTAGRG GSVCEKVQPP SMPAFKGHSF LAFPTLRAYH TLRLALEFRA LETEGLLLYN GNARGKDFLA LALLDGRVQF RFDTGSGPAV LTSLVPVEPG RWHRLELSRH WRQGTLSVDG ETPVVGESPS GTDGLNLDTN LYVGGIPEEQ VAMVLDRTSV GVGLKGCIRM LDINNQQLEL SDWQRAAVQS SGVGECGDHP CLPNPCHGGA LCQALEAGMF LCQCPPGRFG PTCADEKSPC QPNPCHGAAP CRVLSSGGAK CECPLGRSGT FCQTVLETAG SRPFLADFNG FSYLELKGLH TFERDLGEKM ALEMVFLARG PSGLLLYNGQ KTDGKGDFVS LALHNRHLEF CYDLGKGAAV IRSKEPIALG TWVRVFLERN GRKGALQVGD GPRVLGESPK SRKVPHTMLN LKEPLYIGGA PDFSKLARGA AVSSGFSGVI QLVSLRGHQL LTQEHVLRAV DVSPFADHPC TQALGNPCLN GGSCVPREAT YECLCPGGFS GLHCEKGLVE HHHHHH

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

    Agrin Protein Rat
  • View Data Sheet

    Name :

    B3GNT2 Human

    Description:

    Beta-1,3-N-Acetylglucosaminyltransferase 2 Human Recombinant

    B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.

    Product # :

    ENZ-973

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    Description

    B3GNT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 375 amino acids (29-397a.a.) and having a molecular mass of 43.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). B3GNT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    B3GNT2 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.

    More Info

    • Introduction

      Beta-1,3-N-Acetylglucosaminyltransferase 2 (B3GNT2) is a part of the beta-1,3-N-acetylglucosaminyltransferase family which takes part in the synthesis of poly-N-acetyllactosamine. B3GNT2 is a type II transmembrane protein which prefers the substrate of lacto-N-neotetraose. B3GNT2 catalyzes the initiation and elongation of poly-N-acetyllactosamine chains and comprises the main polylactosamine synthase.

    • Synonyms

      B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.

    • 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

      ADPKSSSQEK NGKGEVIIPK EKFWKISTPP EAYWNREQEK LNRQYNPILS MLTNQTGEAG RLSNISHLNY CEPDLRVTSV VTGFNNLPDR FKDFLLYLRC RNYSLLIDQP DKCAKKPFLL LAIKSLTPHF ARRQAIRESW GQESNAGNQT VVRVFLLGQT PPEDNHPDLS DMLKFESEKH QDILMWNYRD TFFNLSLKEV LFLRWVSTSC PDTEFVFKGD DDVFVNTHHI LNYLNSLSKT KAKDLFIGDV IHNAGPHRDK KLKYYIPEVV YSGLYPPYAG GGGFLYSGHL ALRLYHITDQ VHLYPIDDVY TGMCLQKLGL VPEKHKGFRT FDIEEKNKNN ICSYVDLMLV HSRKPQEMID IWSQLQSAHL KCHHHHHH.

    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.

    B3Gnt2 Human
  • 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.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered 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 :

    IFNG Human

    Description:

    IFN-Gamma Human Recombinant

    Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    Product # :

    CYT-206

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    • sds-page

    Description

    IFN-gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 17kDa.The IFN-gamma is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 4.6.

    Purity

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

    Biological Activity

    The specific activity as determined in a viral resistance assay is < 0.05 ng/ml, corresponding to a specific activity of 2.0 x 10,000,000 IU/mg.

    sds-page

    IFN-Gamma Human SDS-PAGE - Product image 1

    More Info

    • Introduction

      IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
      IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs.

    • Synonyms

      Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile distilled water or 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFQGR RASQ.

    • Background

      IFN-gamma Human

      About IFN-gamma Human:

      IFN-gamma, often known as interferon gamma (and originally known as immune interferon), is a soluble, dimerized cytokine that is the only interferon in the type II class. Besides its primary function in preventing the spread of the vesicular stomatitis virus, interferon gamma release assays are extensively employed in the diagnosis of tuberculosis. IFN-gamma, encoded by the IFNG gene in humans, controls immunological responses by cell signaling, particularly through the JAK-STAT pathway. Subsequently, interferon gamma plays a crucial role in cancer immunotherapy by preventing tumor growth, managing immune defenses against pathogens and monitoring cells activity. In this article we will delve into the science behind IFN-gamma and explain its significance in biomedical research.



      Description:

      IFN-gamma Human Recombinant is a single non-glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 17kDa that its original source is Escherichia Coli. This product appears as a sterile-filtered white lyophilized powder, ensuring purity and stability. Its formulation involves lyophilization from a filtered concentrated solution in PBS (pH 4.6). Its purity is determined both by analysis by RP-HPLC and SDS-PAGE and is therefore greater than 98%. In terms of stability, lyophilized IFN gamma is stable at room temperature for three weeks. However, it is preferable to store it desiccated below -18°C. In any case, you should prevent freeze thaw cycles. Additionally, reconstitution of IFN-gamma is recommended in sterile distilled water or 20mM AcOH, maintaining a concentration of at least 100µg/ml.

      Protein Function:

      Interferon gamma is a key player in immune control. It is a protein that plays a major role in complex cell signaling networks. The JAK-STAT pathway, which is essential for immunological regulation, is triggered by IFN-gamma through its interaction with the heterodimeric receptor. IFN-gamma's ability to regulate inflammation, apoptosis, cytokine signaling, and cell proliferation through protein mediated signaling skills is crucial for maintaining immune vigilance and response mechanisms. The incorporation of IFN-gamma into our product is validated by protein quantitation using two independent methods: UV spectroscopy and RP-HPLC.

      Applications and Usage:

      IFN-gamma Human is tailored for laboratory research, serving as a vital tool in elucidating immune mechanisms, exploring antiviral features, and unraveling tumor suppressor functions.

      Safety Information:

      IFN-gamma Human is only intended to be used in laboratory research, in line with safety protocols. It emphasizes adherence to ethical and regulatory norms and is not designed for use as household chemicals, pharmaceuticals, agricultural goods, or food additives.

      What is the molecular weight/Mw of IFNG HUMAN Protein?
      IFNG HUMAN Protein has a total Mw of 17kDa.

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

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

      What is the Biological Activity of IFNG HUMAN Protein?
      The specific activity as determined in a viral resistance assay is < 0.05 ng/ml, corresponding to a specific activity of 2.0 x 10,000,000 IU/mg.

      What is the amino acid sequence of IFNG HUMAN Protein?
      MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFQGR RASQ.

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

      What is the endotoxin level for IFNG HUMAN Protein?
      The endotoxin level is minimal, IFNG 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 0.640 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 IFN-g 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.

    Interferon Gamma Human
  • View Data Sheet

    Name :

    Thymosin β4

    Description:

    Thymosin-b4 Human Recombinant

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

    Product # :

    HOR-003

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES

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

    Thymosin B4
  • View Data Sheet

    Name :

    EIF2B1 Human

    Description:

    Eukaryotic Translation Initiation Factor 2B Subunit 1 Alpha Human Recombinant

    Translation initiation factor eIF-2B subunit alpha, eIF-2B GDP-GTP exchange factor subunit alpha, EIF2B1, EIF2BA, EIF2B.

    Product # :

    PRO-209

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    Description

    EIF2B1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (1-305 a.a.) and having a molecular mass of 35.8kDa.EIF2B1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF2B1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF2B1 is one of five subunits of eukaryotic translation initiation factor 2B (EIF2B), which is a GTP exchange factor for eukaryotic initiation factor 2 and an essential regulator for protein synthesis. Phosphorylation of eIF2 inhibits GEF activity of EIF2B, an inhibition which requires the eIF2B1 subunit. Defects in eIF2B1 are a cause of leukoencephalopathy with vanishing white matter (VWM), a brain disease which is characterized by head trauma and motor deterioration.

    • Synonyms

      Translation initiation factor eIF-2B subunit alpha, eIF-2B GDP-GTP exchange factor subunit alpha, EIF2B1, EIF2BA, EIF2B.

    • 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 MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT SAIETLCGVD SSVAVSSGGE LFLRFISLAS LEYSDYSKCK KIMIERGELF LRRISLSRNK IADLCHTFIK DGATILTHAY SRVVLRVLEA AVAAKKRFSV YVTESQPDLS GKKMAKALCH LNVPVTVVLD AAVGYIMEKA DLVIVGAEGV VENGGIINKI GTNQMAVCAK AQNKPFYVVA ESFKFVRLFP LNQQDVPDKF KYKADTLKVA QTGQDLKEEH PWVDYTAPSL ITLLFTDLGV LTPSAVSDEL IKLYL.

    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.

    Eif2B1 Human
  • View Data Sheet

    Name :

    FCER1A Human 201 a.a

    Description:

    IgE Receptor Subunit A Human Recombinant

    Fc Fragment Of IgE, High Affinity I, Receptor For; Alpha Polypeptide, FCE1A, IgE Fc Receptor Subunit Alpha, FcERI, Fc-Epsilon RI-Alpha, Fc Epsilon RI Alpha-Chain, Fc IgE Receptor, Alpha Polypeptide, High Affinity Immunoglobulin Epsilon Receptor Alpha-Subunit, High Affinity Immunoglobulin Epsilon Receptor Subunit Alpha, Immunoglobulin E Receptor, High-Affinity, Of Mast Cells, Alpha Polypeptide.

    Product # :

    PRO-2357

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    Description

    FCER1A Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 201 amino acids.FCER1Ais fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1x PBS, 50mM Arginine and 0.05% NaN3.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide (FCER1A) binds to the Fc region of immunoglobulins epsilon. FCER1A is a high affinity receptor. In addition FCER1A is responsible for starting the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators such as histamine which is responsible for the manifestations of allergy. This receptor is contains of an alpha subunit, a beta subunit, and two gamma subunits. FCER1A stands for the alpha subunit. Among the diseases associated with FCER1A are mast-cell leukemia, and allergic asthma.

    • Synonyms

      Fc Fragment Of IgE, High Affinity I, Receptor For; Alpha Polypeptide, FCE1A, IgE Fc Receptor Subunit Alpha, FcERI, Fc-Epsilon RI-Alpha, Fc Epsilon RI Alpha-Chain, Fc IgE Receptor, Alpha Polypeptide, High Affinity Immunoglobulin Epsilon Receptor Alpha-Subunit, High Affinity Immunoglobulin Epsilon Receptor Subunit Alpha, Immunoglobulin E Receptor, High-Affinity, Of Mast Cells, Alpha Polypeptide.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      The Recombinant FCER1A protein although stable at 4°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

      HMAPAMESPTL LCVALLFFAP DGVLAVPQKP KVSLNPPWNR IFKGENVTLT CNGNNFFEVS STKWFHNGSL SEETNSSLNI VNAKFEDSGE YKCQHQQVNE SEPVYLEVFS DWLLLQASAE VVMEGQPLFL RCHGWRNWDV YKVIYYKDGE ALKYWYENHN ISITNATVED SGTYYCTGKV WQLDYESEPL NITVIKAPLEHHHHHH.

    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.

    Fcer1A Human 201 Aa
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    Name :

    TRAPPC2L Human

    Description:

    Trafficking Protein Particle Complex 2-Like Human Recombinant

    Trafficking protein particle complex subunit 2-like protein, TRAPPC2L.

    Product # :

    PRO-1543

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    Description

    TRAPPC2L Human Recombinant produced in E. coli is a single polypeptide chain containing 162 amino acids (1-139) and having a molecular mass of 18.4kDa. TRAPPC2L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TRAPPC2L solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Trafficking Protein Particle Complex 2-Like (TRAPPC2L) takes part in vesicular transport from endoplasmic reticulum to Golgi. TRAPPC2L is a part of the TRAPP small subunits family and is expressed in various organs like testis, liver, bladder, lung, spleen and brain.

    • Synonyms

      Trafficking protein particle complex subunit 2-like protein, TRAPPC2L.

    • 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 MGSMAVCIAV IAKENYPLYI RSTPTENELK FHYMVHTSLD VVDEKISAMG KALVDQRELY LGLLYPTEDY KVYGYVTNSK VKFVMVVDSS NTALRDNEIR SMFRKLHNSY TDVMCNPFYN PGDRIQSRAF DNMVTSMMIQ VC.

    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.

    Trappc2L Human
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    Name :

    IFNAR1 Human

    Description:

    Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant

    IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.

    Product # :

    CYT-1138

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    • SDS-PAGE

    Description

    IFNAR1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 415 amino acids (28-436a.a.) and having a molecular mass of 47.9kDa. IFNAR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    IFNAR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    IFNAR1 Human - Product image 1

    More Info

    • Introduction

      Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.

    • Synonyms

      IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 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

      KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

    • Background

      What is the molecular weight/Mw of IFNAR1 HUMAN Protein?
      IFNAR1 HUMAN Protein has a total Mw of 47.9kDa.

      What is the source or expression system of IFNAR1 HUMAN Protein?
      Sf9, Insect cells.

      What is the Purity of IFNAR1 HUMAN Protein?
      IFNAR1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNAR1 HUMAN Protein?
      The biological functionality of IFNAR1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IFNAR1 HUMAN Protein?
      KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

      What applications can IFNAR1 HUMAN Protein be used in?
      IFNAR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNAR1 HUMAN Protein?
      The endotoxin level is minimal, IFNAR1 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.

    Ifnar1 Human
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