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Search results

1000 results found for “Glucagon”

Name

Description

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  • View Data Sheet

    Name :

    Tesamorelin

    Description:

    Tesamorelin

    Product # :

    HOR-062

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    Description

    Tesamorelin is a synthetic single, non-glycosylated polypeptide chain containing 44 amino acids, having a molecular mass of 5135.78 Dalton and a Molecular formula of C221H366N72O67S.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      trans-3-hexenoyl-Tyr-Ala-Asp-Ala-IlePhe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-GluArg-Gly-Ala-Arg-Ala-Arg-Leu-NH2.

    • Background

      Tesamorelin is a growth hormone-releasing hormone (GHRH) analogue. Tesamorelin stimulates the pituitary gland to produce endogenous growth hormone, which targets visceral adipose tissue. Tesamorelin has evolved from a HIV treatment into an effective metabolic and regenerative therapy.

    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.

    Tesamorelin
  • View Data Sheet

    Name :

    GLTPD1 Human

    Description:

    Glycolipid Transfer Protein Domain Containing 1 Human Recombinant

    Ceramide-1-Phosphate Transfer Protein, Glycolipid Transfer Protein Domain-Containing Protein 1, Glycolipid Transfer Protein Domain Containing 1, GLTP Domain-Containing Protein 1, GLTPD1, GLTPD1, Ceramide-1-phosphate transfer protein, CPTP.

    Product # :

    PRO-2093

    Price :

    Quantity :

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    Description

    GLTPD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 26.8kDa. GLTPD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLTPD1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 50% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glycolipid Transfer Protein Domain Containing 1 (GLTPD1) belongs to the GLTP family. GLTPD1 mediates the intracellular transfer of ceramide-1-phosphate between organelle membranes and the cell membrane. GLTPD1 is essential for normal structure of the Golgi stacks. In addition, GLTPD1 is able to bind phosphoceramides with a diversity of aliphatic chains, however GLTPD1 has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains. Moreover, GLTPD1 is inefficient with phosphoceramides which contains lignoceryl (C24:0). GLTPD1 participates in the regulation of the cellular levels of ceramide-1-phosphate, and in that way contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid.

    • Synonyms

      Ceramide-1-Phosphate Transfer Protein, Glycolipid Transfer Protein Domain-Containing Protein 1, Glycolipid Transfer Protein Domain Containing 1, GLTP Domain-Containing Protein 1, GLTPD1, GLTPD1, Ceramide-1-phosphate transfer protein, CPTP.

    • 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 MGSMDDSETG FNLKVVLVSF KQCLDEKEEV LLDPYIASWK GLVRFLNSLG TIFSFISKDV VSKLRIMERL RGGPQSEHYR SLQAMVAHEL SNRLVDLERR SHHPESGCRT VLRLHRALHW LQLFLEGLRT SPEDARTSAL CADSYNASLA AYHPWVVRRA VTVAFCTLPT REVFLEAMNV GPPEQAVQML GEALPFIQRV YNVSQKLYAE HSLLDLP.

    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.

    Gltpd1 Human
  • View Data Sheet

    Name :

    Prolactin Mouse, PEG

    Description:

    Prolactin Pegylated Mouse Recombinant

    Product # :

    CYT-1247

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • Citations

    Description

    Pegylated Prolactin Mouse Recombinant is a single non-glycosilated polypeptide chain having a molecular mass of ~ 39 kDa containing 199 amino acids and an additional Ala at N-terminus Prolactin Mouse was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Prolactin was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

    Purity

    Greater than 97.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Mouse Prolactin inhibits proliferation of Nb2 cells or Baf/3 cells stably transfected with human prolactin receptors, though its activity is lower than pegylated human prolactin. However, it is anticipated that its activity in vivo in mice will be higher due to prolonged persistence in circulation.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Prolactin Mouse although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 4 mg/ml and filter sterilization Prolactin mouse can be stored at 4°C for several weeks. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Prolactin Mouse in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Prolactin aka as lactotropin and mammotropin, is a neuroendocrine hormone synthesized primarily by the pituitary gland in response to eating but also a variety of other cell types including the placenta, brain and uterus. Prolactin takes part in metabolism, regulation of the immune system and pancreatic development. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.675 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by DNAman computer analysis program of protein sequences.

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

    Prolactin Mouse Peg
  • View Data Sheet

    Name :

    Thrombin

    Description:

    Human Thrombin

    Product # :

    PRO-339

    Price :

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    • description
    • source
    • formulation
    • biological activity
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    Description

    Thrombin was purified from human plasma.

    Source

    Human Plasma.

    Formulation

    Lyophilized protein containing mannitol, sodium chloride, calcium chloride.

    Biological Activity

    The specific activity was found to be 116 US Units/mg protein.

    Citations

    More Info

    • Introduction

      Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.

    • Physical Appearance

      lyophilized powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized human thrombin in sterile a 0.9% NaCl solution at 500U/ml.

    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.

    Thrombin Human
  • View Data Sheet

    Name :

    GLSA1 E.Coli

    Description:

    Glutaminase 1 E.Coli Recombinant

    Glutaminase 1, ybaS.

    Product # :

    ENZ-133

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • formulation
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    Description

    GLSA1 E.Coli Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310a.a.) and having a molecular mass of 35.0kDa. The GLSA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GLSA1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GlsA1 is a member of the great superfamily of serine-dependent beta-lactamases and penicillin-binding proteins which exist almost in every bacteria and eukaryotes and catalyze the hydrolytic deamidation of l-glutamine to l-glutamate and free NH4+.

    • Synonyms

      Glutaminase 1, ybaS.

    • 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 MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA KQLGYNVFKG

    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.

    Glsa1 Ecoli
  • View Data Sheet

    Name :

    NANOG Human, His

    Description:

    Nanog Human Recombinant, His Tag

    NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.

    Product # :

    PRO-881

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    Description

    NANOG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154) and having a molecular mass of 19.6 kDa.The NANOG is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NANOG protein (0.25mg/ml) is supplied in 20mM Tris-HCL, pH-8, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      NANOG is a multidomain homeobox transcription factor which functions to maintain the undifferentiated state of pluripotent stem cells. NANOG expression counteracts the differentiation-promoting signals induced by the extrinsic factors LIF, Stat3 and BMP. Once NANOG expression is downregulated, cell differentiation can proceed. Proteins which regulate NANOG expression include transcription factors Oct4, SOX2, FoxD3, and Tcf3 and tumor suppressor p53.

    • Synonyms

      NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.

    • 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 MSVDPACPQS LPCFEASDCK ESSPMPVICG PEENYPSLQM SSAEMPHTET VSPLPSSMDL LIQDSPDSST SPKGKQPTSA EKSVAKKEDK VPVKKQKTRT VFSSTQLCVL NDRFQRQKYL SLQQMQELSN ILNLSYKQVK TWFQNQRMKS KRWQ

    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.

    Nanog Human His
  • View Data Sheet

    Name :

    ASNS Mouse

    Description:

    Asparagine Synthetase Mouse Recombinant

    Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase. 

    Product # :

    ENZ-1100

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    Description

    ASNS produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 567 amino acids (1-561a.a.) and having a molecular mass of 65.1 kDa.ASNS is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ASNS protein solution ( 0.25mg/ml ) contains PBS (pH 7.4) and 40% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.

    • Synonyms

      Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.

    • 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

      MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPDMRIPK NGIEKHLLRE TFEDCNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDEMMSA SQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK WINATDPSAR TLTHYKS AAK AHHHHHH.

    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.

    Asns Mouse
  • View Data Sheet

    Name :

    PGK1 Human, Active

    Description:

    Phosphoglycerate Kinase 1 Human Recombinant, BioActive

    Phosphoglycerate kinase 1, MGC117307, MGC142128, MGC8947, MIG10, PGKA.

    Product # :

    PKA-124

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    Description

    PGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-417a.a.) and having a molecular mass of 46.8kDa.PGK1 is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PGK1 solution (1mg/ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.0) and 1mM DTT.

    .

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 600unit/mg. One unit will convert 1 umole of 1,3-Bisphosphoglycerate to 3-PGA per minute at pH 8.0 at 37C.

    Citations

    More Info

    • Introduction

      Phosphoglycerate kinase 1, also referred to PGK1, is an X-linked enzyme whichfunctions in the glycolytic pathway.The gene encoding the erythrocyte enzyme PGK1 & it seems that PGK-1 plays a role as a polymerase alpha cofactor protein (primer recognition protein) as a glyxolytic enzyme role. The PGK1 catalyzes the reversible conversion of 1, 3-diphosphoglycerate to 3-phosphoglycerate during glycolysis, generating one molecule of ATP.

    • Synonyms

      Phosphoglycerate kinase 1, MGC117307, MGC142128, MGC8947, MIG10, PGKA.

    • 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 MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI

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    Pgk1 Enzyme
  • View Data Sheet

    Name :

    TIPIN Human

    Description:

    TIMELESS Interacting Protein Human Recombinant

    TIMELESS Interacting Protein, CSM3 Homolog.

    Product # :

    PRO-1710

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    Description

    TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.

    • Synonyms

      TIMELESS Interacting Protein, CSM3 Homolog.

    • 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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR

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    Tipin Human
  • View Data Sheet

    Name :

    Procalcitonin Rhesus

    Description:

    Procalcitonin Rhesus Recombinant

    Calcitonin.

    Product # :

    HOR-016

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    Description

    Procalcitonin Rhesus Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala26-Asn140) containing 125 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 14kDa.

    Source

    Escherichia Coli.

    Formulation

    Procalcitonin was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Calcitonin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHASAPFRSALESS PDPATLSEEE ARLLLAALVQ DYVQMKASEL EQEQETEGSS LDSPRSKRCG NLSTCMLGTY TQDFNKFHTF PQTAIGVGAP GKKRDMSSDL ERNRRRYVSM PQDAN.

    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.

    Procalcitonin Rhesus
  • View Data Sheet

    Name :

    CIDEC Human

    Description:

    Cell Death-Inducing DFFA-Like Effector C Human Recombinant

    Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    Product # :

    PRO-2026

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    Description

    CIDEC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu2-Gln238) containing 247 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 28kDa.

    Source

    Escherichia Coli.

    Formulation

    CIDEC filtered (0.4µm) solution at a concentration of 0.4mg/ml in 30mM acetate buffer and 10mM dithiothreitol, pH 4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cell Death-Inducing DFFA-Like Effector C (CIDEC) belongs to the cell death-inducing DNA fragmentation factor-like effector family, whose members have significant roles in apoptosis. CIDEC is expressed mainly in adipocytes, intestine, heart, stomach, and weakly in the brain, kidney and liver. CIDEC overexpression in preadipocytes induces apoptosis. CIDEC regulates enlargement of lipid droplets.

    • Synonyms

      Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    • Physical Appearance

      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

      MKHHHHHHASEYAMKSLSLL YPKSLSRHVS VRTSVVTQQL LSEPSPKAPR ARPCRVSTAD RSVRKGIMAY SLEDLLLKVR DTLMLADKPF FLVLEEDGTT VETEEYFQAL AGDTVFMVLQ KGQKWQPPSE QGTRHPLSLS HKPAKKIDVA RVTFDLYKLN PQDFIGCLNV KATFYDTYSL SYDLHCCGAK RIMKEAFRWA LFSMQATGHV LLGTSCYLQQ LLDATEEGQP PKGKASSLIP TCLKILQ.

    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.

    Cidec Human
  • View Data Sheet

    Name :

    LTF Human S.Plasma

    Description:

    Lactoferrin Human (Seminal Plasma)

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

    Product # :

    PRO-1591

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    Description

    The Human Lactoferrin produced from pooled Human seminal plasma has a molecular mass of 76.165kDa (calculated without glycosylation) containing 691 amino acid residues.

    Source

    Human seminal plasma.

    Formulation

    LTF protein filtered (0.4µm) and lyophilized in 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Purity greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      GRRRSVQWCA VSQPEATKCF QWQRNMRKVR GPPVSCIKRD SPIQCIQAIA ENRADAVTLD GGFIYEAGLA PYKLRPVAAE VYGTERQPRT HYYAVAVVKK GGSFQLNELQ GLKSCHTGLR RTAGWNVPIG TLRPFLNWTG PPEPIEAAVA RFFSASCVPG ADKGQFPNLC RLCAGTGENK CAFSSQEPYF SYSGAFKCLR DGAGDVAFIR ESTVFEDLSD EAERDEYELL CPDNTRKPVD KFKDCHLARV PSHAVVARSV NGKEDAIWNL LRQAQEKFGK DKSPKFQLFG SPSGQKDLLF KDSAIGFSRV PPRIDSGLYL GSGYFTAIQN LRKSEEEVAA RRARVVWCAV GEQELRKCNQ WSGLSEGSVT CSSASTTEDC IALVLKGEAD AMSLDGGYVY TAGKCGLVPV LAENYKSQQS SDPDPNCVDR PVEGYLAVAV VRRSDTSLTW NSVKGKKSCH TAVDRTAGWN IPMGLLFNQT GSCKFDEYFS QSCAPGSDPR SNLCALCIGD EQGENKCVPN SNERYYGYTG AFRCLAENAG DVAFVKDVTV LQNTDGNNNE AWAKDLKLAD FALLCLDGKR KPVTEARSCH LAMAPNHAVV SRMDKVERLK QVLLHQQAKF GRNGSDCPDK FCLFQSETKN LLFNDNTECL ARLHGKTTYE KYLGPQYVAG ITNLKKCSTS PLLEACEFLR K.

    • Human Virus Test

      Samples from each donor have been tested and found negative for HBsAg, HIV-1+2, HCV, syphilis, aHBc, RRR.

    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.

    Ltf Human Seminal Plasma
  • View Data Sheet

    Name :

    IGF1 Human, A70T

    Description:

    Insulin Like Growth Factor-1, Mutant A70T Human Recombinant

    Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    Product # :

    CYT-1091

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    Description

    IGF1 A70T Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7kDa. The IGF1 A70T is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IGF1 A70T Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM PB and 150 mM NaCl, pH 6.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

    • Synonyms

      Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      It is recommended to reconstitute the lyophilized IGF1 A70T in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKST.

    • Background

      What is the molecular weight/Mw of IGF1 HUMAN, A70T Protein?
      IGF1 HUMAN, A70T Protein has a total Mw of 7.7kDa.

      What is the source or expression system of IGF1 HUMAN, A70T Protein?
      Escherichia Coli.

      What is the Purity of IGF1 HUMAN, A70T Protein?
      IGF1 HUMAN, A70T Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGF1 HUMAN, A70T Protein?
      The biological functionality of IGF1 HUMAN, A70T Protein will be determined in the future.

      What is the amino acid sequence of IGF1 HUMAN, A70T Protein?
      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKST.

      What applications can IGF1 HUMAN, A70T Protein be used in?
      IGF1 HUMAN, A70T Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGF1 HUMAN, A70T Protein?
      The endotoxin level is minimal, IGF1 HUMAN, A70T 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.

    Igf1 A70T
  • View Data Sheet

    Name :

    CRYM Human

    Description:

    Crystallin, Mu Human Recombinant

    Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    Product # :

    PRO-2291

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    Description

    CRYM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 334 amino acids (1-314) and having a molecular mass of 35.9kDa. CRYM is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CYRM 1mg/ml solution containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Crystallin, Mu (CRYM) is a taxon-specific crystallin protein which binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. CRYM doesn’t perform a structural role in lens tissue; instead CRYM binds thyroid hormone for possible regulatory or developmental roles. CRYM gene mutations are linked with autosomal dominant non-syndromic deafness. CRYM specifically catalyzes the reduction of imine bonds in brain substrates which may include cystathionine ketamine and lanthionine ketamine.

    • Synonyms

      Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CRYM 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

      MGSSHHHHHH SSGLVPRGSH MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT VAAKLIYDSW SSGK

    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.

    Crym Human
  • View Data Sheet

    Name :

    S100A6 Human

    Description:

    S100 Calcium Binding Protein A6 Human Recombinant

    Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.

    Product # :

    PRO-148

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    Description

    S100A6 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 110 amino acids (1-90 a.a.) and having a molecular mass of 12.3kDa. The S100A6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A6 function in stimulation of prolactin secretion and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

    • Synonyms

      Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.

    • 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 MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL DRNKDQEVNF QEYVTFLGAL ALIYNEALKG.

    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.

    S100A6 Human
  • View Data Sheet

    Name :

    ACTN1 Human

    Description:

    Actinin Alpha 1 Human Recombinant

    ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.

    Product # :

    PRO-2227

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    Description

    ACTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31.4kDa. ACTN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACTN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

    • Synonyms

      ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-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 MGSEFMDHYD SQQTNDYMQP EEDWDRDLLL DPAWEKQQRK TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY LDIPKMLDAE DIVGTARPDE KAIMTYVSSF YHAF.

    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.

    Actn1 Human
  • View Data Sheet

    Name :

    SH3BGRL3 Human

    Description:

    SH3 Domain Binding Glutamic Acid-Rich Protein Like 3 Human Recombinant

    SH3 Domain Binding Glutamic Acid-Rich Protein Like 3, SH3BGRL3-Like Protein, SH3 Domain-Binding Protein 1, SH3BP-1, TNF Inhibitory Protein, TIP-B1.

    Product # :

    PRO-1216

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    Description

    SH3BGRL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 116 amino acids (1-93) and having a molecular mass of 12.8 kDa.SH3BGRL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SH3BGRL3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SH3 domain-binding glutamic acid-rich-like protein 3 (SH3BGRL3) which is located on chromosome 1p34.3-35, encodes for a small 93 amino acids protein. SH3BGRL3 is the newest member of thioredoxin super family, whose posttranslational altered form was recognized as TNF-alpha inhibitory protein. SH3BGRL3 may act as a regulator in all-trans retinoic acid-induced pathway and also as a modulator of glutaredoxin biological activity.

    • Synonyms

      SH3 Domain Binding Glutamic Acid-Rich Protein Like 3, SH3BGRL3-Like Protein, SH3 Domain-Binding Protein 1, SH3BP-1, TNF Inhibitory Protein, TIP-B1.

    • 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 MGSMSGLRVY STSVTGSREI KSQQSEVTRI LDGKRIQYQL VDISQDNALR DEMRALAGNP KATPPQIVNG DQYCGDYELF VEAVEQNTLQ EFLKLA

    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.

    Sh3Bgrl3 Human
  • View Data Sheet

    Name :

    DR1 Human

    Description:

    Down-Regulator of Transcription 1 Human Recombinant

    NC2, NC2-BETA, Negative cofactor 2-beta.

    Product # :

    PRO-542

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    Description

    DR1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (1-176 a.a.) and having a molecular mass of 21.6 kDa. The DR1 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DR1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF, 0.1M NaCl & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DR1 is a phosphoprotein that inhibits both basal and activated levels of transcription. DR1 is phosphorylated in vivo which affects its interaction with TBP. DR1 has a histone fold motif at the amino terminus, a TBP-binding domain, and a glutamine- and alanine-rich region. By selectively repressing polymerases II and III, DR1 alters the physiological balance of transcriptional output in favor of polymerase I.

    • Synonyms

      NC2, NC2-BETA, Negative cofactor 2-beta.

    • 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 MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI SSEANEICNK SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK RRKASSRLEN LGIPEEELLR QQQELFAKAR QQQAELAQQE WLQMQQAAQQ AQLAAASASA NQAGSSQDE EDDDDI.

    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.

    Dr1 Human
  • View Data Sheet

    Name :

    Batroxobin

    Description:

    Batroxobin

    Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.

    Product # :

    PRO-2146

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    Description

    Batroxobin, isolated from Bothrops atrox snake venom, has an Mw of approximately 43kDa.

    Formulation

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

    Citations

    More Info

    • Introduction

      Batroxobin is a serin protease that reduces fibronogen levels and is originally extracted from snake venom of Bothrops Atrox. Batroxobin is used in defibrinogenation and thrombolysis and also has an effect on c-fos gene and growth factor.
      Batroxobin can efficiently restrain proliferation of VSMCs, by blocking the release and uptake of Ca2+, thus influencing [Ca2+]i.
      Batroxobin converts fibrinogen to fibrin through the restricted release of fibrinopeptide-A from fibrinogen to promote blood to clot. Unlike thrombin, it is not affected by heparin and hirudin.

    • Synonyms

      Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Store the lyophilized Batroxobin between 2-8°C. Do not freeze!

    • Solubility

      It is recommended to reconstitute the lyophilized Batroxobin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.

    • Unit Definition

      100BU [Batroxobin Units]=1mg.

    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.

    Batroxobin Native
  • View Data Sheet

    Name :

    TAGLN2 Human

    Description:

    Transgelin-2 Human Recombinant

    Transgelin-2, SM22-alpha homolog, TAGLN2, KIAA0120, HA1756.

    Product # :

    PRO-124

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    Description

    TAGLN2 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 208 amino acids (13-199 a.a.) and having a molecular mass of 23.4kDa. The TAGLN2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TAGLN2 solution (1 mg/ml), 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Transgelin 2 (TAGLN2) is one of the earliest markers of differentiated smooth muscle. TAGLN2 contains a calponin like repeat and a calponin-homology (CH) domain. TAGLN2 is downregulated in some transformed cell lines, indicating that a reduction of transgelin expression may be an early indicator of the onset of transformation. TAGLN2 also binds actin, causing actin fibers to gel within minutes of binding. The binding of transgelin to actin occurs at a ratio of 1:6 actin monomers.

    • Synonyms

      Transgelin-2, SM22-alpha homolog, TAGLN2, KIAA0120, HA1756.

    • 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 MEVQQKIEKQ YDADLEQILI QWITTQCRKD VGRPQPGREN FQNWLKDGTV LCELINALYP EGQAPVKKIQ ASTMAFKQME QISQFLQAAE RYGINTTDIF QTVDLWEGKN MACVQRTLMN LGGLAVARDD GLFSGDPNWF PKKSKENPRN FSDNQLQEGK NVIGLQMGTN RGASQAGMTG YGMPRQIL.

    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.

    Tagln2 Human
  • View Data Sheet

    Name :

    TAGLN3 Human

    Description:

    Transgelin-3 Human Recombinant

    Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.

    Product # :

    PRO-946

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    Description

    TAGLN3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.6 kDa.The TAGLN3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TAGLN3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.

    • Synonyms

      Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.

    • 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 MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS NKGASQAGMT GYGMPRQIM

    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.

    Tagln3 Human
  • View Data Sheet

    Name :

    CAPSL Human

    Description:

    Calcyphosine-Like Human Recombinant

    Calcyphosine-like protein, CAPSL, MGC26610.

    Product # :

    PRO-185

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    Description

    CAPSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-208) and having a molecular mass of 26.3 kDa.The CAPSL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CAPSL protein at 1mg/ml in 20mM Tris-HCL, pH-8, 0.2M NaCl, 5mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CAPSL is a calcium-binding protein holding two conserved calcium-binding motifs (EF-hands) which are found in a superfamily of calcium sensors and calcium signal modulators. In addition, the CAPSL gene is in the same linkage disequilibrium (LD) block as the IL7R gene and there is well known association between the CAPSL-IL7R locus and type 1 diabetes.

    • Synonyms

      Calcyphosine-like protein, CAPSL, MGC26610.

    • Physical Appearance

      CAPSL is supplied as a 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 MAGTARHDRE MAIQAKKKLT TATDPIERLR LQCLARGSAG IKGLGRVFRI MDDDNNRTLD FKEFMKGLND YAVVMEKEEV EELFQRFDKD GNGTIDFNEF LLTLRPPMSR ARKEVIMQAF RKLDKTGDGV ITIEDLREVY NAKHHPKYQN GEWSEEQVFR KFLDNFDSPY DKDGLVTPEE FMNYYAGVSA SIDTDVYFII MMRTAWKL

    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.

    Capsl Human
  • View Data Sheet

    Name :

    CARD17 Human

    Description:

    Caspase Recruitment Domain Family, Member 17 Human Recombinant

    CARD17, Caspase Recruitment Domain Family, Member 17, Caspase recruitment domain-containing protein 17, INCA, Caspase-1 inhibitor INCA, Inhibitory caspase recruitment domain protein.

    Product # :

    PRO-1688

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    Description

    CARD17 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 14.3 kDa.CARD17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CARD17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Caspase Recruitment Domain Family, Member 17 (CARD17) is a regulator of procaspase-1/CASP1 activation involved in the regulation of the proteolytic maturation of pro-IL-1beta/IL1B and its release throughout inflammation. CARD17 inhibits the release of IL1B in reaction to LPS in monocytes. Though, unlike CASP1, CARD17 do not induce NF-kappa-B activation.

    • Synonyms

      CARD17, Caspase Recruitment Domain Family, Member 17, Caspase recruitment domain-containing protein 17, INCA, Caspase-1 inhibitor INCA, Inhibitory caspase recruitment domain protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMADKVLK EKRKQFIRSV GEGTINGLLG ELLETRVLSQ EEIEIVKCEN ATVMDKARAL LDSVIRKGAP ACQICITYIC EEDSHLAGTL GLSAGPTSGN HLTTQDSQIV LPS.

    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.

    Card17 Human
  • View Data Sheet

    Name :

    Placental Lactogen Bovine

    Description:

    Placental Lactogen Bovine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    Product # :

    CYT-511

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    Description

    Placental Lactogen Bovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

    Purity

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

    Biological Activity

    Placental Lactogen Bovine is biologically active as evidenced by inducing proliferation of Nb2 cells.

    Citations

    More Info

    • Introduction

      Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
      Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Placental Lactogen Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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 Placental Lactogen 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 six N-terminal amino acids was determined and was found to be Ala-Glu-Asp-Tyr-Ala-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.86 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8. This value is calculated by the DNAman computer analysis program of protein sequences.

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

    Placental Lactogen Bovine
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