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Search results

1000 results found for “Glucagon”

Name

Description

Product #

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Quantity

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  • 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

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    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.

    Citations

    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 :

    SRGN Human

    Description:

    Serglycin Human Recombinant

    Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.

    Product # :

    PRO-965

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
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    Description

    SRGN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (28-158) and having a molecular mass of 17.4 kDa (Molecular weight on SDS-PAGE will appear higher).SRGN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.

    • Synonyms

      Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.

    • 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 MGSHMYPTRR ARYQWVRCNP DSNSANCLEE KGPMFELLPG ESNKIPRLRT DLFPKTRIQD LNRIFPLSED YSGSGFGSGS GSGSGSGSGF LTEMEQDYQL VDESDAFHDN LRSLDRNLPS DSQDLGQHGL EEDFML.

    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.

    Srgn Human
  • View Data Sheet

    Name :

    Placental Lactogen Ovine

    Description:

    Placental Lactogen Ovine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    Product # :

    CYT-512

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Placental Lactogen Ovine 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 97.0% as determined by:
    (a) Analysis gel filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Placental Lactogen Ovine 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 Ovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Placental Lactogen Ovine 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 five N-terminal amino acids was determined and was found to be Ala-Gln-His-Pro-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.85 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Placental Lactogen Ovine
  • View Data Sheet

    Name :

    Leptin qA Human

    Description:

    Leptin Antagonist Quadruple Mutant Human Recombinant

    Product # :

    CYT-353

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.Leptin Antagonist Quadruple Mutant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin Quadruple Antagonist Mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Quadruple Mutant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.89 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Qa Human
  • View Data Sheet

    Name :

    CREG1 Human

    Description:

    Cellular Repressor of E1A-Stimulated Genes 1 Human Recombinant

    Cellular repressor of E1A-stimulated genes 1, protein CREG1, CREG.

    Product # :

    PRO-1196

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    CREG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 213 amino acids (32-220) and having a molecular mass of 23.6 kDa.CREG1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CREG1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cellular Repressor of E1A-Stimulated Genes 1 (CREG1) both activates and inhibits gene expression to stimulate cellular proliferation and hinder differentiation. CREG1 antagonizes transcriptional activation and cellular transformation by E1A. CREG1 shares partial sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. CREG1 contributes to the transcriptional control of cell growth and differentiation.

    • Synonyms

      Cellular repressor of E1A-stimulated genes 1, protein CREG1, CREG.

    • 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 MGSMRGGRDH GDWDEASRLP PLPPREDAAR VARFVTHVSD WGALATISTL EAVRGRPFAD VLSLSDGPPG AGSGVPYFYL SPLQLSVSNL QENPYATLTM TLAQTNFCKK HGFDPQSPLC VHIMLSGTVT KVNETEMDIA KHSLFIRHPE MKTWPSSHNW FFAKLNITNI WVLDYFGGPK IVTPEEYYNV TVQ

    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.

    Creg1 Human
  • View Data Sheet

    Name :

    Hexarelin

    Description:

    Hexarelin

    Product # :

    HOR-288

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    Description

    Hexarelin has 7 amino acids H-His-D-2-Methyl-Trp-Ala-Trp-D-Phe-Lys-NH2 and having a molecular weight of 887 Dalton. The Molecular Formula is C47H58N12O6.

    Formulation

    The Hexarelin peptide was lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Introduction

      Hexarelin stimulates GH secretion. Hexarelin is more resistant to proteolytic degradation than GHRP-6.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) powder.

    • Stability

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

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

    Hexarelin
  • View Data Sheet

    Name :

    SHBG Protein

    Description:

    Sex Hormone-Binding Globulin Human

    Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.

    Product # :

    PRO-2757

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    Description

    SHBG is a protein of approximately 45kD.

    Source

    Human serum.

    Formulation

    The protein is supplied in 0.01M HEPES, PH 7.4 and 0.15M NaCl.

    Citations

    More Info

    • Introduction

      Sex-hormone-binding globulin (SHBG) is a beta-globulin which specifically binds steroid hormones; it is involved in the transport of sex steroids in plasma. The main site of SHBG synthesis is assumed to be the hepatocytes. The production of SHBG is regulated by androgen/estrogen balance, thyroid hormones, insulin and dietary factors, among others. The concentration of SHBG is a key factor regulating their distribution between protein-bound and free states. SHBG concentration determination is primarily significant in the evaluation of mild disorders of androgen metabolism and it allows detection of women with hirsutism who are likely to react to estrogen therapy. Testosterone/SHBG-ratios correlate well with both measured and calculated values for free testosterone thus aid to distinguish between subjects with excessive androgen activity and normal individuals. SHBG gene polymorphisms are linked with polycystic ovary syndrome and type 2 diabetes mellitus.

    • Synonyms

      Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.

    • Physical Appearance

      Streile filtered colorless solution.

    • Stability

      Upon arrival, Store at -20°C. Please prevent freeze-thaw cycles.

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, Parvovirus B19, HBc, HBV, HIV and Syphilis.

    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.

    Shbg Protein
  • View Data Sheet

    Name :

    Thymopentin

    Description:

    Thymopentin

    Product # :

    HOR-241

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    Description

    Thymopentin has a molecular formula of C30H49N9O9, Arg-Lys-Asp-Val-Tyr-OH having an Mw of 679.8 Dalton.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

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

    Biological Activity

    What is the molecular weight/Mw of THYMOPENTIN Protein? THYMOPENTIN Protein has a total Mw of 0.67kDa. What is the Purity of THYMOPENTIN Protein? THYMOPENTIN Protein is >99% pure as determined by SDS-PAGE. What is the Biological Activity of THYMOPENTIN Protein? The biological functionality of THYMOPENTIN Protein will be determined in the future. What applications can THYMOPENTIN Protein be used in? THYMOPENTIN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for THYMOPENTIN Protein? The endotoxin level is minimal, THYMOPENTIN Protein was purified using conventional chromatography techniques.

    Citations

    More Info

    • Introduction

      Thymopentin, also known as TP-5, is a synthetic pentapeptide which is the active site of the naturally occurring hormone thymopoietin with immunomodulating properties (corresponding to the amino acids 32-36 of thymopoietin). Thymopentin enhances the production of thymic T cells and may help restore immunocompetence in immunosuppressed subjects. This agent also augments the effects of ionizing radiation by arresting cancer cells in the G2/M phase of the cell cycle.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymopentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TP-5 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

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

    Thymopentin
  • View Data Sheet

    Name :

    Protein-A/G, His

    Description:

    Protein A/G Recombinant, His Tag

    Product # :

    PRO-1927

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 3 of protein G (C1-C2-C3) containing 513 amino acids in total and having a molecular mass of 56.9kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 8 IgG-binding domains EDABC-C1C2C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1, C2 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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 Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE KLAAALEHHH HHH.

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

    Protein A G His
  • View Data Sheet

    Name :

    Thymosin beta 4 Human

    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.

    Citations

    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

    • Background

      What is the molecular weight/Mw of THYMOSIN BETA 4 HUMAN Protein?
      THYMOSIN BETA 4 HUMAN Protein has a total Mw of 4.9kDa.

      What is the source or expression system of THYMOSIN BETA 4 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of THYMOSIN BETA 4 HUMAN Protein?
      THYMOSIN BETA 4 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of THYMOSIN BETA 4 HUMAN Protein?
      The biological functionality of THYMOSIN BETA 4 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of THYMOSIN BETA 4 HUMAN Protein?
      SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES

      What applications can THYMOSIN BETA 4 HUMAN Protein be used in?
      THYMOSIN BETA 4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for THYMOSIN BETA 4 HUMAN Protein?
      The endotoxin level is minimal, THYMOSIN BETA 4 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant THYMOSIN BETA 4 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of THYMOSIN BETA 4 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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 :

    UCHL1 (1-126) Human

    Description:

    Ubiquitin Carboxyl-Terminal Hydrolase L1 (1-126) Human Recombinant

    PGP 9.5, UCHL1, PGP9.5, PARK5.

    Product # :

    PRO-2823

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    Description

    The UCHL1 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCHL1 His-Tagged Fusion Protein, produced in E. coli, is a 19kDa protein containing 126 amino acid residues of the UCHL1 Human, 1-126 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      PGP 9.5, UCHL1, PGP9.5, PARK5.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized UCHL1 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 0.5mg/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.

    • Background

      Human Ubiquitin Carboxyl-Terminal Hydrolase L1 (UCH-L1) is an important enzyme involved in the ubiquitin-proteasome system, which regulates protein degradation and turnover in cells.

      UCHL1 Function:

      UCHL1 mainly removes ubiquitin molecules from proteins, thereby recycling ubiquitin and regulating protein stability. This action is important for controlling various cellular processes and maintaining cellular homeostasis and.

      UCHL1 Structure

      UCHL1 is characterized by a catalytic domain which facilitates its hydrolase activity, allowing it to cleave ubiquitin from substrates.

      UCHL1 Role in Neurodegeneration

      UCHL1 has been implicated in neurodegenerative diseases, such as Parkinson’s and Alzheimer's disease. Its expression levels and activity can affect neuronal survival and function.

      UCH-L1 is also studied in the context of cancer. Altered levels of UCHL1 may affect on tumour progression and response to therapy.

      UCHL1 Biomarker Potential

      UCHL1 is being investigated as a potential biomarker for diseases, especially neurodegenerative disorders due to its involvement in various pathologies.

      UCHL1 Research

      Ongoing studies focus on understanding its role in various cellular contexts, its regulation, and its potential as a therapeutic target.

      In conclusion, UCHL1 is a very important component of cellular regulation, with implications in health and disease.

    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.

    Uchl1 Protein
  • View Data Sheet

    Name :

    CJC-1295

    Description:

    CJC-1295

    Product # :

    HOR-066

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    Description

    CJC-1295 is a synthetic single, non-glycosylated polypeptide chain containing 29 amino acids, having a molecular mass of 3367.89 Dalton and a Molecular formula of C152H252N44O42.

    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 CJC-1295 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CJC-1295 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 CJC-1295 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Tyr-D-Ala-Asp-Ala-IlePhe-Thr-Gln-Ser-Tyr-Arg-Lys-Val-Leu-Ala-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Leu-Ser-Arg-NH2.

    • Background

      CJC-1295 is a synthetic growth hormone-releasing hormone (GHRH) analog which regulates the GH–IGF-1 axis, aging biology, metabolism and peptide pharmacology. CJC-1295 identifies serum protein biomarkers downstream of GH/IGF-1 activation. CJC-1295 plays a role as a bridge compound between modified peptide therapeutics, native hypothalamic peptides and long-acting biologic hormone regulators.

    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.

    CJC-1295
  • View Data Sheet

    Name :

    GLU-C S.aureus

    Description:

    Glutamyl endopeptidase Staphylococcal Recombinant

    Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.

    Product # :

    ENZ-955

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    Description

    Recombinant Staphylococcal GLU-C produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 267 amino acids and having a molecular mass of 28.9kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glutamyl endopeptidase (GLU-C) is an enzyme which cleaves peptide bonds on the carboxyl-terminal side of glutamic acid and, less frequently, aspartic acid (for example: Glu-|-Xaa, Asp-|-Xaa). GLU-C is a pathogenic factor involved in the adherence and colonization of human tissue. GLU-C preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. GLU-C is required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. GLU-C is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. Furthermore, GLU-C protects bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. GLU-C may also be involved in the stability of secreted lipases.

    • Synonyms

      Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

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

    • Amino Acid Sequence

      MLPNNDRHQI TDTTNGHYAP VTYIQVEAPT GTFIASGVVV GKDTLLTNKH VVDATHGDPH ALKAFPSAIN QDNYPNGGFT AEQITKYSGE GDLAIVKFSP NEQNKHIGEV VKPATMSNNA ETQVNQNITV TGYPGDKPVA TMWESKGKIT YLKGEAMQYD LSTTGGNSGS PVFNEKNEVI GIHWGGVPNE FNGAVFINEN VRNFLKQNIE DIHFANDDQP NNPDNPDNPN NPDNPNNPDE PNNPDNPNNP DNPDNGDNNN SDNPDAA.

    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.

    Glu C Saureus
  • View Data Sheet

    Name :

    Gliadin Gamma 18.6kDa Wheat

    Description:

    Gliadin Gamma 18.6kD Wheat Recombinant

    Product # :

    PRO-114

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    Description

    Gliadin is a cDNA coding for an epitope-carrying fragment of a wheat gamma-gliadin isoform, having a molecular mass of 19 kDa (high proline content and the low pI are likely causes for the observed discrepancy between calculated molecular weight and the observed electrophoretic mobility of approx. 50 kDa on standard SDS-PAGE), pH 4.6. By sequence design the epitopes correspond to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation. Gliadin protein is fused to a hexa-histidine purification tag.

    Source

    Escherichia Coli.

    Formulation

    Gliadin is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl, and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

    • 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.

    • Immunological Functions

      1. Binds IgG- and IgA-type human autoantibodies associated with celiac disease. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot.

    • coating concentration

      0.15-0.5 µg/ml (depending on the type of ELISA plate and coating buffer).

    • Applications

      Western blot with monoclonal anti-hexa-His-tag antibody.

    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.

    Gliadin Wheat
  • View Data Sheet

    Name :

    STMN2 Human

    Description:

    Stathmin Like-2 Human Recombinant

    SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.

    Product # :

    PRO-752

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    Description

    Recombinant Human Stathmin Like-2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (39-179 a.a) and having a molecular mass of 16.4 kDa. STMN2 is purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The STMN2 protein solution contains 50mM MES, pH-6.0, 0.1mM PMSF, 1 mM EDTA and 10% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      STMN2 is a neuronal growth-associated protein which shares a majority of its amino acid sequence with the phosphoprotein stathmin. STMN2 is involved in neuronal differentiation and in modulating membrane interaction with the cytoskeleton through neurite outgrowth. STMN2 is necessary for maintaining the anchorage-independent growth state of beta-catenin/TCF-activated hepatoma cells. SCG10 is a novel indicator of osteogenesis and osteoblast that takes part in the regulation of the adipocyte/osteoblast balance. STMN2 plays a role as an effector downstream of Rnd1 to regulate axon extensions by modulating microtubule organization.

    • Synonyms

      SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MDMEVKQINK RASGQAFELI LKPPSPISEA PRTLASPKKK DLSLEEIQKK LEAAEERRKS QEAQVLKQLA EKREHEREVL QKALEENNNF SKMAEEKLIL KMEQIKENRE ANLAAIIERL QEKERHAAEV RRNKELQVEL SG.

    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.

    Stmn2 Human
  • View Data Sheet

    Name :

    LGALS7 Human

    Description:

    Galectin-7 Human Recombinant

    Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.

    Product # :

    CYT-016

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    Description

    Galectin-7 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 136 amino acids and having a molecular mass of 15kDa.The LGALS7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LGALS7 was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris, 150mM NaCl, 1mM EDTA and 5% Trehalose, pH 8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.

    • Synonyms

      Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LGALS7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-7 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 Galectin-7 in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNP
      RLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQ
      YHHFRHRLPLARVRLVEVGGDVQLDSVRIF

    • Background

      What is the molecular weight/Mw of LGALS7 HUMAN Protein?
      LGALS7 HUMAN Protein has a total Mw of 15kDa.

      What is the source or expression system of LGALS7 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS7 HUMAN Protein?
      LGALS7 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS7 HUMAN Protein?
      The biological functionality of LGALS7 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of LGALS7 HUMAN Protein?
      MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNP
      RLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQ
      YHHFRHRLPLARVRLVEVGGDVQLDSVRIF

      What applications can LGALS7 HUMAN Protein be used in?
      LGALS7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS7 HUMAN Protein?
      The endotoxin level is minimal, LGALS7 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.

    Lgals7 Human
  • View Data Sheet

    Name :

    GPBB Human

    Description:

    Glycogen Phosphorylase Human Recombinant

    Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.

    Product # :

    ENZ-282

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    Description

    Glycogen Phosphorylase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain. The Human GPBB mature chain: 2 - 843 aa; that is a total of 842 aa having a molecular mass of 96695.96 Dalton. The theoretical pI is 6.40.The GPBB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 50% glycerol.

    Purity

    Greater than 85.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glycogen phosphorylase is one of the phosphorylaseenzymes(EC2.4.1.1). It breaks up glycogeninto glucosesubunits. Glycogenis left with one less glucosemolecule, and the free glucosemolecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphateby the enzyme phosphoglucomutase.
      Glycogen phosphorylase can only act on linearchainsof glycogen(a 1-4 glycosidic linkage). Its work will immediately come to a halt four residues away from a 1-6 branch(which are exceedingly common in glycogen). In these situations, a debranching enzymeis necessary, which will straighten out the chain in that area. Additionally, an alpha 1-6 glucosidaseenzymeis required to break the remaining 1-6 residue that remains in the new linear chain. After all this is done, glycogen phosphorylase can continue.
      An insulinstimulated enzyme known as phosphoprotein phosphatase(PP-1) inactivates glycogen phosphorylase to prevent glycogen break up.
      GPBB - a sensitive marker for the AMI diagnosis within 4 hours after the onset of chest pain. It has also been shown that GPBB is increased in a considerable proportion of AMI patients within 2-3 hours from chest pain onset. GPBB is increased early in patients with unstable angina. GPBB can also be a sensitive marker for the detection of peri-operative myocardial ischaemia and infarction in patients undergoing coronary artery bypass grafting.

    • Synonyms

      Glycogen phosphorylase brain form, EC 2.4.1.1, GPBB, MGC9213, PYGB.

    • Physical Appearance

      Sterile Filtered colourless liquid formualtion.

    • Stability

      GPBB although stable at 10°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Applications

      Immunoassays and western blot.

    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.

    Glycogen Phosphorylase Human
  • View Data Sheet

    Name :

    Betacellulin Mouse

    Description:

    Betacellulin Mouse Recombinant

    Betacellulin, Probetacellulin.

    Product # :

    CYT-131

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    Description

    BTC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids and having a molecular mass of 9.0kDa. The BTC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×108 IU/mg.

    Citations

    More Info

    • Introduction

      BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Synonyms

      Betacellulin, Probetacellulin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 9kDa.

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

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

      What is the Biological Activity of BETACELLULIN Protein?
      The ED50 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×108 IU/mg.

      What is the amino acid sequence of BETACELLULIN Protein?
      DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY

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

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

    Btc Mouse
  • View Data Sheet

    Name :

    IDNK E.Coli

    Description:

    Thermosensitive Gluconokinase E.Coli Recombinant

    Thermosensitive gluconokinase, Gluconate kinase 1, idnK.

    Product # :

    PKA-060

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    Description

    IDNK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187 a.a) and having a molecular mass of 23.4kDa. IDNK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thermosensitive Gluconokinase, also known as IDNK is a 187 a.a protein which is a member of the gluconokinase gntK/gntV family. IDNK catalyzes theconversion of ATP and D-gluconate to ADP and 6-phospho-D-gluconate. In addition, IDNK is considered to take part in gender determination, deletion of the distal portion of 9p is able to lead to a development of male to female sex reversal, the phenotype of a female with a male X, Y genotype.

    • Synonyms

      Thermosensitive gluconokinase, Gluconate kinase 1, idnK.

    • 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 MGSMAGESFI LMGVSGSGKT LIGSKVAALL SAKFIDGDDL HPAKNIDKMS QGIPLSDEDR LPWLERLNDA SYSLYKKNET GFIVCSSLKK QYRDILRKGS PHVHFLWLDG DYETILARMQ RRAGHFMPVA LLKSQFEALE RPQADEQDIV RIDINHDIAN VTEQCRQAVL AIRQNRICAK EGSASDQRCE.

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    Idnk Ecoli
  • View Data Sheet

    Name :

    ATG3 Human

    Description:

    Autophagy Related 3 Human Recombinant

    APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.

    Product # :

    PRO-1987

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    Description

    ATG3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314 a.a) and having a molecular mass of 38.3kDa. ATG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ATG3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.

    • Synonyms

      APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.

    • 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 MGSMQNVINT VKGKALEVAE YLTPVLKESK FKETGVITPE EFVAAGDHLV HHCPTWQWAT GEELKVKAYL PTGKQFLVTK NVPCYKRCKQ MEYSDELEAI IEEDDGDGGW VDTYHNTGIT GITEAVKEIT LENKDNIRLQ DCSALCEEEE DEDEGEAADM EEYEESGLLE TDEATLDTRK IVEACKAKTD AGGEDAILQT RTYDLYITYD KYYQTPRLWL FGYDEQRQPL TVEHMYEDIS QDHVKKTVTI ENHPHLPPPP MCSVHPCRHA EVMKKIIETV AEGGGELGVH MYLLIFLKFV QAVIPTIEYD YTRHFTM.

    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.

    Atg3 Human
  • View Data Sheet

    Name :

    RGS10 Human

    Description:

    Regulator of G-Protein Signaling 10 Human Recombinant

    Regulator Of G-Protein Signaling 10, RGS10.

    Product # :

    PRO-890

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    Description

    RGS10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (1-181) and having a molecular mass of 23.7 kDa.The RGS10 is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RGS10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RGS10 is a member of the RGS family that regulate molecules which perform as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins can disengage G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. The nucleus localized RGS10 is associates specifically with the activated forms of the two related G-protein subunits, G-alphai3 and G-alphaz but is unable to cooperate with the structurally and functionally distinct G-alpha subunits.

    • Synonyms

      Regulator Of G-Protein Signaling 10, RGS10.

    • 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 MGSHMFNRAV SRLSRKRPPS DIHDSDGSSS SSHQSLKSTA KWAASLENLL EDPEGVKRFR EFLKKEFSEE NVLFWLACED FKKMQDKTQM QEKAKEIYMT FLSSKASSQV NVEGQSRLNE KILEEPHPLM FQKLQDQIFN LMKYDSYSRF LKSDLFLKHK RTEEEEEDLP DAQTAAKRAS RIYNT

    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.

    Rgs10 Human
  • View Data Sheet

    Name :

    SELPLG Human

    Description:

    Selectin P Ligand Human Recombinant

    Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.

    Product # :

    PRO-2714

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    Description

    SELPLG Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 496 amino acids (42-295 a.a) and having a molecular mass of 53.4kDa.SELPLG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The SELPLG solution (1mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SELPLG glycoprotein functions as a high affinity counter-receptor for the cell adhesion selectin molecules (P, E and L) located in stimulated T lymphocytes and myeloid cells. SELPLG binds leukocytes to activated platelets or endothelia expressing selectins, a vital role in leukocyte trafficking throughout inflammation. In order to have a high-affinity binding activity SELPLG needs two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans. Polymorphisms and abnormal expression of SELPLG are linked to defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.

    • Synonyms

      Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.

    • 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

      DGSQATEYEY LDYDFLPETE PPEMLRNSTD TTPLTGPGTP ESTTVEPAAR RSTGLDAGGA VTELTTELAN MGNLSTDSAA MEIQTTQPAA TEAQTTPLAA TEAQTTRLTA TEAQTTPLAA TEAQTTPPAA TEAQTTQPTG LEAQTTAPAA MEAQTTAPAA MEAQTTPPAA MEAQTTQTTA MEAQTTAPEA TEAQTTQPTA TEAQTTPLAA MEALSTEPSA TEALSMEPTT KRGLFIPFSV SSVTHKGIPM AASNLSVLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK 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.

    Cd162 Human
  • View Data Sheet

    Name :

    TRH Human

    Description:

    Thyrotropin Releasing Hormone Human

    Thyroliberin, TRH, MGC125964, MGC125965, Protirelin, TRF.

    Product # :

    HOR-264

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    Description

    Thyrotropin Releasing Hormone Human C16H22N6O4 has a molecular mass of 362.4 Dalton.The TRH is purified by proprietary chromatographic techniques.

    Formulation

    The TRH was lyophilized with no additives.

    Purity

    Greater than 98.2% as determined by analysis by RP-HPLC.

    Citations

    More Info

    • Introduction

      Thyrotropin-releasing hormone (TRH), also called thyrotropin-releasing factor (TRF), thyroliberin or protirelin, is a tripeptide hormonethat stimulates the release of thyroid-stimulating hormoneand prolactinby the anterior pituitary.
      TRH is produced by the hypothalamus, near the paraventricular nucleus.
      It travels across the median eminenceto the pituitary via the hypophyseal portal system. It is released from cells called thyrotropes.
      In addition to the brain, TRH can also be detected in other areas of the body including the gastrointestinal systemand pancreatic islets.
      Protirelin stimulates the secretion of pituitary thyroid stimulating hormone from the anterior pituitary and has been shown that protirelin increases secretion of prolactin. Protirelin is identified as 5-oxo-L-prolyl-L-histidyl-L-proline amide. It is a synthetic tripeptide that is believed to be structurally identical to the naturally-occurring thyrotropin-releasing hormone produced by the hypothalamus.

    • Synonyms

      Thyroliberin, TRH, MGC125964, MGC125965, Protirelin, TRF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Pyr-His-Pro-NH2.

    • Background

      What is the molecular weight/Mw of TRH HUMAN Protein?
      TRH HUMAN Protein has a total Mw of 0.36kDa.

      What is the Purity of TRH HUMAN Protein?
      TRH HUMAN Protein is >98.2% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of TRH HUMAN Protein?
      Pyr-His-Pro-NH2.

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

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


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    Trh Human
  • View Data Sheet

    Name :

    INHBC Human

    Description:

    Inhibin-Beta C Chain Human Recombinant

    Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.

    Product # :

    HOR-010

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    Description

    INHBC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (237-352) and having a molecular mass of 14.9kDa.INHBC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      INHBC, the beta C chain of inhibin, belongs to the TGF-beta superfamily. INHBC formulates heterodimers with beta A and beta B subunits. Other members of the TGF-beta superfamily are Actv's and Inhibins, hormones with contradictory roles which take part in pituitary, hypothalamic, and gonadal hormone secretion, as well as differentiation and growth of numerous cell types.

    • Synonyms

      Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.

    • 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 MGSGIDCQGG SRMCCRQEFF VDFREIGWHD WIIQPEGYAM NFCIGQCPLH IAGMPGIAAS FHTAVLNLLK ANTAAGTTGG GSCCVPTARR PLSLLYYDRD SNIVKTDIPD MVVEACGCS

    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.

    Inhbc Human
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